INTRODUCTION TO BIOCHEMISTRY

Definition
The science that is concerned with the structures, interactions, and transformations of
biological molecules. The chemistry of life
Biochemistry can be subdivided three principal areas
 Structural chemistry
 Metabolism
 The chemistry of processes and substances that store and transmit biological information
(molecular genetics)
Biochemistry and Life
The cell is the fundamental unit of life
 Prokaryotes and eukaryotes
 Eukaryotic cells
 animal cells
 plant cells (chloroplasts and cell walls)
Cells are composed of:
 Small molecules
 Macromolecules
 Organelles
Expect for water, most of the molecules found in the cell are macromolecules, can be classified
into four different categories:
 Lipids
 Carbohydrates
 Proteins
 Nucleic acids
 Lipids are primarily hydrocarbon structures

 Carbohydrates, like lipids, contain a carbon backbone, but they

also contain many polar hydroxyl (-OH) groups and therefore
very soluble in water.
 Proteins are the most complex macromolecules in the cell.
 They are composed of linear polymers called polypeptides, which contain amino acids
connected by peptide bonds
Each amino acid contains a central carbon atom attached to four substituents
o A carboxyl group
o An amino group
o A hydrogen atom
o An R group

Nucleic acids are the large macromolecules in the cells.

They are very long linear polymers, called polynucleotides, composed of nucleotides
A nucleotide contains:
 A five-carbon sugar molecules
 One or more phosphate groups
 A nitrogenous base
 DNA: A, T, G, C
 RNA: A, U, G,C
DNA Contain Four Bases RNA

Watson-Crick base pairs

The Double Helix

Biochemical Energy
 All cellular functions re quire energy.
 The most-important chemical form of energy in most cells is ATP, adenosine 5’-
triphosphate.
 ATP ADP + Pi
 Most ATP synthesis occurs in chloroplasts and mitochondria
ADT and ATP Structures

Energy Transfer
 CARBOHYDRATES
Occurrences
Carbohydrates are the most abundant organic compounds in the plant world. They act as
storehouses of chemical energy (glucose, starch, glycogen); are the components of supportive
structures in plants (cellulose), crustacean shells (chitin) and connective tissues in animals
(acidic polysaccharides) and are essential components of nucleic acids (D-ribose and 2-deoxy-
D-ribose). Carbohydrates make up about three fourths of the dry weight of plants.
The Nature of Carbohydrates
Carbohydrates are compounds of great importance in both the biological and commercial world
They are used as a source of energy in all organisms and as structural materials in membranes,
cell walls and the exoskeletons of many arthropods. Hydrates of carbon. All carbohydrates
contain the elements carbon (C), hydrogen (H) and oxygen (O) with the hydrogen and oxygen
being present in a 2 : 1 ratio
Carbohydrates are usually defined as
Polyhydroxy aldehydes or ketones, or substances that hydrolyze to yield polyhydroxy
aldehydes or ketones”. (0r) Aldehyde or Ketone derivatives of polyhydroxy alcohols
Carbohydrates are aldehyde or ketone compounds with multiple hydroxyl groups
General molecular formula Cn (H2O)n
The term ―carbohydrate comes from the observation that when you heat sugars, you get
carbon and water (hence, hydrate of carbon).
Functions of carbohydrates
Main sources of ENERGY in body (4kcal/g)
– RBCs and Brain cells have an absolute requirement of carbohydrates
- Storage form of energy (starch and glycogen)
- Excess carbohydrate is converted to fat.
- Glycoproteins and glycolipids are components of cell membranes and receptors.
- Structural basis of many organisms.e.g. Cellulose in plants,
- exoskeleton of insects, cell wall of microbes,
- Mucopolysaccharides and ground substance in higher organisms.
MONOSACCHARIDES
Def : They are the simplest carbohydrate unites which cannot be hydrolysed to a simpler form
They are classified into a) simple monosaccharides b) derived monosaccharides
Simple monosaccharides sub classified according to
1-The number of carbon atoms present in their molecule and,
2- The type of carbonyl group they contain.
Derived monosaccharides include the derivatives of simple monosaccharides such as
oxidation products, reduction products, substitution products and esters
2.‐ According to the number of carbon atoms (n):
If sugar contains
3 carbons → it's called triose, 4c→ tetroses 5c→ pentose 6c→ hexose 7c→ heptoses

3- By combining the two methods, we find that

3c-Aldotriose ketotriose
4c-Aldotetrose Ketotetrose
5c-Aldopentise Ketppentose
6c-Aldohexose Ketohexose
Three Carbon Four Carbon
GLUCOSE
MONOSACCHARIDE STRUCTURES
The simplest monosaccharide that possesses a hydroxyl group and a carbonyl group with an
asymmetric carbon atom is the aldotriose -glyceraldehyde.( Reference carbohydrate) (A
carbon is said to be asymmetric if four different groups or atoms are attached to it. The carbon
is also called as a chiral center). Glyceraldehyde is considered as a reference compound and it
exists in two optically active forms, D and L. A chiral object cannot be superimposed on its
mirror image. A chiral carbon (Asymmetric carbon) is one that has four different groups
attached to it.

1. The straight – chain (open chain) structural formula

Aldohexose- an account for some of the properties of glucose, but cannot explain some
Reaction
D-glucose

2. Cyclic structure
When an aldehyde or a ketone group is present in a molecule that also possesses hydroxyl
groups, an intramolecular arrangement may occur to form a hemiacetal or a hemiketal,
respectively. This intramolecular hemiacetal or hemiketal is the basis for the cyclic
structure of the sugars .Hence, Haworth (an English chemist) proposed a cyclic
hemiacetal structure that accounts completely for its chemical properties
Hemiacetals or Hemiketals

An aldehyde or ketone can react with an alcohol in a 1:1 ratio to yield a hemiacetal
or hemiketal, respectively, creating a new chiral center at the carbonyl carbon
Two types of ring structures are possible, the five-membered furanose and the six membered
pyranose ring if the carbonyl group interact with hydroxyl group. These names are derived
from the parent compounds 'furan' and 'pyran'. The most common ring structure for
aldohexoses is the pyranose ring structure that involves the first carbonyl carbon and the
hydroxyl group attached to the fifth carbon. The furanose ring structure is formed by interaction
of carbonyl carbon with the hydroxyl group attached to the fourth carbon. This furanose form
is less stable than the pyranose structure and is not very common among Aldohexose

Six membered pyranose ring Five membered furanose ring

Isomerism
Isomers are different compounds that have the same molecular formula. Different compounds
means that they have different physical properties (melting point, boiling point etc.). They may
also have very different chemical properties depending on the type of isomerism present. It was
coined by J.J. Berzelius for different compounds with same molecular formula

Structural isomers, in which the atoms are joined in a different order, so that they have
different structural formulae
Types of structural isomerism
Chain isomerism
These isomers arise because of the possibility of branching in carbon chains. For example,
there are two isomers of butane, C4H10. In one of them, the carbon atoms lie in a "straight
chain" whereas in the other the chain is branched.

Position isomerism
In position isomerism, the basic carbon skeleton remains unchanged, but important groups are
moved around on that skeleton.
Functional Isomers
D-glucose and D-fructose differ in the position of carbonyl group (aldehyde and ketone group).
These two compounds are functional isomer

Stereoisomerism or constitutional isomers

Another type of isomerism exhibited by compounds possessing asymmetric carbon atom like
monosaccharides, is stereoisomerism. These stereoisomers differ in the spatial arrangement of
atoms or groups. There are two types of stereoisomerisms - geometrical and optical isomerism.

Geometric Isomerism
Geometric isomers (also called cis/trans isomers) are a type of stereoisomer resulting from a
double bond or a ring structure. The double bond or ring in the structure means that not all
bonds are free to rotate, giving rise to geometric isomers whose shapes cannot interconvert.
Geometrical isomerism is not noticed among carbohydrates.
Optical isomerism
Optical isomers differ in the arrangement of atoms around an
asymmetric carbon atom. The number of possible optical
isomers can be calculated using the formula 2n where
n=number of asymmetric carbon atoms. For example,
glucose contains four asymmetric carbon atoms and the
possible optical isomers of glucose are 24 = 16. Optical
isomers are named like this because of their effect on plane
polarised light.

Enantiomers
Enantiomers are non- superimposable mirror images of each other. They differ in the ability to
rotate the plane polarized light .A solution of one enantiomer rotates the plane of such light to
the right, and a solution of the other to the left. D-glucose and L-glucose are examples of
enantiomers.
Epimers
Epimers are monosaccharides differing in configuration around a single carbon atom other than
the carbonyl carbon. e.g. Mannose and glucose are epimers with respect to carbon 2. Galactose
and glucose are epimers with respect to carbon 4.

D-Galactose is an epimer of D-glucose because the two sugars differ only in the configuration
at C-4. D-Mannose is an epimer of D-glucose because the two sugars differ only in the
configuration at C-2.
Anomers
When a molecule such as glucose converts to a cyclic form, it generates a new chiral centre
at C-1.
The carbon atom that generates the new chiral centre (C-1) is called the anomeric carbon.
Anomers are special cases — they are epimers that differ in configuration only at the anomeric
carbon
For example, α-D-glucose and β-D-glucose are Anomers

The α form has the anomeric OH group at C-1 on the

opposite side of the ring from the CH2OH group at C-5.
The β form has the anomeric OH group on the same side as
the CH2OH

Diastereomers
Diastereomers are stereoisomers that are not mirror images of each other. D-glucose, D-
mannose, D-galactose and other members of aldohexose are diastereoisomers.
Stereoisomers with two or more stereocenters can be diastereomers. It is sometimes difficult
to determine whether or not two molecules are diastereomers.
Optical activity
Molecules that are chiral can rotate the plane of polarized light. The property of rotating the
plane of polarized light is called optical activity, A ray of ordinary light vibrates in all directions
at right angles to the direction in which the ray is travelling. When this light is passed through
a Nicol prism, the emerged light vibrates in only one direction and such light is called as a
'plane polarized light
When a beam of plane polarized light is passed through a sugar solution, that is optically active,
the plane-polarized light will be rotated either to the right (clockwise) or to the left
(anticlockwise). When the plane polarized light is rotated to the right, the compound is
dextrorotatory and is written as (+). • If the plane polarized light is rotated to the left, the
compound is levorotatory (-)
Mutarotation
Mutarotation is a term given to the change in the observed optical rotation of a substance with
time. Glucose, for example, can be obtained in either its a or b-pyranose form. The two forms
have different physical properties such as melting point and optical rotation. When either form
is dissolved in water, its initial rotation changes with time. Eventually both solutions have the
same rotation. In Glucose solution, 2/3 of sugar exist as β form, & 1/3 as α form. Inter
conversion of α & β forms is called MUTA ROTATION
Mutarotation of D-Glucose

β-D-Glucopyranose α-D-Glucopyranose
Initial: []D +18.7° Initial: []D +112.2°
Oligosaccharides
These consist of 2 and up to 10 molecules of simple sugars and are hydrolysable. They are sub
classified into di-, tri- and tetrasaccharides etc…, according to the number of molecules of
simple sugars they yield on hydrolysis
Disaccharides
Disaccharides are sugars composed of two monosaccharides covalently bonded together by a
glycosidic linkage. The most abundant disaccharides are sucrose, lactose and maltose.
The disaccharides can be classified into homo disaccharides and hetero disaccharides
A) Homo disaccharides: are formed of the same monosaccharide units maltose, isomaltose,
cellobiose and trehalose
B) Hetero disaccharides: are formed of different monosaccharide and include: sucrose, lactose

 Maltose, also known as malt sugar, is formed from two glucose molecules
 Lactose, or milk sugar, is a disaccharide formed when the monosaccharides glucose and
galactose are joined
 Sucrose is common household sugar and is formed when the monosaccharides glucose and
fructose bond

MALTOSE = GLUCOSE + GLUCOSE

LACTOSE = GLUCOSE + GALACTOSE
SUCROSE = GLUCOSE + FRUCTOSE

Lactose:
It is formed of β-galactose and α-glucose linked by β-1,4-glucosidic linkage
Contain free anomeric carbon so reducing sugar
Lactose is a reducing disaccharide found only in milk.
It is made up of galactose at the non-reducing end and glucose at the reducing end.

Maltose (malt sugar):

Maltose is a disaccharide made up of two glucose residue joined by a glycosidic linkage
between C-1 of one glucose residue and C-4 of the other. The anomeric carbon atom of the
second glucose is free and therefore maltose is a reducing sugar.
Sucrose, a sugar of commercial importance, is widely distributed in higher plants. Sugarcane
and sugar beet are the sole commercial sources. It is made up of glucose and fructose. The
anomeric carbon atom of glucose (C-1) and fructose (C-2) are involved in linkage and is
therefore a non-reducing disaccharide. Sucrose is a major intermediate product of
photosynthesis and it is the principal form in which sugar is transported from the leaves to other
portions of plants via their vascular systems.
Invert sugar
The hydrolysis of sucrose when followed Polarimetrically the optical rotation changes from
positive (dextro-) to negative (levo-). The dextrorotatory sucrose on hydrolysis yield
levorotatory mixture of glucose and fructose. The levorotaion is due to the presence of fructose
which is by itself more levorotatory (-92) than dextrorototary glucose (+52.2). This
phenomenon is called inversion and the mixture of glucose and fructose is called invert sugar.
This reaction is catalysed by the enzyme invertase. Invert sugar is sweeter than sucrose. Honey
contains plenty of invert sugar and therefore is very sweet.
Polysaccharides
Polysaccharides are large polymers of the monosaccharides. Unlike monosaccharides and
disaccharides, polysaccharides are either insoluble or form colloidal suspensions. The
polysaccharides found in nature either serve a structural function (structural polysaccharides)
or play a role as a stored form of energy (storage polysaccharides).
Storage polysaccharides (digestible polysaccharides)
The principal storage polysaccharides are STARCH AND GLYCOGEN. Starch is a polymer
of alpha glucose and is, in fact, a mixture of two different polysaccharides – AMYLOSE AND
AMYLOPECTIN
Starch
The principal food-reserve polysaccharide in the plant kingdom is starch. It forms the major
source of carbohydrate in the human diet. Starch has been found in some protozoa, bacteria
and algae. But the major source is plants where it occurs in the seeds, fruits, leaves, tubers and
bulbs in varying amount from a few percent to over 74%. Starch is an alpha-glucan that has
structurally distinct components called amylose and amylopectin. A third component referred
as the intermediate fraction has also been identified in some starches. Starch molecules are
organized into quasicrystalline macromolecular aggregates called granules. The shape of the
granules are characteristics of the source of the starch. The two components, amylose and
amylopectin, vary in amount among the different sources from less than 2% of amylose in
waxy rice or waxy maize to about 80% amylose in amylomaize. The majority of starches
contain 15 to 35% of amylose.

AMYLOSE

Amylose is formed by a series of condensation reactions that bond alpha glucose molecules
together into a long chain forming many glycosidic bonds
Amylose is made up of α D-glucose units linked mostly in a linear way by α 1- 4 linkages
It has a molecular weight of 150,000 to 1,000,000 depending on its biological origin. It consists
of a mixture of linear molecules with limited, long-chain branching involving α 1-6 Linkages.
Amylose gives a characteristic blue color with iodine due to the ability of the iodine to occupy
a position in the interior of a helical coil of glucose units
Amylopectin
Amylopectin consists of a straight chain of alpha glucose units with branch points occurring at
approximately every twelth glucose unit along the straight chain. The branch point’s form when
carbon 6 of a glucose molecule in the straight chain forms a glycosidic bond with carbon 1 of
a glucose molecule positioned above the chain.

This highly branched amylopectin molecule is wrapped around the amylose to make up the
final starch molecule. This large insoluble molecule with branch points that allow for easy
access for enzymes when breaking down the molecule, makes starch an ideal food storage
compound. Amylopectin is a branched, water-insoluble polymer comprised of thousands of D-
glucose residues. It contains 94-96% α 1-4 and 4-6% α 1-6 linkages. The molecular weight of
amylopectin is in the order of 107 - 108. The amylopectin molecule is 100 - 150 A in diameter
and 1200-4000 A long.
Inulin
Inulin is a non-digestible fructosyl oligosaccharide found naturally in more than 36000 types
of plants. It is a storage polysaccharide found in onion, garlic, chicory, artichoke, asparagus,
banana, wheat and rye. It consists of mainly, if not exclusively, of - 2->1 fructosyl-fructose
links. A starting glucose moiety can be present, but is not necessary. Inulin is a soluble fibre
that helps maintain normal bowel function, decreases constipation, lowers cholesterol and
triglycerides. It is used for fat replacement and fibre enrichment in processed foods
STRUCTURAL POYSACCHARIDES (indigestible polysaccharides)
 Cellulose is the most abundant organic substance found in nature. It is the principal constituent
of cell walls in higher plants. It occurs in almost pure form (98%) in cotton fibres and to a
lesser extent in flax (80%), jute (60-70%), wood (40-50%) and cereal straws (30-43%). It is
linear, unbranched homoglycan of 10,000 to 15,000 D-glucose units joined by β 1- 4 linkages
The structure of cellulose can be represented as a series of glucopyranose rings in the chair
conformation.
Pectin- It is in fruits of many plants. The constituent monosaccharide is ά-D – galactouronic
acid
Chitin- Most abundant in nature after cellulose, found in fungi and anthropods. The constituent
monosaccharides are N- Acetyl- D- glucosamine. It is non- reducing sugar
Properties of carbohydrate
Monosaccharides
1. Reaction with alcohol – The Glycosidic OH group of mutarotating sugars reacts with
alcohol to form ά and β glycosides or acetals. Thus glucose form glucosides and fructose
from fructosides
2. Reaction with acetic anhydride- The Glycosidic and alcoholic OH group of
monosaccharides and disaccharides react with acetylating agents to form acetate derivatives
called esters
3. Oxidation with acids- Only the aldehydes group of sugar is oxidized to produce
monocarboxylic acid with bromine water, while with nitric acid both aldoses and ketoses
react to form dicarboxylic acid
4. Oxidation with metal hydroxides- Metal hydroxides like copper hydroxide oxidize free
aldehydes or keto group of mutarotating monosaccharides and at the same time they
themselves reduce to free metal
Reducing sugar + Cu2+ oxidized sugar + 2 Cu+
2Cu+ + 2OH- 2Cu.OH Cu2O + H2O
Yellow Red
This sugar is active ingredient in Fehling’s, Benedict’s and Barfoed’s reagent
5. Reduction- The sugars undergo reduction with sodium amalagam to form corresponding
alcohols. Glucose yields sorbitol and fructose yields mixture of sorbitol and mannitol. With
strong acids, it undergo reduction to form levulinic acid.
6. Reaction with hydrogen cyanide- (Kilani synthesis). It forms cyanohydrins
7. Reaction with alanine– The aldehydes group of carbohydrate condenses with the amino
group of alanine to form Schiff’s base.
8. Reaction with Phenyl hydrazine – reaction of monosaccharides with phenyl hydrazine
yields osazone
9. Fermentation- Monosaccharides are readily fermented by yeast to form alcohol
Disaccharides
1. Sucrose- it is dextrorotatory, a non- reducing sugar, does not exhibit mutarotation, does
not form osazone and fermentable
2. Lactose- It is dextrorotatory, a reducing sugar, exhibit mutarotation, form osazone and
non-fermentable
3. Maltose- It is dextrorotatory, a reducing sugar, exhibit mutarotation, form osazone and
fermentable
4. Cellobiose- It is a reducing sugar, exhibit mutarotation
Polysaccharides
1. Starch- It is made up of amylose and amylopectin. Amylose gives blue colour with iodine,
amylopectin gives purple with iodine and dextrorotatory,
2. Glycogen- It is a non-reducing sugar, gives red colour with iodine, white powder, fairly
stable in hot alkali
3. Cellulose- It gives no colour with iodine, fibrous, tough, white solid
4. Inulin- It is a non-reducing sugar, gives no colour with iodine
5) Chitin- It is non-reducing sugar
Physical Properties of Carbohydrates
a) Monosaccharides
1) Crystaline compound
2) Sweet to taste
3) Soluble in water
4) Need to be digested before absorbed in blood stream
b) Disaccharides
1) Crystaline compound
2) Sweet to taste
3) Soluble in water
4) Need to be digested before absorbed in blood stream
c) Polysaccharides
1) Amorphous compound
2) Not soluble in water
3) No sweet taste
4) Form colloidal suspension and need to be digested before absorbed
Reducing property of sugars
Sugars are classified as either reducing or non-reducing depending upon the presence of
potentially free aldehyde or keto groups. The reducing property is mainly due to the ability of
these sugars to reduce metal ions such as copper or silver to form insoluble cuprous oxide,
under alkaline condition

Any carbohydrate which is capable of being oxidized and causes the reduction of other
substances without having to be hydrolyzed first is known as reducing sugar. The aldehyde
group of aldoses is oxidized to carboxylic acid. This reducing property is the basis for
qualitative (Fehling's, Benedict's, Barfoed's tests) and quantitative reactions. All
monosaccharides are reducing. In the case of oligosaccharides, if the molecule possesses a free
aldehyde or ketone group it belongs to reducing sugar (maltose and lactose). The carbohydrates
which are unable to be oxidized and do not reduce other substances are known as non- reducing
sugars. If the reducing groups are involved in the formation of glycosodic linkage. the sugar
belongs to the non- reducing group (trehalose, sucrose, raffinose and stachyose). The reason
that sucrose is a non-reducing sugar is that it has no free aldehyde or keto group. Additionally,
its anomeric carbon is not free and can’t easily open up its structure to react with other
molecules.
Reaction with acids
Monosaccharides are generally stable to hot dilute mineral acids though ketoses are appreciably
decomposed by prolonged action. Heating a solution of hexoses in a strong non-oxidising
acidic conditions, hydroxyl methyl furfural is formed. The hydroxymethyl furfural from hexose
is usually oxidized further to other products .When phenolic compounds such as resorcinol,
naphthol or anthrone are added, mixture of coloured compounds are formed. The Molisch test
used for detecting carbohydrate in solution is based on this principle. When conc.H2SO4 is
added slowly to a carbohydrate solution containing naphthol, a pink color is produced at the
juncture
Reaction with alkali
Dilute alkali
Sugars in weak alkaline solutions undergo isomerization to form 1,2-enediols followed by the
formation of a mixture of sugars.
Strong alkali
Under strong alkaline conditions sugar undergo caramelization reactions
 CARBOHYDRATE
FILL UP THE BLANKS
1. Starch is classified under ________
2. Isomerism is a common property due to the presence of _______ and structural
arrangement
3. Cellulose is a polysaccharide made up of glucose and the linkages are ____
4. Plant gums are ___
5. Starch is a polymer of ______
6. Amylopectin has branched chained ______ units
7. ___ is the sugar present in milk
8. The storage polysaccharides of animal tissue is ________
9. Isomerism and optical activity property of carbohydrate is due to ______
10. _____ is a non-reducing sugar
11. The change in the optical activity of sugar solution is known as _____
12. The carbon atom to which four different atoms or groups are attached is called _____
carbon atom
13. The plant gums are the Heteropolysaccharides containing several units of ______
14. Gluconic acid is a _____ acid
15. The group that confers sweet taste to glucose is ______
16. Freshly prepared glucose solution has a specific rotation of _____
17. The sugar used for silvering the mirror is ______
18. Fructose is the hydrolytic product of ________
19. _______ is a non-reducing disaccharide sugar
20. The reagent used to form osazone with sugars is __
21. Carbohydrates consists of ______ elements in the ratio 1:2:1
22. The general formula of monosaccharide is _____
23. Galactose is ___ type of monosaccharide
24. Oligosaccharides on hydrolysis give _____ number of monosaccharides
25. The monosaccharide glucose has got __ functional group
26. The monosaccharide having keto group is known as _____
27 The isomers having similar molecular formula but different structural formula is called
as ___
28 Stereoisomers are grouped into ______ and _________
29 Number of optical isomers of the compound depends on number of ________
30 In a carbohydrate, If H is in the left and OH is on the right, It is designated by_____
31 Number of optical isomers present in glucose is ______
32 If the compound causes rotation of the polarized light to the left, it is said to be ______
33 In a mixture where optical activity is zero, such a mixture is called as _____
34 Mutarotation is undergone by ______ sugars only
35 Pyranose rings has got ______ type of linkage by oxygen atom
36 Hexoses are formed by hydrolysis of _______
37 Glucose on reaction with bromine water yields _____
38 Fructose undergo reduction in the presence of H catalyst to form ________
39 Reaction between glucose and alanine results in the formation of ______
40 Monosaccharide on reduction with phenyl hydrazine results in the formation of ____
41 Glucose is converted to ethyl alcohol on fermentation by the action of _____
42 Any carbohydrate which is capable of being oxidized and causes the reduction of other
substances is called as _______
43 Test for identifying the reducing property of sugar is found by________
44 ____ is an example of reducing disaccharide sugar
45 Sucrose on hydrolysis yields ____ and _____
46 ____ enzyme is involved in the hydrolysis of sucrose
47 Glucose and glucose combination results in the formation of ______
48 Lactose is composed of one molecules of ____ and ___
49 Lactose is also called as _______
50 Amylose and Amylopectin are components of _____-
51 Glycogen is a _____
52 Starch on reaction with iodine gives_____ colour
53 Reducing centre in aldose sugar lies at ______
54 Reducing sugar in ketose sugar lies at _______
55 Fruit sugar is chemically called as _______
56 _____ is an example of homopolysachharides
57 Glucose carries ______ asymmetric carbon atoms
58 Sucrose has specific rotation of _____
59 Carbohydrates are polyhydroxy ______-
60 Cellulose is a polysaccharide made of glucose and the linkages are _______
61 Hydrolysis of sucrose by the invertase yields ___ and ____
62 Compounds possessing a free aldehydes or ketone group and two or more hydroxyl
groups are ______
63 The shift or change in the optical activity of a particular carbohydrate is known as ____
64 Inulin is polymer of ______ occurring in composite plant
65 Monosaccharides having six carbon atoms are called as ___
66 Compound containing ά 1-6 linkage with 2000 to 3000 glucose units is called as ___
67 General formula for carbohydrate is ______
68 An example of triose is ___
69 The cane sugar is made up of ____- and ______
70 ____is an aldopentose while _____ is a ketohexose sugar
71 The milk sugar______ is made up of glucose and _____
72 Invert sugar is also called as _______
73 Glucose and galactose are the constituents of _______
74 Starch is made up of ____ sub units
75 ___is an optically inactive triose
76 The ability of sugars to form esters indicate the presence of ____group in their molecule
77 _______ reaction is used to distinguish between aldose and ketoses
78 Fructose on reduction with sodium amalgam yields mixture of ______
79 ____ is an isomer of mannose
80 Molisch test with sugar develops ___ colour
81 Sucrose is a________ sugar
82 Isomerit compounds have _________ molecular formula
83 Starch contains __________ units
84 During germination starch is converted to ________
85 Maltose is a disaccharide formed by the linkage of ___________
86 Pentosans have the molecular formula ______
87 Starch on hydrolysis yields _______
88 Fructose is a______ sugar (other than fruit)
89 Optical isomerism is caused by________
90 Non- reducing disaccharides is________
91 Cellulose is a polysaccharide containing a _________
92 Aldose containing the group _______
93 The number of molecules of water eliminated when the two molecules of
monosaccharide react is______
94 Disaccharide that is formed by the union of two of the same monosaccharide is_____
95 The fraction of starch that give blue colour with iodine is _______
96 The sugar units derived on the hydrolysis of starch is_______
97 Ribose is a._______ sugar
98 The animal sugar is called as _________
99 Amylopectin content in starch is_________
100 The structural polysaccharide is_______
101 Reducing lactose sugar has got ___ type linkage
102 Sucrose is commercially obtained from_______
103 Invertase is an enzyme which hydrolyses________
104 Xylose is a carbohydrate occurs in______
105 The shift or change in the optical activity of particular carbohydrates is called as_____
106 Levulose is commonly named as_________
107 Dextrin is one of the hydrolysed products of ______
108 Fructose is a ________
109 An example of homopolysachharides is _______
110 Amylopectin contains _________
111 Glycosidic bond is formed between ________
112 ______ Biomolecules simply refers as “Staff of life”
113 In carbohydrates a special functional groups present ______ and _____
114 Simplest carbohydrate is _______
115 Examples of Epimers is _______
116 _________ will answer Molisch test
117 The red precipitate formed when glucose is heated with “Benedict’s reagent” is…
118 _______ Sugar exhibits inversion of optical rotation on heating with dilute acid ….
119 The end product of hydrolysis of “Starch” by amylase is …
120 Example for “Fructosan” is ……..
121 The reagent used for distinguishing a reducing monosaccharide from a reducing
disaccharide is …
122 Fructose and Glucose can be distinguished by ….
123 Concept of tetrahedral carbon atom” are first introduces by …
124 The general formula for carbohydrate is _________
125 _______ is an example of aldotriose
126 The glycosidic linkage between glucose in maltose is _____
127 A ketose pentose will have _______ stereoisomers
128 ____________ is an example epimers
129 Hydrolysis of glycoside bond involves _________of glycosidic bonds
130 Most complex also most abundant carbohydrates that are found in nature are ________
131 The most common monomer of carbohydrate is _______
132 Carbohydrates occur naturally in _____ form
133 Different ways to represent a carbohydrate molecule are straight chain, Fischer and
_______
134 _________ representation of a carbohydrate can a hemiketal or hemiacetal be observed
135 Cell wall in plants is made of _________ carbohydrate
136 _________ test is used for testing reducing sugar
137 D & L Designation can be used to _______ molecules
138 A straight chain hexose sugar forms ____ type of ring
139 Casein contained in milk is a/an _________
140 Complete hydrolysis of cellulose gives _______
141 The change in optical rotation of freshly prepared solution of glucose is known as ____
142 _____ compounds, when heated at 483k turns to caramel
143 Methyl α‐D glucoside and methyl –β‐D glucoside are________
144 Number of chiral carbon atoms in β‐D‐ (+) ‐glucose is _______
145 _______ monosaccharides is present as five membered cyclic structure (furanose
structure)
146 A polymer of fructose is ______
147 _________ test is undertaken to differentiate between Glucose and Fructose
148 A 0.5 mol dm3 solution of sucrose was heated at 80 °C for 5 min with Benedict’s reagent.
The resulting colour is _____
149 The relationship between glucose, mannose and galactose is ________
150 All carbohydrate foods are composed of the __________ elements
 Answers
Sl.No Answer Sl.No Answer
1 Storage polysaccharide 34 Reducing
2 Asymmetric carbon atom 35 C1-C5
3 1-4 Glycosidic linkage 36 Cane sugar
4 Natural polysaccharide 37 Gluconic acid
5 Glucose 38 Sorbitol and Mannitol
6 1-6 Glycosidic linkage 39 Schiff’s base
7 Lactose 40 Osazone
8 Glycogen 41 Yeasts
9 Asymmetric carbon atom 42 Reducing sugar
10 Sucrose 43 Fehling’s solution
11 Mutarotation) 44 Lactose/maltose
12 Asymmetric 45 Glucose and fructose
13 Glucose 46 Invertase
14 Monobasic acid 47 Maltose
15 Aldehyde 48 Glucose and Galactose
16 + 112.2 49 Milk sugar
17 Glucose 50 Starch
18 Sucrose 51 Non-reducing sugar
19 Sucrose 52 Blue
20 Phenyl Hydrazine 53 Carbon No.1
21 C, H, O 54 Carbon No 2
22 CnH2nOn 55 Fructose
23 Hexoses 56 Starch and Cellulose
24 2 to 10 57 4
25 Aldehydes 58 + 66.50
26 Ketoses/ Fructose 59 Aldehydes or Ketones
27 Structural isomers 60 β- 1-4 Glycosidic linkage
28 Geometrical, optical 61 Glucose and Fructose
29 Asymmetric carbon atom 62 Monosaccharide
30 D- form 63 Mutarotation
31 16 64 Inulin
32 Levorotatory 65 Hexoses
33 Racemic 66 Amylopectin
Sl.No Answer Sl.No Answer
67 ( CH2O)n 100 Pectin
68 Glyceraldehyde’s 101 C1-C4
69 Glucose and Fructose 102 Sugarcane
70 Ribose, Fructose 103 Sucrose
71 Lactose and Galactose 104 Flower of plants
 72 Sucrose 105 Mutarotation
73 Lactose 106 Fructose
74 2, Amylose and Amylopectin 107 Sucrose
75 Glyceraldehydes 108 Ketohexoses
76 Alcohol 109 Cellulose
77 Mild oxidant- HOBr 110 ά – 1-4 and ά-1-6 linkage
78 Sorbitol and Mannitol 111 Two monosaccharides
79 D- Glucose 112 Carbohydrate
80 Violet 113 CHO and C=O
81 Non- reducing sugar 114 Glyceraldehyde
82 same 115 D glucose and D- mannose
D Glucose and D galactose
83 Glucose + Glucose 116 Carbohydrate
84 Maltose 117 Cuprous oxide
85 Glucose + Glucose 118 sucrose
86 (C5H8O4)n 119 Maltose
87 Dextrin 120 Inulin
88 Levose sugar 121 Barfoed’s
89 Asymmetric carbon atom 122 Seliwanoff
90 Sucrose 123 Kekulé (1862)
91 Linear chain of beta D glucose units 124 Cm(H2O)n
92 CHO 125 glyceraldehyde,
93 One 126 α(1→4)
94 Maltose 127 Eight
95 Amylose 128 Glucose and mannose
96 ά D glucose 129 breakdown
97 Pentose 130 Starch
98 Glycogen 131 glucose
99 80-85% 132 D
Sl.No Answer Sl.No Answer
133 Haworth 138 Pyranose
134 Ring 139 lactose
135 Cellulose 140 D-glucose units.
136 Fehling 141 Mutarotation
137 chiral 142 Glucose
143 Anomers 147 Seliwanoff
144 5 148 Cherry red
145 Glucose 149 Epimers
146 Inulin 150 CHO
 DEFINITION
1. Carbohydrate: Carbohydrates are chemically defined as polyhydroxy aldehydes or
ketones, their derivatives and their polymers. ( or) Aldehyde or Ketone derivatives of
polyhydroxy alcohols
2. Monosaccharides : They are the simplest carbohydrate unites which cannot be
hydrolysed to a simpler form
3. Oligosaccharides: They contain two to ten monosaccharide units joined by glycosidic
linkages that can be easily hydrolysed.
4. Polysaccharides: They are high molecular weight polymers containing more than ten
monosaccharides.
5. Chiral or Asymmetric carbon: A chiral carbon (Asymmetric carbon) is one that has
four different groups attached to it.
6. Isomers: Isomers are different compounds that have the same molecular formula
7. Structural isomers: The atoms are joined in a different order, so that they have different
structural formulae
8. Functional Isomers: Differ in the position of carbonyl group D-glucose and D-fructose
(aldehyde and ketone group). These two compounds are functional isomer
9. Stereoisomerism or constitutional isomers: These stereoisomers differ in the spatial
arrangement of atoms or groups
10. Geometric Isomerism: Geometric isomers (also called cis/trans isomers) are a type of
stereoisomer resulting from a double bond or a ring structure
11. Optical isomerism: Optical isomers differ in the arrangement of atoms around an
asymmetric carbon atom.
12. Enantiomers: Enantiomers are non- superimposable mirror images of each other. D-
glucose and L-glucose are examples of enantiomers.
13. Epimers: Epimers are monosaccharides differing in configuration around a single
carbon atom other than the carbonyl carbon. Mannose and glucose are epimers with
respect to carbon 2. Galactose and glucose are epimers with respect to carbon 4
14. Anomers: When a molecule such as glucose converts to a cyclic form, it generates a new
chiral centre at C-1. The carbon atom that generates the new chiral centre (C-1) is called
the anomeric carbon
15. Homopolysachharides: When made from a single kind of monosaccharide. Eg starch,
cellulose, inulin, glycogen, chitin
16. Heteropolysaccharides: They are made up of more than one type of monosaccharides.
Eg. Hemicellulose
17. Diastereomers: Diastereomers are stereoisomers that are not mirror images of each
other. D-glucose, D-mannose, D-galactose
18. Optical activity: Molecules that are chiral can rotate the plane of polarized light. The
property of rotating the plane of polarized light is called optical activity.
19. Mutarotation: Mutarotation is the change in the optical rotation because of the change
in the equilibrium between two anomers, when the corresponding stereocenters
interconvert. Inter conversion of α & β forms is called MUTA ROTATION
20. Maltose: Maltose, also known as malt sugar, is formed from two glucose molecules
21 Lactose : It is formed of b-galactose and a-glucose linked by b-1,4-glucosidic linkage
22 Sucrose: Sucrose is formed when glucose forms a glycosidic bond with fructose
23 Invert sugar: The dextrorotatory sucrose on hydrolysis yield levorotatory mixture of
glucose and fructose. This phenomenon is called inversion and the mixture of glucose
and fructose is called invert sugar
24 Starch: Starch is a polymer of alpha glucose and is, in fact, a mixture of two different
polysaccharides – Amylose and Amylopectin
25 Amylose: Amylose is formed by a series of condensation reactions that bond alpha
glucose molecules together into a long chain forming many glycosidic bonds
26 Amylopectin: Amylopectin consists of a straight chain of alpha glucose units with
branch points occurring at approximately every twelth glucose unit along the straight
chain
27 Cellulose: It is a polymer of beta glucose units where each glucose molecule is inverted
with respect to its neighbour
28 Reducing sugar: A reducing sugar is any sugar that is capable of acting as a reducing
agent because it has a free aldehyde group or a free ketone group
29 Non-Reducing Sugar: The carbohydrates which are unable to be oxidized and do not
reduce other substances are known as non- reducing sugars.

Write short notes on:

1) Cellulose:
It is structural polysaccharide. It is a long straight chain polysaccharide consisting of many β –
D glucose units joined together by (1, 4) Glycosidic linkages. Because it consists of only of
glucose units, it is known as glucosans or glucans. It occurs in the cell wall of plants and
molecular weight ranges from 200,000 to 2, 000,000. It is fibrous, tough, white solid, insoluble
in water, gives no colour with iodine, lack sweetness and has no nutritive value
2) Starch
It is reserve food materials of higher plants and is found in cereals, potatoes etc. It consists of
two components namely amylose and Amylopectin. Amylose is a long unbranched chain ( ά -
1-4 linkage) with 15-20% content and Amylopectin branched chain It is composed of linearly
linked alpha 1,4 linked glucose units (coiled into tubular sections) with occasional alpha 1-6
Glycosidic bonds which provide branching points. Each amylopectin molecule may contain
100,000-200,000 glucose units, and each branch is about 20 or 30 glucose units in length, so
that these molecules are bushy and nearly spherical in shape with 80-85% content in starch.
Hydrolysis of starch leads to formation of ά – D glucose units by diastase enzyme. Synthesis
of starch involves simultaneous synthesis of amylose and amylopectin. Amylose are formed
by elimination of water from Glycosidic OH group of one ά- D glucose molecule and alcoholic
OH group on carbon 4 of the adjacent glucose. Amylopectin in addition to ά -1-4 linkage like
amylose, it has many sided chain attached to basic chain by 1, 6 glucosidic linkage
3) Sucrose
It is also called as table sugar, cane sugar, beet sugar. It is mainly found in plants. It is present
in varying amounts in different parts of the plant. It is non- reducing sugar because Glycosidic
bond blocks reducing group of both monosaccharides units. On hydrolysis, it yields one
molecule of glucose and one molecule of fructose.
C12H22O11 + H2O C6H12O6 + C6H12O6
Sucrose Glucose Fructose
Hydrolysis is done by enzyme invertase or dilute acids. The glucose and fructose are produced
with a in the optical rotation from positive to negative which is called as inversion.
C12H22O11 + H2O C6H12O6 + C6H12O6
+ 66.5 + 52.5 - 92.0
Sucrose is fermented with yeast, soluble in water, slightly soluble in alcohol, ether. It is
colourless. Invert sugar is sweeter than sucrose itself.
4.) Isomerism
It was coined by J.J. Berzelius for different compounds with same molecular formula. Isomer
is formed only in the presence of asymmetric carbon atom. It is classified into structural and
Stereoisomers. Structural isomerism (Similar molecular formula with different structural
formula) has three types namely chain, functional and positional. Stereoisomers (Similar
structural and molecular formula but different spatial arrangement.) have two types namely
geometrical and optical. Number of optical isomers in a compound depends on number of
asymmetric carbon atoms. Number of optical isomers is equal to 2n where n refers to number
of asymmetric carbon atoms. When light is passed through optically active solution, it can be
rotated either left or right side. A compound rotating the plane of polarized light to the right is
called as dextrorotatory and designated as D or (+). If the compound causes rotation of the
polarized light to the left is called as levorotatory and indicated by L or (-).
5) Monosaccharides
These are simplest of carbohydrates and are known as sugars. These are the building blocks of
complex carbohydrates. These cannot be hydrolysed. These are sweet tasting, crystalline and
soluble in water. They have a potential aldehydes or keto group and hence are reducing sugars
in nature. Aldehydes group are known as aldoses or aldose sugar. Monosaccharides having
keto group are known as ketoses or keto sugar. Depending up on the number of carbon atoms,
monosaccharides are classified into triose ( Glyceraldehyde’s), tetroses ( Erythroses), pentoses(
ribose), Hexoses( glucose, fructose) and heptoses ( Sedoheptulose). Monosaccharides exhibit
gradual change in specific rotation called as Mutarotation
6) Optical activity
Optical activity takes place mainly due to the presence of asymmetric carbon atom. Optical
isomers differ from each other in the disposition of the various atoms or groups of atoms in
space around the asymmetric carbon atom. It is referred to as mirror image of each other.
Number of optical isomers in any compound depends on the number of asymmetric carbon
atoms. According to the rule of Le-bell Van’ts Hoff total number of optical isomers of a
compound will be equal to 2n where n refers to number of asymmetric carbon atoms When a
beam of light is allowed to pass through optically active solution, it can be rotated to the right
side ( Dextrorotatory- D( +)) and can be rotated to the left side( Levorotatory L ( -)). When
equal amounts of D and L type of isomers are present, the resulting mixture is optically inactive
which is called as racemic mixture. When a monosaccharide is dissolved in water, the optical
rotating power of solution gradually changes until reaches a constant value which is referred
to as Mutarotation.
7) Oxidation of hexose sugar
Monosaccharides on oxidation under proper condition form different products eg. aldoses may
form monobasic acid or dibasic saccharic acid or monobasic uronic acid
A) Production of adonic acids: Aldoses when oxidized in the presence of bromine water, al
Aldehyde group is converted into carboxyl group
CHO-(CHOH)4-CH2OH + HoBr COOH—( CHOH)4 – CH2OH + HBr
Glucose Bromine water Gluconic acid
Ketoses are not readily oxidized by bromine water
B) Saccharic acid — The aldoses and ketoses undergo oxidation in the presence of
Nitric acid to convert to carbonyl to form saccharic acid or dibasic acid. Eg. D-
glucose, D-galactose and D-mannose are converted to D-glucoric acid, D-galactosaccharic
acid and D-mannaric acid
CHO-(CHOH)4-CH2OH + HNO3 COOH- (CHOH)4—COOH
Glucose Glucoric acid
While fructose is oxidized to tartaric acid, glycolic acid and trihydroxy glutaric acid
CH2OH- C= O- (CHOH )3-CH2OH + HNO3 COOH-(CHOH)3-COOH
Fructose Trihydroxy glutaric acid
COOH- (CHOH)2 –COOH
Tartaric acid
CH2OH-COOH
Glycolic acid
8) Lactose
It is composed of one molecule of glucose and on molecule of galactose. It is also called as
milk sugar. Lactose in human milk is 60% and in cow’s milk about 4.5%. It is formed in
mammary glands. It is dextrorotatory. The ά and β forms has specific rotation of + 90 and
+ 35 respectively and equimolar has + 52.5. It is less soluble in water, less sweet than
sucrose. Upon the action of lactose, lactose yields glucose and galactose. It is a reducing
sugar and has C1-C4 Glycosidic linkage. So it reduces Fehling’s solution.
9) Asymmetric carbon atom.
The carbon atom whose four valencies are satisfied by four different groups is called as
asymmetric carbon atom. The presence of asymmetric carbon atom in the carbohydrate
makes possible for the formation of isomers in them. The arrangement of the groups in
different patterns in Stereoisomers always takes place around asymmetric carbon atom.
Number of possible optical isomers in any compound depends upon the number of
asymmetric carbon atom. Total number of optical isomers of a compound is given by the
formula 2n where n is number of asymmetric carbon atom. Presence of asymmetric carbon
atom confers optical activity to it. Accordingly D and L types of compound are present.
10) Classification of carbohydrate
Depending upon their complexity and behaviour on hydrolysis, the carbohydrates are
classified into three categories
a) Monosaccharides b) Oligosaccharides c) Polysaccharides
Monosaccharides based on number of carbon atoms present in it, it is classified as follows
1) Triose – Glyceraldehydes 2) Tetroses- Erythroses 3) Pentoses- Riboses 4) Hexoses-
Glucoses/ Fructoses 5) Heptoses - Sedoheptuloses
Oligosaccharides are classified based on number of monosaccharides formed on
hydrolysis. Number of monosaccharides formed ranged from 2 to 10. Accordingly a) two
– disaccharides b) three- trisaccharides c) four- tetrasaccharides etc.,
Disaccharides based on the linkage is classified into 1) reducing sugar and 2) non- reducing
sugar
Reducing sugar has got two types of linkage a) C1-C4 (maltose and lactose) and C1- C6
(gentibiose and melibiose) and non- reducing sugar has C1-C1 linkage (sucrose)
Polysaccharides are classified into a) Homoglycans (Cellulose) b) Heteroglycans (Hemi
cellulose). Based on their functional aspect, polysaccharides are classified into a) Nutrient
/ digestible/storage – (Starch, glycogen and inulin) b) Structural/indigestible (Cellulose/
pectin/chitin).
11) Mutarotation
When a monosaccharide is dissolved in water, the optical rotatory power of the solution
gradually changes until a constant value is attained. A freshly prepared aqueous solution
of ά D glucose for instance has a specific rotation of + 112.2 and when this solution is
allowed to stand, the rotation falls to + 52..7 and remains constant. This gradual change in
specific rotation is known as mutarotation. All reducing sugars undergo mutarotation.
12) Reducing and non-reducing sugar
Any carbohydrate which is capable of being oxidized and causes the reduction of other
substances without having to be hydrolysed first is known as reducing sugar. The
carbohydrates which are unable to be oxidized and do not reduce other substances are
known as non- reducing sugars. All free monosaccharides having free aldehydes or ά
hydroxy ketonic groups are capable of being oxidized and cause the reduction of the other
substances is reducing sugars. Fehling’s solution and Benedict’s solution are used to carry
out the oxidation to check for reducing sugar. The sucrose is non- reducing sugar because
the Glycosidic bond blocks reducing groups of both the monosaccharides units. Reducing
 sugar will exhibit mutarotation. Reducing sugar will have C1-C4 linkage while non-
reducing sugar will have C1-C1 linkage. Reducing sugar are hemiacetal, do form osazones
with phenyl hydrazines, form oximes with hydroxylamine. But non- reducing sugar are
acetal, do not form osazone and oximes
13) Polysaccharides
It is formed by combination of many monosaccharides joined together by Glycosidic
linkages. They are also called as glycans. It is classified into Homoglycans (made up of one
kind of monosaccharides) and Heteroglycans (made up of different kinds of
monosaccharides). Polysaccharides are grouped based on their functional aspect,
polysaccharides are classified into a) Nutrient/ digestible/storage – (Starch, glycogen and
inulin) b) Structural/indigestible (Cellulose/ pectin/chitin). The starch is made up of
amylose and amylopectin and is reserve food materials for higher plants. Glycogen is the
major reserve food in animals and often called as animal starch. Cellulose is a long straight
chain polysaccharides consisting of many β- D glucose units joined together by ά -1-4
Glycosidic linkage. Hemi cellulose is made up of pentoses and hexoses. It is long chained
but shorter chains with branched ones.

ESSAY TYPES
1. What are the main types of carbohydrates found in plants? Add a note on their
importance in plant metabolism
The main type of carbohydrates found in plants are monosaccharides (triose, tetroses,
pentoses, hexoses and heptoses), oligosaccharides (disaccharides and trisaccharides) and
polysaccharides (storage polysaccharides- starch, glycogen) and structural polysaccharides
(cellulose, chitin). The metabolism of carbohydrates is of utmost importance to organisms
individually and collectively. Fundamentally all organic food stuffs are ultimately derived
from the synthesis of carbohydrates through photosynthesis. The catabolism of
carbohydrates provides the major share of energy requirements for maintainenance of life
and work function. Carbohydrates act as an energy reservoirs and serve architectural
function and are important constituents of nucleic acids. Plant contains higher amount of
carbohydrates compared to animals. The carbohydrates present in grains, tubers, roots are
referred to as starch and forms a stable food.
2) Describe the mechanism of biosynthesis and degradation of sucrose
Synthesis of sucrose
Synthesis of sucrose in plants may take place in three different ways
1) From glucose –1-phosphate and fructose in the presence of the enzyme Phosphorylase.
Eg. In bacteria
Glucose- 1-Phosphate + Fructose Sucrose + Pi
2) From UDPG (Urdine Di- phosphate glucose) and fructose in the presence of the
enzyme sucrose synthetase eg. In higher plants
 UDPG + Fructose UDP + Sucrose
Sucrose synthetase
3) From UDPG and fructose- 6-phosphate in the presence of enzyme sucrose
Phosphate synthetase. eg, in higher plants
UDPG + fructose -6-phosphate UDP + sucrose phosphate
Sucrose phosphate synthetase
Sucrose phosphate is hydrolysed in the presence of phosphatase enzyme to yield sucrose
Sucrose Phosphate Sucrose + phosphate
Phosphatase
Break down of sucrose
Sucrose is broken down or hydrolysed to yield glucose and fructose in the presence of the
enzyme invertase or sucrase. The reaction is irreversible
Sucrose + H2O Glucose + Fructose
Invertase
3) Describe the properties of carbohydrate
Monosaccharides
1) Reaction with alcohol – The Glycosidic OH group of mutarotating sugars reacts with
alcohol to form ά and β glycosides or acetals. Thus glucose form glucosides and
fructose from fructosides
2) Reaction with acetic anhydride- The Glycosidic and alcoholic OH group of
monosaccharides and disaccharides react with acetylating agents to form acetate
derivatives called esters
3) Oxidation with acids- Only the aldehydes group of sugar is oxidized to produce
monocarboxylic acid with bromine water, while with nitric acid both aldoses and
ketoses react to form dicarboxylic acid
4) Oxidation with metal hydroxides- Metal hydroxides like copper hydroxide
oxidize free aldehydes or keto group of mutarotating monosaccharides and at the
same time they themselves reduce to free metal
Reducing sugar + Cu2+ oxidized sugar + 2 Cu+
2Cu+ + 2OH- 2Cu.OH Cu2O + H2O
Yellow Red
This sugar is active ingredient in Fehling’s, Benedict’s and Barfoed’s reagent
5) Reduction- The sugars undergo reduction with sodium amalagam to form
corresponding alcohols. Glucose yields sorbitol and fructose yields mixture of
sorbitol and mannitol. With strong acids, it undergo reduction to form levulinic
acid.
6) Reaction with hydrogen cyanide- (Kilani synthesis). It forms cyanohydrins
 7) Reaction with alanine – The aldehydes group of carbohydrate condenses with the
amino group of alanine to form Schiff’s base.
8) Reaction with Phenyl hydrazine – reaction of monosaccharides with phenyl
Hydrazine yields osazone
9) Fermentation- Monosaccharides are readily fermented by yeast to form alcohol
Disaccharides
1) Sucrose- it is dextrorotatory, a non- reducing sugar, does not exhibit
mutarotation, does not form osazone and fermentable
2) Lactose- It is dextrorotatory, a reducing sugar, exhibit mutarotation, form osazone and
Non-fermentable
3) Maltose- It is dextrorotatory, a reducing sugar, exhibit mutarotation, form osazone and
fermentable
4) Cellobiose- It is a reducing sugar, exhibit mutarotation
Polysaccharides
1) Starch- It is made up of amylose and amylopectin. Amylose gives blue colour with
Iodine, amylopectin gives purple with iodine and dextrorotatory,
2) Glycogen- It is a non-reducing sugar, gives red colour with iodine, white powder,
Fairly stable in hot alkali
3) Cellulose- It gives no colour with iodine, fibrous, tough, white solid
4) Inulin- It is a non-reducing sugar, gives no colour with iodine
5) Chitin- It is non-reducing sugar
4) Compare the structural features of amylose, cellulose and chitin
Sl.No Amylose Cellulose Chitin

1 Formed by elimination Formed by eliminating The alcoholic OH

of a molecule of water a molecule of water group on carbon atom
from Glycosidic OH from Glycosidic OH on 2 of β- D glucose
group of one ά- D carbon atom 1 of one β- units is replaced by
glucose and alcoholic D glucose and the N- acetylamino group
OH group on carbon 4 of alcoholic OH group on
the adjacent ά- D carbon 4 of the
glucose adjacent β- D glucose
2 The linkage in amylose It is regarded as an It is linear polymer of
is ά -1-4 linkage anhydride of β- D N- acetyl- D_
glucose glucosamine units
joined together by β-
1-4 glucosidic
linkage

5) Enumerate the important monosaccharides and their occurrence

The important monosaccharides are a) Triose b) Tetroses c) Pentoses d) Hexoses e)
 Heptoses
1) Triose – Glyceraldehydes. The simplest compound having three carbon atoms. It is
colourless, sweet, crystalline and soluble in water, insoluble in ether, cannot be
hydrolysed and formed in the plants during glycolysis
2) Tetroses- Erythroses. This has four carbon atoms, colourless, crystalline, soluble in
water, insoluble in ether. It is produced in plants in photosynthesis in presence of
transketolase from fructose -6- phosphate
3) Pentoses- Riboses and Ribulose. They have 5 carbon atoms. In plants they are found in
combined state. It reduces Fehling’s solution and gives Molisch’s test. They are not
fermentable. Ribose is an aldopentoses and ribulose is keto pentoses. It is used in the
formation of RNA. Arabinose is colourless, sweet in taste. It can be obtained by the
hydrolysis of gum Arabic, peach gum and cherry gum. It reduces Fehling’s solution. Xylose
is aldosugar and xylulose is ketonoic form and is formed in photosynthesis. It is colourless,
crystalline, optically inactive. It is also formed by hydrolysis of wood gum or xylose.
4) Hexoses- Glucose/ fructose- These sugars are six carbon atoms and cannot be hydrolysed.
Glucose is called as dextrose formed by the hydrolysis of cane sugar, glucosides, starch and
cellulose etc., It is needle shaped crystals, anhydrous. Fructose is a keto sugar formed in
equal quantity with glucose by the hydrolysis of cane sugar, soluble in hot absolute alcohol
and ether. Mannose is prepared by hydrolysing mannane found in ivory nuts.
5) Heptoses – Glucoheptoses and Sedoheptulose. They are seven sugar carbon atom. It is
ketosugar and formed in photosynthesis
6) Discuss the four important chemical reactions of carbohydrates
1) Oxidation with acids:
a) Mild oxidizing agent (HOBr). Only the aldehydes group is oxidized by bromine water
to produce monocarboxylic acid. Ketoses do not react with bromine water
CHO-(CHOH)4- CH2OH + HOBr COOH - (CHOH)4- CH2OH + HBr
Glucose Gluconic acid
b) Strong acids (HNO3): Both aldoses and ketoses react with nitric acid to form
dicarboxylic acid
CHO-(CHOH)4- CH2OH + HNO3 COOH - (CHOH)4- COOH + H2O
Glucose Glucaric acid
c) Oxidation with metal hydroxide: Metal hydroxide Cu(OH)2 oxidize the free aldehydes
and keto group and reduce itself to form free metal
Reducing sugar + 2 Cu2+ Oxidized sugar + 2 Cu2+
Blue
2+ -
2 Cu + 2OH 2CuOH Cu2O + H2O
Yellow Red
 2) Reduction: The sugars may be reduced in various ways depending upon the type of
reducing sugars used.
a) With sodium amalgam: The monosaccharides are reduced to form alcohol by treating
it with sodium amalgam. Glucose yields sorbitol and fructose yields mixture of sorbitol
and mannitol
CHO-(CHOH)4- CH2OH + Na amalgam CH2OH-(CHOH)3 - CH2OH
Glucose Sorbitol
CH2OH- C=O-(CHOH)4- CH2OH + 4H CH2OH-(CHOH)3- CH2OH
Fructose Sorbitol
CH2OH-(CHOH)3- CH2OH
Mannitol

b) With strong mineral acid- Hexoses on reaction with acid undergo reduction to form
5-hydroxy methyl furfural which is on further heating form levulinic acid
c) With dilute alkali: Glucose fructose and mannose are interconvertible in weak
alkaline solution such as calcium hydroxide and barium hydroxide at low temperature
3) Reaction with Phenyl hydrazine: One mole of aldose reacts with one mole of phenyl
hydrazine to form one molecule of hydrazones and hydrazones is oxidized to form
aldohydrazones and finally osazone. Osazone is noticed in monosaccharides and
disaccharides.
4) Reaction with alanine. The aldehydes group of carbohydrates condenses with amino
group of alanine to form Schiff’s base
H CH3
CHO-(CHOH)4- CH2OH + CH3-NH2-C-H-COOH C= N-C-H + H2O
R COOH
7) Write a detailed note on polysaccharides with examples
Polysaccharides are also compound sugars and yield more than 10 molecules of
monosaccharides on hydrolysis. These may be further classified depending up on
whether monosaccharides molecules produced as a result of the hydrolysis of
polysaccharides of the same type (homo polysaccharides) or if different types (Hetero
polysaccharides). The general formula (C6H10O5)x. Based on the functional aspect,
polysaccharides are grouped in to
a) Nutrients/digestible polysaccharides – These act as a metabolic reserve of
monosaccharides in plant and animals eg. Starch, glycogen
b) Structural/ indigestible polysaccharides- These serve as rigid mechanical
structures in plants and animals- cellulose, pectin and chitin
 1) Starch- Major reserve food in higher plants. It consists of ά-D –glucose and made
up of amylose and amylopectin. Amylose gives blue colour with iodine; amylopectin
gives purple colour with iodine. It is dextrorotatory. It yields glucose units on hydrolysis.
Hence it is a glucosans
2) Glycogen- It is major source of food of animals. It is stored in liver and muscles of
animals. The constituent monosaccharides are ά-D –glucose. It si non-reducing sugar,
gives red colour with iodine. It yields glucose units on hydrolysis, hence a glucosans
3) Inulin – It is found in tubers and roots. The constituent monosaccharide is β- D-
glucose. It is non-reducing sugar, gives no colour with iodine, yields fructose on
hydrolysis, hence fructosans
4) Cellulose- It is widely distributed in plants. The constituent monosaccharide is is β-
D-glucose., gives no colour with iodine , yields glucose units on hydrolysis, hence
glucosans
5) Pectin-It is in fruits of many plants. The constituent monosaccharide is ά-D –
galactouronic acid
6) Chitin- Most abundant in nature after cellulose, found in fungi and anthropods. The
constituent monosaccharides are N- Acetyl- D- glucosamine. It is non- reducing sugar.
8) What re polysaccharides? Differentiate between amylose and amylopectin
Polysaccharides are formed by the combination of many monosaccharides joined
together by Glycosidic linkages. They are also known as glycans and are again classified
into Homoglycans and Heteroglycans. These polysaccharides which are made up of only
kind of monosaccharides are known as Homoglycans. While those which are made up of
two or more kinds of monosaccharides are known as hetero glycans. Polysaccharides are
hydrolysed either by enzymes or mineral acid. The most common examples of
polysaccharides are starch, cellulose, glycogen, Chitin and inulin
Amylose Amylopectin
1) It contains 15-20% in starch 1) It contains 80-85% in starch
2) It is straight chain compound of about 2) It is branched chain compound of
100-700 glucose units about 300-5500 glucose units
3) The molecular weight is 10000 to 50000 The molecular weight is 50000-
1000000
4) It has ά-1-4 linkage It has ά-1-4 linkage and ά- 1-6 linkage
5) It does not form paste and readily soluble It is not readily dispersed in water and
in water form paste
6) It gives blue colour with iodine It gives red colour with iodine
7) Enzymatic hydrolysis of amylose with On incomplete hydrolysis yields
amylase yields maltose disaccharide isomaltose
9) Distinguish between mono, Oligo and Polysaccharides
Monosaccharides Oligosaccharides Polysaccharides
1) It is simplest sugar eg. It is also sugar, but it may It is no reducing sugar eg.
Glucose be non-reducing or Starch, glycogen
reducing sugar eg.,
sucrose, maltose
2) It contains generally up It contains generally 12 to It contains more number of
to 9 carbon atoms 36 carbon atoms carbon atoms
3) They contain carbonyl Do not contain carbonyl Do not contain carbonyl
group and show the group and does not show group and does not show
properties of aldehydes reaction with aldehydes or reaction with aldehydes
and ketones ketone group and ketone group
4) They are colorless, They are generally They are colorless,
crystalline and sweet colorless, crystalline and amorphous and tasteless
sweet
5) Soluble in water Soluble in water Insoluble in water
6) They are optically They are optically active They are optically inactive
active
7) They have free or No No
potential aldehydes or
ketone group
8) It cannot be hydrolyzed It can be hydrolyzed to It can be hydrolyzed to
yield 2-10 molecules of yield more than 10
monosaccharides molecules of
monosaccharides
10) Discuss the importance/significance of carbohydrates
A) In plants and animals
1) It is structural materials of plants
2) It is reserve food material as starch in tubers, roots and grains
3) Sucrose is present in the nectar of flowers and in fruits
4) Carbohydrate on oxidation yields energy which is utilized by plants for various
physiological processes
B) For human beings
1) The starches and sugar are the main food easily digestible and oxidisable to provide
energy for various physiological activities
2) Carbohydrates present in seeds such as rice, maize, rye, barley are utilized for the
production of alcoholic beverages
3) Carbohydrates derivatives such as glucosides form important drugs and other
medicines for various diseases
4) Carbohydrates particularly cellulose and its derivatives are used in the production of
artificial silk, paper and plastics
 5) Blood contains glucose as sugar. Blood glucose are removed by muscles and older
tissues and form glycogen which provides energy on oxidation. Mammary glands
form milk sugar
11) What are the important tests for carbohydrates?
1) Fehling’s solution test: Mix Fehling’s solution A and B in equal amounts in a test
tube. Now add equal volume of glucose solution and boil it till brick red precipitate is
produced. The Fehling’s solution contains cupric sulfate, sodium hydroxide and sodium
potassium tartrate. When solution is mixed with glucose and boiled, the aldehydes group
of glucose is oxidized and cupric salt is reduced to cuprous oxide giving red precipitate
C6H12O6 + 2 Cu(OH)2 C6H12O7+ Cu2O + H2O
Blue Red
2) Benedict’s test: Mix 3 ml of Benedict’s solution and one ml of glucose solution and
warm them gently. A reddish brown colour of cuprous oxide is produced. On warming
the colour of the mixture turn from blue to green and from green to reddish brown.
Benedict’s solution contains blue colour copper sulfate. When alkaline solution of
glucose is added to this and warmed, the aldehydes group of glucose is oxidized and blue
colored copper sulfate is changed to green colored copper hydroxide and ultimately
copper hydroxide changed to reddish brown cuprous oxide
3) Molisch’s Test: Sugar and their polymers give characteristic colour in the presence of
strong sulfuric acid and ά naphthol. The sugars in the presence of acids undergo
dehydration to form furfural and the violet colour is produced by the condensation of
aldehydes and phenol
4) Seliwanoff test: It is a chemical test which distinguishes between aldose and ketose
sugar. Sugars containing keto group when heated with HCl and resorcinol, bright red
colour is produced
 PROTEINS
The word "Protein" was coined by J.J. Berzelius in 1838 and was derived from the Greek word
"Proteios" meaning the ‘first rank’.
Introduction:
• Most abundant organic molecules of the living system
• Its fundamental basis of structures and function of life.
• 50 % of dry weight of every cell
• It’s a polymer of L α-amino acids.
• 300 different amino acids occur in nature –only 20 as standard amino acids.
• 21st amino acid added - Seleno cysteine
Definition
Proteins are organic complex nitrogenous compounds of high molecular weight, formed of C,
H, O, N [N= 16%].
They are formed of a number of amino acids linked together by peptide linkage [-CO-NH-].
The carboxylic group of the first amino acid units with the amino group of the second amino
acid and so on.
General Properties of Proteins
 Proteins are substances of high molecular weight.
 Proteins form colloidal solution and having its same properties as:
Tyndall effect & Brownian movement
 Proteins are non-dialyzable due to their large molecules.
 Proteins are amphoteric which liable to react with acid and alkali.
 Each protein has its own isoelectric point.
 Protein acts as a buffer solution which resists the change of its pH by addition of acid or
alkali.
 Denaturation
Biological Importance of Proteins
 They provide the body with nitrogen, sulfur, and some vitamins.
 Formation of enzymes and protein hormones.
 Formation of supporting structures in the body as bone, cartilage, skin, nails, hair and
muscles.
 They enter in the formation of buffer system of the blood.
 They enter in the formation of haemoglobin
 They include plasma proteins, which carry hormones, minerals and lipids (in the form of
lipoprotein complex).
 They enter in formation of antibodies (immunoglobulins
CLASSIFICATION OF PROTEINS
Proteins are classified on the basis of
– Chemical nature and solubility
• Simple • Conjugates • Derived
– Function
• Structural • Enzyme or catalytic • Transport • Hormonal
• Contractile • Storage • Genetic • Defence • Receptor
– Nutritional Importance
• Complete • partially incomplete • Incomplete
Classification of proteins according to their solubility and composition
I- Simple proteins:
i.e. on hydrolysis gives only amino acids
as albumin , globulins, glutellin, Prolamines , Protamines, Histones, Albuminoids
(Scleroproteins).
Albumins
 Albumins are readily soluble in water, dilute acids and alkalies coagulated by heat.
 Seed proteins contain albumin in lesser quantities.
 Albumins may be precipitated out from solution using high salt concentration, a process
called 'salting out'.
 They are deficient in glycine.
 Serum albumin and ovalbumin (egg white) are examples
Globulins
 Globulins are insoluble or sparingly soluble in water, but their solubility is greatly increased
by the addition of neutral salts such as sodium chloride.
 These proteins are coagulated by heat.
 They are deficient in methionine.
 Serum globulin, fibrinogen, myosin of muscle and globulins of pulses are examples.
Prolamins
 Prolamins are insoluble in water but soluble in 70-80% aqueous alcohol.
 Upon hydrolysis they yield much proline and amide nitrogen, hence the name prolamin.
 They are deficient in lysine.
 Gliadin of wheat and zein of corn are examples of Prolamins.
Glutelins
Glutelins are insoluble in water and absolute alcohol but soluble in dilute alkalies and acids.
They are plant proteins e.g., glutenin of wheat.
Histones
Histones are small and stable basic proteins
 They contain fairly large amounts of basic amino acid, histidine.
 They are soluble in water, but insoluble in ammonium hydroxide.
 They are not readily coagulated by heat.
 They occur in globin of haemoglobin and nucleoproteins
Protamines
Protamines are the simplest of the proteins.
 They are soluble in water and are not coagulated by heat.
 They are basic in nature due to the presence of large quantities of arginine.
 Protamines are found in association with nucleic acid in the sperm cells of certain fish.
 Tyrosine and tryptophan are usually absent in protamines.
Albuminoids
 These are characterized by great stability and insolubility in water and salt solutions.
 These are called Albuminoids because they are essentially similar to albumin and
globulins.
 They are highly resistant to proteolytic enzymes.
 They are fibrous in nature and form most of the supporting structures of animals.
 They occur as chief constituent of exoskeleton structure such as hair, horn and nails.
ii. Conjugated or compound proteins
 These are simple proteins combined with some non-protein substances known as
prosthetic groups.
 The nature of the non-protein or prosthetic groups is the basis for the sub classification
of conjugated proteins.
Its again of 6 types
1. Phosphoproteins: These are proteins conjugated with phosphate group. Phosphorus is
attached to OH group of serine or threonine. e.g. Casein of milk and vitellin of yolk.
2. Lipoproteins: These are proteins conjugated with lipids. Functions: a - help lipids to
transport in blood b - Enter in cell membrane structure helping lipid soluble substances to
pass through cell membranes
3. Glycoproteins: proteins conjugated with sugar (carbohydrate e.g. – Mucin , Some
hormones such as erythropoietin, present in cell membrane structure blood groups.
4. Nucleoproteins: These are basic proteins (e.g. histones) conjugated with nucleic acid
(DNA or RNA). e.g. a- chromosomes : are proteins conjugated with DNA
b- Ribosomes : are proteins conjugated with RNA
5. Chromoprotein: prosthetic group is colored in nature. Ex: Haemoglobins, cytochromes
6. . Metallo protein: it contains metal ions such as Fe, Co, Zn, Cu, Mg,
iii. Derived proteins
 Denatured or degraded product of simple or conjugated protein by the action of acids,
alkalies or enzymes
 They include two types of derivatives, primary-derived proteins and secondary-derived
proteins
Its of 2 types
– Primary derived protein: denatured or coagulated or first hydrolysed product of proteins.
They are
• Cogulatedproteins: denatured protein produced by agents such as heat, acids, alkalies
• Proteans: earliest product of protein hydrolysis by enzymes, dilute acids, alkalies etc.
Insoluble in water
• Metaprotein: second stage of protein hydrolysis obtained by treatment with slightly stronger
acids and alkalies
Secondary protein derivatives:
These are the hydrolytic products of proteins
- Proteoses:
Result from partial hydrolysis of proteins.
- Peptones:
Result from further hydrolysis of proteases.
Soluble in H2O.
- Peptides:
Resulting from further hydrolysis of peptones.
- Amino acids
Protein -----> Protean ------- Metaprotein
Proteoses ------> Peptones ------->Peptides ------ amino acids
Classification of proteins based on function
Catalytic proteins – Enzymes
 The most striking characteristic feature of these proteins is their ability to function within
the living cells as biocatalysts.
 These biocatalysts are called as enzymes.
 Enzymes represent the largest class.
 Nearly 2000 different kinds of enzymes are known, each catalysing a different kind of
reaction.
 They enhance the reaction rates a million fold
Regulatory proteins – Hormones
These are polypeptides and small proteins found in relatively lower concentrations in animal
kingdom but play highly important regulatory role in maintaining order in complex metabolic
reactions e.g., growth hormone, insulin etc.
Protective proteins – Antibodies
These proteins have protective defence function.
These proteins combine with foreign protein and other substances and fight against certain
diseases.
e.g., immunoglobulin.
These proteins are produced in the spleen and lymphatic cells in response to foreign
substances called antigen.
The newly formed protein is called antibody which specifically combines with the antigen
which triggered its synthesis thereby prevents the development of diseases.
Fibrin present in the blood is also a protective protein
Storage proteins
It is a major class of proteins which has the function of storing amino acids as nutrients and as
building blocks for the growing embryo.
Storage proteins are source of essential amino acids, which cannot be synthesized by human
beings.
The major storage protein in pulses is globulins and Prolamins in cereals. In rice the major
storage protein is glutelins. Albumin of egg and casein of milk are also storage proteins.
Transport proteins
- Some proteins are capable of binding and transporting specific types of molecules through
blood.
- Haemoglobin is a conjugated protein composed of colourless basic protein, the globin
and ferroprotoporphyrin or haem.
- It has the capacity to bind with oxygen and transport through blood to various tissues.
- Myoglobin, a related protein, transports oxygen in muscle.
- Lipids bind to serum proteins like albumin and transported as lipoproteins in the blood
Toxic proteins
- Some of the proteins are toxic in nature.
- Ricin present in castor bean is extremely toxic to higher animals in very small amounts.
- Enzyme inhibitors such as trypsin inhibitor bind to digestive enzyme and prevent the
availability of the protein.
- Lectin, a toxic protein present in legumes, agglutinates red blood cells.
- A bacterial toxin causes cholera, which is a protein.
- Snake venom is protein in nature
Structural proteins
These proteins serve as structural materials or as important components of extra cellular fluid.
Examples of structural proteins are myosin of muscles, keratin of skin and hair and collagen
of connective tissue.
Carbohydrates, fats, minerals and other cellular components are organized around such
structural proteins that form the molecular framework of living material.
Contractile proteins
Proteins like actin and myosin function as essential elements in contractile system of skeletal
muscle.
Secretary proteins
Fibroin is a protein secreted by spiders and silkworms to form webs and cocoons.
Classification based on size and shape
Based on size and shape, the proteins are also subdivided into globular and fibrous proteins
 Globular proteins are mostly water-soluble and fragile in nature e.g., enzymes, hormones
and antibodies.
 Fibrous proteins are tough and water-insoluble.
 They are used to build a variety of materials that support and protect specific tissues, e.g.,
skin, hair, fingernails and keratin
Structures of Protein
Conformation of a protein refers to the three-dimensional structure in its native state. There are
many different possible conformations for a molecule as large as a protein. A protein can
perform its function only when it is in its native condition. Due to the complexity of three-
dimensional structures, the structure of protein is discussed at different levels of its
organization. Proteins are formed of a large number of amino acid linked together by peptide
bonds (polypeptide chain).
There are four orders of protein structures

Alpha Helix
α helix is twisted by an equal amount about each α-carbon. The formation of the α-helix is
spontaneous and is stabilized by H-bonding between amide nitrogen and carbonyl carbons of
peptide bonds spaced four residues apart. This orientation of H-bonding produces a helical
coiling of the peptide backbone such that the R-groups lie on the exterior of the helix and
perpendicular to its axis.
5 kind of bonds stabilize tertiary structure
 van der Waals interaction (between neighbouring atoms) Van derWaals forces include
attractions and repulsions between atoms, molecules, and surfaces
 H-bonds within the chains or between chains
 hydrophobic interactions (between non-polar)
 ionic interactions (between oppositely charged groups)
 Disulphide linkages, the SH groups of two neighbouring cysteine’s form –s=s bond known
as disulphide linkage. (covalent bond)
Quaternary Structure
 Majority of proteins are composed of single polypeptide chains
 Some of protein consists of 2 or more polypeptide chain which may be identical or
different
 Such protein are termed as oligomers and poses quaternary structures.
 Proteins with identical Proteins oligomers.-homo subunits are termed Homodimers
 Proteins containing several distinct polypeptide chains are termed heterodimer
 Quaternary structure refers to a functional protein aggregate (organization) formed by
Interpolypeptide linkage of subunits or polypeptide chains.
 Myoglobin has no quaternary structure

Haemoglobin molecule, which consists of four separate

polypeptide chains, exhibits quaternary structure.

Properties of Protein
Physical
 Pure proteins are generally tasteless, though the predominant taste of protein hydrolysates
is bitter.
 Pure proteins are odourless.
 Because of the large size of the molecules, proteins exhibit many properties that are colloidal
in nature.
 Proteins, like amino acids, are amphoteric and contain both acidic and basic groups.
 They possess electrically charged groups and hence migrate in an electric field.
 Many proteins are labile and readily modified by alterations in pH, UV radiation, heat and
by many organic solvents
 The absorption spectrum of protein is maximum at 280 nm due to the presence of tyrosine
and tryptophan, which are the strongest chromophores in that region
Denaturation of Protein
 The comparatively weak forces responsible for maintaining secondary, tertiary and
quaternary structure of proteins are readily disrupted with resulting loss of biological
activity.
 This disruption of native structure is termed denaturation
 it is a change in native state (physical, chemical, and biological properties) of proteins
without destruction of their peptide linkages ,but destruction of secondary bonds leading
to unfolding protein molecule
Denaturating agents:
Physical: High temperature, high pressure, X-ray, ultraviolet rays-mechanical agitation.,
Chemical: Strong acids, strong alkalies organic solvents, heavy metals
Results of denaturation
Physical:
- Decrease solubility, increase viscosity and can not be crystallized.
Chemical:
- Unfolding of the protein molecule.
- Destruction of some subsidiary hydrogen bonds.
- Exposure of some groups as (SH) of cystiene.
Biological:
-Loss of activity, if it is hormone or enzyme.
-Loss of antigen antibody reaction (allergic manifestation). Easily digested
Chemical properties
Colour reactions of proteins
1. The colour reactions of proteins are of importance in the qualitative detection and
quantitative estimation of proteins and their constituent amino acids.
2. Biuret test is extensively used as a test to detect proteins in biological materials
Biuret reaction
A compound, which is having more than one peptide bond when treated
with Biuret reagent, produces a violet colour.
This is due to the formation of coordination complex between four
nitrogen atoms of two polypeptide chains and one copper atom

Xanthoproteic reaction
Addition of concentrated nitric acid to protein produces yellow colour on heating, the colour
changes to orange when the solution is made alkaline. This is due to the nitration of the phenyl
rings of aromatic amino acids.
Hopkins-Cole reaction
Indole ring of tryptophan reacts with glacial acetic acid in the presence of concentrated
sulphuric acid and forms a purple coloured product
Hydrolysis:
a) By acidic agents- Proteins up on hydrolysis with concentrated HCl at 100- 110oC for 6 to
20 hours yield amino acid in the form of their hydrochlorides
b) By alkaline agents – Proteins may also be hydrolyzed by 2N NaOH
c) By proteolytic enzymes- Certain proteolytic enzymes like pepsin and trypsin hydrolyze the
proteins under certain conditions of temperature and acidity
Reaction involving both COOH and NH2 groups
a) Ninhydrin test- It is powerful oxidizing agent and causes oxidative decarboxylation of α-
amino acids producing CO2, NH3 and aldehyde with one less carbon atom than the parent
amino acids. The reduced Ninhydrin then react with the liberated NH3 forming blue colored
complex
Why is protein folding?
Protein folding is the process by which a protein structure assumes its functional shape or
conformation. All protein molecules are heterogeneous unbranched chains of amino acids. By
coiling and folding into a specific three-dimensional shape they are able to perform their
biological function
Protein folding is a spontaneous process directed by the amino acid sequence of each individual
protein. Protein folding occurs in a cellular compartment called the endoplasmic reticulum.
This is a vital cellular process because proteins must be correctly folded into specific, three-
dimensional shapes in order to function correctly. Unfolded or misfolded proteins contribute
to the pathology of many diseases
Protein folding is “the final step in the decoding of genetic information
AMINO ACID

General Structure of Amino Acid

Each amino acid (except proline) has a carboxyl group, an amino group and a distinctive side
chain bonded to the alpha carbon atom. At physiological pH the carboxyl group is dissociated
forming the negatively charged carboxylate ion (-COO-), and the amino group is protonated (-
NH3+)
Bond Formation
Linking two amino acids together
Definitions (N-terminal, C-terminal,
Polypeptide backbone, amino acid residue, side chains)

20 Amino Acids

Nonpolar,
Hydrophobic

Polar, uncharged

Polar, charged

Amino Acid Classification

aliphatic
G P
beta-branched
CS-S A
CH S N
V
L
I T D
Q
E
negative
M K
F Y H R
aromatic W
positive
hydrophobic charged
polar
Bioinformatics Methods II, Spring 2003
Amino acids can be classified in 4 ways:
1 .Based on structure
2. Based on the side chain characters
3. Based on nutritional requirements
4. Based on metabolic fate
Based On Structure
Aliphatic amino acids

They are classified in three broad categories

A- Monobasic, monocarboxylic amino acids i.e. neutral or uncharged:
They are further subdivided in 5 groups:
a. Simple amino acids-example: glycine, alanine

b. Branched chain amino acids-e.g.: valine, leucine, isoleucine

c. Hydroxyl group containing amino acids-e.g.: serine, threonine

d. Sulphur containing amino acids-e.g.: cysteine, cystine, methionine

e. Amide group containing amino acids-e.g.- asparagine, glutamine

B) Mono amino dicarboxylic acid

Example: aspartic acid, glutamic acid

C) Di /poly amino mono carboxylic acid

Example: lysine, arginine

2) Aromatic amino acids

Phenyl alanine and tyrosine
3) Heterocyclic amino acids
Tryptophan and Histidine

4) Imino acids
Proline

5) Derived amino acids (non-protein amino acid) Non-α-amino acids

e.g.: β-alanine, γ-amino butyric acid (GABA), δ-amino Levulinic acid
Derived and Incorporated in tissue proteins:
e.g.: Hydroxy-proline, hydroxy-lysine
Derived but not incorporated in tissue proteins:
e.g.: Ornithine, Citrulline, Homocysteine, Arginosuccinic acid
II- Classification according to polarity of side chain (R):
A- Polar amino acids: in which R contains polar hydrophilic group so can forms hydrogen
bond with H2O. In those amino acids, R may contain:
1- OH group: as in serine, threonine and tyrosine
2- SH group: as in cysteine
3- Amide group: as in glutamine and asparagine
4- NH2 group or nitrogen act as a base (basic amino acids ): as lysine, arginine and histidine
5- COOH group (acidic amino acids): as aspartic and glutamic.
B- Non polar amino acids:
R is alkyl hydrophobic group which can’t enter in hydrogen bond formation. 9 amino acids
are non-polar (glycine, alanine, valine, leucine, isoleucine, phenyl alanine, tryptophan,
proline and methionine)
III- Nutritional classification:
1- Essential amino acids: These amino acids can’t be formed in the body and so, it is essential
to be taken in diet. Their deficiency affects growth, health and protein synthesis.
2- Semi essential amino acids: These are formed in the body but not in sufficient amount for
body requirements especially in children.
Summary of essential and semi essential amino acids:
Villa HM = Ten Thousands Pound
V= valine i= isoleucine l= lysine l= leucine
A = arginine* H= histidine* M= methionine
T= tryptophan Th= threonine P= phenyl alanine
*= arginine and histidine are semi essential
3- Non essential amino acids: These are the rest of amino acids that are formed in the body in
amount enough for adults and children. They are the remaining 10 amino acids.
IV- Metabolic classification: according to metabolic or degradation products of amino acids
they may be:
1- Ketogenic amino acids: which give ketone bodies. Lysine and Leucine are the only pure
ketogenic amino acids.
2- Mixed ketogenic and glucogenic amino acids: which give both ketone bodies and glucose.
These are: isoleucine, phenyl alanine, tyrosine and tryptophan.
3- Glucogenic amino acids: Which give glucose. They include the rest of amino acids. These
amino acids by catabolism yields products that enter in glycogen and glucose formation
Amphoteric properties of amino acids: that is they have both basic and acidic groups and so
can act as base or acid.
Neutral amino acids (monobasic, monocarboxylic) exist in aqueous solution as “Zwitter ion”
i.e. contain both positive and negative charge. Zwitter ion is electrically neutral and can’t
migrate into electric field.
Isoelectric point (IEP) = is the pH at which the Zwitter ion is formed. e.g IEP of alanine is 6
Chemical properties of amino acids:
1- Reactions due to COOH group:
Salt formation with alkalis, ester formation with alcohols, amide formation with amines and
decarboxylation
2-Reactions due to NH2 group: deamination and reaction with Ninhydrin reagent.
Ninhydrin reagent reacts with amino group of amino acid yielding blue colored product. The
intensity of blue color indicates quantity of amino acids present. Ninhydrin can react with
imino acid like proline and hydroxy proline but gives yellow colour
3. Reaction due to side chain ( R)
a) Million reaction : for Tryosine it gives red colour
b) Rosenheim reaction : for tryptophan, it gives violet ring
c) Pauly reaction: for imidazole ring of histidine , give yellow to reddish product
d) Sakagushi test: for guanido group of arginine and gives red colour
e) Lead sulphide test ( sulfur test): sulfur containing amino acid gives brown colour
:
Properties of amino acids
Physical
 Amino acids are white crystalline substances.
 Most of them are soluble in water and insoluble in non-polar organic solvents (e.g.,
chloroform and ether).
 Aliphatic and aromatic amino acids particularly those having several carbon atoms have
limited solubility in water but readily soluble in polar organic solvents.
 They have high melting points varying from 200-300oC or even more.
 They are tasteless, sweet or bitter.
 Some are having good flavour. Sodium glutamate is a valuable flavouring agent and is used
in the preparation of certain dishes and sauces.
Amphoteric nature of amino acids
 Amino acids are amphoteric compounds, as they contain both acidic (COOH) and basic
(NH2) groups.
 They can react with both alkalies and acids to form salts.
 In acid solution amino acids carry positive charges and hence they move towards cathode
in an electric field.
 In alkaline solution, the amino acids carry negative charges and therefore move towards
anode.
 When an amino acid is dissolved in water, it exists as inner salt carrying both positive and
negative charges.
 This occurs as a result of dissociation of carboxyl group to release the H+ ion, which passes
from the carboxyl to the amino group.
 The amino acids possessing both positive and negative charges are called Zwitter ions
 The zwitterion reacts as an acid with a base by liberating a proton (H+) from the NH3+
group and as a result possesses a net negative charge.
 On the other hand, zwitterions reacts with an acid as base, combining with the proton (H+)
of the acid resulting in the formation of a compound having a net positive charge.
 These reactions are reversible.
 The pH at which the amino acid has no tendency to move either towards positive or
negative electrode is called isoelectric pH or isoelectric point.
 At isoelectric pH, the amino acid molecule bears a net charge of zero
Isomerism
All amino acids except proline, found in protein are
α-amino acids because NH2 group is attached to the
α-carbon atom, which is next to the COOH group.
Examination of the structure of amino acids reveals
that except glycine, all other amino acids possess
asymmetric carbon atom at the alpha position.
Because of the presence of asymmetric carbon
atom, amino acids exist in optically active forms
'D' and 'L' do not refer to the optical rotation, but to the steric configuration of amino group to
the right and left side of the carboxyl group. The direction of optical rotation of amino acid is
indicated by the symbol + or -, which follows the designation 'D' or 'L'. The steric configuration
and optical rotation of an amino acid may be simultaneously expressed as D (+) or D (-) and L
(+) or L (-). L-forms are more common than D-forms and most of the naturally occurring amino
acids are L-amino acids
Peptides and Proteins
20 amino acids are commonly found in protein.
These 20 amino acids are linked together through “peptide bond forming peptides and proteins
(what’s the difference?).
-The chains containing less than 50 amino acids are called “peptides”, while those containing
greater than 50 amino acids are called “proteins”.
Peptide bond formation:
α-carboxyl group of one amino acid (with side chain R1) forms a covalent peptide bond with
α-amino group of another amino acid ( with the side chain R2) by removal of a molecule of
water. The result is : Dipeptide ( i.e. Two amino acids linked by one peptide bond). By the
same way, the dipeptide can then forms a second peptide bond with a third amino acid (with
side chain R3) to give Tripeptide. Repetition of this process generates a polypeptide or protein
of specific amino acid sequence.
FILL UP THE BLANKS
1. The basic functional group of protein is_______
2. Amino acid lowers a net charge of zero at _______
3. Water soluble proteins are_________
4. The S containing amino acids are____,___ and ______
5. Phenyl alanine is a _____ amino acid
6. _____ is an amino acid found in thyroid secretions
7. _____ is an example of basic amino acid_______
8. ______ is a factor for converting nitrogen to protein
9. ____ is an aromatic amino acid
10. The essential amino acid is _______
11. _______ enzyme splits peptides of proteins
12. The linkage formed when two molecules of amino acids linked together is called as
______
13. _______ is a salt soluble protein in cereals
14. The average content of nitrogen in protein is _____
15. The building blocks of proteins are ______
16. An example of mono-dicarboxylic acid is ______
17. Proteins when treated with dilute copper sulfate and made alkaline with sodium
hydroxide develop violet colour. This is due to ______
18. Amino acids soluble in water and in ammonia are known as _____
19. Methionine is an amino acid and also contain
20. Proteins contain NH2 and COOH are called _______
21. Example of fibrous proteins is _____
22. two essential amino acids are _______ and ______
23. The pH at which amino acid has no net charge is called _______
24. Albumin is an example for ____
25. Globulin is an example for ______
26. The bond responsible for the secondary structure of proteins is _____
27. Proteins are least soluble at__ point
28. _____ is an example of pyrimidine bases
29. The condensation products of nucleotides are called _______
30. The purine bases are _______ and _______
31. The type of RNA which gets involved in the transform of amino acid in protein synthesis
is ______
32. The nitrogenous base present in cephalin is _______
33. Nucleotide is composed of nucleoside and ______
34. The alcohol soluble proteins are known as _____
35. Nucleotide is _____form of nucleoside
36. _____ is a nitrogenous base present only in DNA and not in RNA
37. In double helical DNA, the number of adenine is equal to ______which are connected by
_____ bonds
38. ______ is the only amino acid lacking an asymmetric carbon atom
39. In amino acid, the 2nd and 4th carbon atoms from COOH group are called _____ and
_____ respectively
40. Interpolypeptide H- bonding results in ______structure
41. The amino acid which break helical structures is_____
42. Histones contain a high proportion of ______ amino acid and are present in _______
43. _______ and _______ are proteins which are example of primary structure
44. The type of structure found in silk and wool are _____and ______
45. _______ and _______are proteins which are example of quaternary structure
46. _________ is the type of configuration found in amino acids
47. ______ and _______are the colors produced in Millon’s test and biuret test
48. The protein content is very high in ____and low in ______
49. All naturally occurring amino acids belong to ______ series
50 Tyrosine is a _________
51 The limiting amino acid in cereals is _______
52 Nucleotide consists of _______
53 Peptide linkage is present in _______
54 The building blocks of proteins are_______
55 Methionine is a ______
56 The primary function of protein is to provide________
57 Globulin is a ________
58 The neutral amino acid has _________
59 At isoelectric point, the protein solution has_______
60 Aspartic acid is a ________
61 The methionine is limiting in _________
62 Adenosine is a _____
63 DNA contains two polynucleotide chains running in ________
64 The first nucleotide derivatives acts as precursor for the synthesis of carbohydrates is
______
65 Prolamins are soluble in _________
66 Tryptophan belongs to the amino acid group of________
67 Among the three types of RNA present in the living system, the tRNA represents
about_______
68 Amphoteric nature of proteins is because of both _________ and _______
69 RNA is usually occurs_______
70 An example for conjugate protein is ______
71 Prolamins are a group of plant _____ protein
72 Uracil base has the related compounds nucleoside and nucleotide as_________
73 Nucleic acid consists of________ sugar
74 Simple proteins on hydrolysis yield ________
75 Amides ( RCONH3) are derivatives of _________
76 An example Heterocyclic amino acid is_______
77 Amino acids having both amino and carboxylic group is known as_____
78 Albumins is a ________ protein
79 The covalent linkage in the primary structure of protein is_________
80 Xantro proteins test is used to find out________ amino acid
81 L-aspartyl-L-phenyl alanine is an example of________
82 Alcohol soluble proteins are known as________
83 Glutathione is having ________ peptide bond
84 Cytochrome is an example for ________
85 Pyrimidines bases of RNA are _________ and _________
86 Trypsin is a _______
87 The nitrogenous base absent in RNA is __________
88 Glycine is a optically ______ molecule
89 Nitroprusside test identifies ________
90 Biuret is a _____test for proteins
91 Proteins on complete hydrolysis yield a group of simple organic compounds of low
molecular weight called as ______
92 The non-amino acid portion of a conjugate protein is called as ______
93 __________ an example of phospho proteins
94 Cytochromes are example of _____
95 __________ is a transport protein
96 The first amino acid isolated was________
97 ______ is a non-protein amino acid
98 The secondary structure of proteins is stabilized by_______
99 _________ represents the quaternary structure of proteins
100 The common name for 6 amino purine is________
101 Ribosome is an example for _______ proteins
102 Egg albumin is an example for______
103 The amino acid which is most likely to disturb alpha helix is _______
104 Amino acid can form disulphide bonds is ________
105 The repeating units in protein is _________
106 The primary structure of proteins represents ______
107 Peptide bond is a ________
108 The first protein sequenced by Fredrick sanger is ________
109 A dipeptide bond has ________
110 Myoglobin is a ____
111 Alpha helix has___________
112 The 3D structure of protein can be determined by _______ and _______
113 _________ is both glycogenic and ketogenic amino acid
114 _______- amino acid is precursor for niacin
115 The first amino acid formed in a polypeptide chain is _______
116 The amino acid having buffering capacity is _________
117 The 21st amino acid is _______
118 The limiting amino acid in pulses is _______
119 All the amino acids found in protein except Proline contains ____
120 Ionic state of amino acids depends upon_____
121 _________ has an imino (>NH) group instead of amino group (‐NH2)
122` Compound that give negative test with Ninhydrin and positive test with benedict’s
Solution.is ____
123 Proteins when heated with concentric acid give a yellow color is provided by ___test
124 Gene is a segment of ________
125 Nucleic acids are polymers of ______
126 The reason for double helical structure of DNA is operation of _______
127 The base is present in RNA but not in DNA is ________
128 Each polypeptide in a protein has amino acids linked with each other in a specific
sequence. This sequence of amino acids is said to be _________
129 In fibrous proteins, polypeptide chains are held together by______
130 DNA and RNA contain four bases each._________ base is not found in RNA
131 .Amino acids and Protein tests include ________
132 Two amino acids of the standard 20 contain sulfur atoms. They are___ and _____
133 Example of non-protein amino acid is ________
134 Amino acid which synthesizes many hormones is: _______
135 An amino acid not found in proteins is_____
136 Sakaguchi’s reaction is specific for________
137 The most dominant amino acid present in proteins is ___
138 GAG triplet codon and is a __________
139 Beta pleated sheet is a _______ protein structure
140 The partial or complete disorganization of a protein’s three-dimensional shape is called
_____

ANSWER
Sl.No Answer Sl.No Answer
1 Amino 34 Prolamins
2 Iso electric point 35 Phosphorylated
3 Albumins 36 Thymine
4 Methionine, Cystine, Cysteine 37 Thymine, H bonding
5 Aromatic 38 Glycine
6 Insulin 39 β,€
7 Lysine, Arginine 40 Secondary
8 6.25 41 Proline
9 Phenyl alanine,Tryosine 42 Basic, Nuclei
10 Histidine 43 Myoglobin, Insulin
11 Trypsin, Pepsin 44 α- secondary, β-secondary
12 Peptide 45 Haemoglobins, Myoglobin
13 Albumins 46 L type
14 16% 47 Red, violet
15 Amino acids 48 Pulses, Cereals
16 Aspartic acid and glutamic acid 49 Aliphatic
17 Biuret test 50 Aromatic amino acid
18 Protamines 51 Lysine
19 Sulphur 52 Nucleoside + H2PO4
20 Simple proteins 53 Proteins
21 Collagens/ Elastin/ Keratins 54 Amino acids
22 Histidine ,Lysine 55 S containing amino acid
23 Isoelectric point 56 Amino acids
24 Salt soluble 57 Water insoluble proteins
25 Storage 58 One NH2 and one COOH group
26 H bonding 59 Zero charge
27 Isoelectric 60 Dicarboxylic acid
28 Thymine/ Cytosine/ Uracil 61 Pulses
29 Nucleic acid 62 Adenine + ribose
30 Adenine, Guanine 63 Opposite
31 t-RNA 64 UDPG
32 Serine/Ethanolamine 65 60-90% alcohol
33 Orthophosphoric acid 66 Heterocyclic amino acid
67 15% 106 Sequence of amino acids
68 Both basic and acidic properties 107 Covalent bond
69 single stranded helix 108 Insulin
70 Nucleoproteins 109 two amino acids
71 Simple 110 hemeproteins
72 Uridine and uridylic acid 111 Coil of amino acid chain
73 Four pentose 112 NMR Spectroscopy and X-Ray Crystallography
74 α amino acid 113 Isoleucine, Phenylalanine, Tryptophan, Tyrosine
and Threonine.
75 Amino acids 114 Tryptophan
76 Proline 115 Methionine
77 Zwitter ions 116 Histidine
78 Simple proteins 117 seleno cystenine
79 Peptide bond 118 Lysine
80 Aromatic amino acid 119 Amino
81 Dipeptide 120 pH
82 Prolamins 121 NH2
83 Penta 122 A monosaccharide
84 Chromo proteins 123 Xanthoproteic acid
85 Cytosine and Uracil 124 DNA
86 Carboxy peptidase 125 nucleotide
87 Thiamine 126 hydrogen bonding
88 Inactive 127 uracil
 89 S-amino acid 128 Amide bond
90 General 129 disulphide cross bridges
91 Amino acid 130 Thymine
92 Prosthetic group 131 Six
93 Casein 132 Methionine and cysteine
94 Haemoproteins 133 carnitine, GABA, Levothyroxine)
95 Carrier protein 134 Tyrosine
96 Glycine 135 8
97 Beta alanine 136 Test for arginine
98 H bonding 137 Glycine
99 Haemoglobins 138 Protein
100 Adenine 139 Tertiary
101 Nucleoprotein 140 Denaturation
102 Storage protein
103 Proline
104 cysteine
105 Amino acids with different R

DEFINITIONS
1. Protein: Any of a class of nitrogenous organic compounds which have large molecules
composed of one or more long chains of amino acids and are an essential part of all living
organisms,
2. Amino acid: A simple organic compound containing both a carboxyl (—COOH) and an
amino (—NH2) group.
3. Essential amino acid: An essential amino acid, or indispensable amino acid, is an amino
acid that cannot be synthesized de novo (from scratch) by the organism, and thus must
be supplied in its diet
4. Peptide bond: A peptide bond is a chemical bond formed between two molecules when
the carboxyl group of one molecule reacts with the amino group of the other molecule,
releasing a molecule of water
5. Zwitterion: Zwitterion is the dipolar form of an amino acid which occurs when H + ion
is transferred from an acid group to an amine group.
6. Simple proteins: Simple proteins yield on hydrolysis, only amino acids.
7. Salting out: Process where albumins may be precipitated out from solution using high
salt concentration
8. Conjugated protein: These are simple proteins combined with some non-protein
substances known as prosthetic groups
9. Denaturation: Denaturation is a process in which proteins or nucleic acids lose the
quaternary structure, tertiary structure and secondary structure which is present in their
native state, by application of some external stress or compound such as a strong acid or
base, a concentrated inorganic salt, an organic solvent
10. Biuret reaction: A compound, which is having more than one peptide bond when treated
with Biuret reagent, produces a violet colour. This is due to the formation of coordination
complex between four nitrogen atoms of two polypeptide chains and one copper atom
11. Amphoteric nature of proteins: Amino acids due to the presence of their ionizable α-
amino and α-carboxylic group can act sometimes as acids and sometimes as bases
depending on the pH of their media.
12. Genetic code: The means by which DNA and RNA molecules carry genetic information
in living cells.
13. Nucleotides: A compound consisting of a nucleoside linked to a phosphate group.
Nucleotides form the basic structural unit of nucleic acids such as DNA.
14. Nucleoside: A compound (e.g. adenosine or cytidine) consisting of a purine or pyrimidine
base linked to a sugar.
15. DNA: Deoxyribonucleic acid, a self-replicating material which is present in nearly all
living organisms as the main constituent of chromosomes. It is the carrier of genetic
information.
16. RNA: Ribonucleic acid, a nucleic acid present in all living cells. Its principal role is to
act as a messenger carrying instructions from DNA for controlling the synthesis of
proteins
WRITE SHORT NOTES ON:
1. Essential Amino Acids
Essential amino acids are those which cannot be synthesized in the body in adequate
amounts and must be supplied from outside as part of food. The presence of these amino
acids is essential for growth of the young and maintenance of the adult. The essential
amino acids are 1) lysine 2) Tryptophan 3) Histidine 4) Leucine 5) Phenyl alanine 6) Iso-
leucine 7) Threonine 8) Methionine 9) Valine and 10) Arginine
2. Basic Amino Acids
Based on the composition of the side chain, the twenty amino acids may be grouped in
to 8 categories. Out of this is basic amino acids where it possess amino group in side
chain eg., Lysine and arginine Basic amino acids are polar and positively charged at pH
values below their pKa's, and are very hydrophilic. Even though the basic amino acids
are almost always in contact with the solvent, the side chain of lysine has a marked
hydrocarbon character, so it is often found near the surface, with the amino group of the
side chain in contact with solvent.
H3N- CH2-CH2-CH2-CH2-CH-COOH
NH2
Lysine ( Lys)
3. Biological properties of Proteins
Proteins are of utmost significance to biological systems. These are most critical to life
and perform various functions. Many proteins act as a catalyst to enhance the rate of
chemical reactions. The fibrous proteins act as structural proteins holding the skeletal
elements. Proteins also perform transport functions. Various proteins are known to be
hormone which regulates the growth of the plants and animals. Some proteins like snake
venom act as toxic one which degrade enzymes. Regulatory proteins regulate cellular or
 metabolic activities. Proteins defend against other organisms. Proteins provide nutrition
to growing embryos and store ion which act as storage proteins,
4. Peptide bonds
The amino acid unit is linked together through the carboxyl and amino group to produce
the primary structure of the protein chain. The bond between two adjacent amino acids
is a special type of amide bond known as the peptide bond and the chain thus formed is
called as peptide chain. A single peptide bond is formed when two amino acids involved
in a reaction and the carboxyl group of one amino acid react with the amino group of
another amino acid, with elimination of one molecule of water. Depending up on the
number of amino acid involved in the reaction, the compound is known as Dipeptide (two
amino acid with one peptide bond), a tripeptide (three amino acid with two peptide bond)
or a polypeptide (many (n…) amino acids with n-1 peptide bonds) where n is number of
amino acids. When a polypeptide chain is formed, one free amino and one carboxyl
group is left at the two different ends. The free amino end is called as N terminal and the
free carboxyl end is called as C-terminal

H H H H
R—C- COOH + HNH—C- R1 R- C-CO-NH- C- R1
NH2 COOH NH2 COOH
Peptide bond
Dipeptide

5) Nucleic acids
The nucleic acids are biopolymers of high molecular weight with mono nucleotide as
their repeating units. The nucleic acid contains carbon, hydrogen, oxygen, nitrogen and
phosphorus. The nucleic acids are of considerable importance in biological systems.
They are two types 1) RNA (Ribose nucleic acid) 2) DNA (Deoxyribose nucleic acid).
The basic chemical subunits of the nucleic acids are nucleotides. The nucleotides are
made of 3 compartments 1) A heterocyclic ring containing nitrogen and nitrogenous base
2) a five carbon pentose sugar 3) A phosphate group. The bases found in nucleic acid are
of two types- Purines and Pyrimidines. Adenine and guanine are purines and cytosine
and Uracil and thymine are pyrimidines bases. The nucleotides found in nucleic acids are
much fewer in number than the amino acids. Ribose nucleic acid is also of common
occurrence in plants as well as animals. It is of three types 1) r-RNA,2) m-RNA 3) t-
RNA .RNA is intimately associated with protein synthesis and are found chiefly in
nucleolus in the nucleus. (Ribosomes and cytoplasm). Besides this, RNA also occurs in
mitochondria and chloroplast. All plant virus contains RNA. DNA which is the seat of
all the hereditary characters is chiefly found in chromatin in the nucleus where it is
associated with proteins called as histones. Some DNA is also found in mitochondria and
chloroplast. DNA is a poly nucleotide having a specific sequence of deoxyribonucleotide
 units covalently joined through 3', 5'phosphodiester bonds, two of the polymers wind
around each other, like the outside and inside rails of winding staircase (double helical
compound).
6 Lipoproteins
It is a conjugate protein. They are complexes of lipids and proteins. The common lipids
which are found as prosthetic groups are lecithin and cephalin. They are insoluble in
water and are found in the membrane, nucleus and lamellas of the chloroplast. A lipid
protein aggregate that serves to carry water- insoluble lipids in the bood. Egg yolk
contains lipoproteins.
7) RNA
Ribose nucleic acid (RNA) is a single stranded structure consisting of only one
polynucleotide chain. RNA consists of the following bases 1) Adenine and Uracil 2)
Guanine and Cytosine. The ratio of purines and pyrimidines bases is not 1:1. The pentose
sugar is β-D-ribose. The size of the RNA molecule is very small in comparison to the
DNA molecule. Molecular weight of RNA may range from several thousands to some
lakhs. There are 3 types of RNA’s in plant cells.
a) Messenger RNA (mRNA)
Molecular weight of mRNA is higher among different types of RNA’s. m-RNA is
synthesized in nucleolus and after taking genetic information from DNA goes into
cytoplasm and helps in the formation of specific protein. Sequence of 3 bases or
nucleotides in m-RNA molecule constitutes a codon.
b) Ribosomal RNA( r-RNA)
r-RNA is found in Ribosomes which act as template for the synthesis of protein
c) Transfer RNA (t-RNA)
Basic structure of all t-RNA molecules is on the clover leaf pattern. T-RNA are found in
cytoplasm and consists of only about 80 bases. t-RNA contains many unusual bases and
nucleosides. There are different t-RNA molecules with specific anticodons to pick up
specific amino acids. However many t-RNA may be specific to a particular amino acids
are single t-RNA species may recognize several amino acids.
8) Chemical properties of proteins
1) Hydrolysis:
a) By acidic agents- Proteins up on hydrolysis with concentrated HCl at 100- 110oC
for 6 to 20 hours yield amino acid in the form of their hydrochlorides
b) By alkaline agents – Proteins may also be hydrolyzed by 2N NaOH
c) By proteolytic enzymes- Certain proteolytic enzymes like pepsin and trypsin
hydrolyze the proteins under certain conditions of temperature and acidity
2) Reaction involving COOH group
a) Reaction with alkalies (salt formation) - The carboxylic group of amino acids
can release H+ ion with the formation of carboxylate (COO-) ions. These may be
neutralized by Na, Ca to form salts
R-CHNH2-COOH + NaOH R-CHNH2-COONa + H2O
b) Reaction with alcohol (Esterification) - Proteins reacts with alcohol to form
Corresponding esters. These esters are volatile than amino acid
R-CHNH2-COOH + C2H5OH R-CHNH2-COO. C2H5 + H2O
c) Reaction with amines – Amino acid reacts with amines to form amides
R-CHNH2-COOH + NH2-R1 R-CHNH2-CO-NH- R1 + H2O
3) Reaction involving amino group:
a) Reaction with mineral acids (Salt formation)- When free amino acids or proteins
are treated with mineral acids like HCl, the acid salts are formed
R-CHNH2-COOH + HCl R-CH-COO.H
NH2HCl
b) Reaction with formaldehyde- With formaldehyde, the hydroxy-methyl derivatives
are formed. These derivatives are insoluble in water and resistant to microbial attack
R-CHNH2-COOH+ H- C-H= O R-CHNH-CH2OH-COOH (N monomethylol
derivatives)
R-CHNH-CH2OH-COOH + H- C-H= O R-CH-COOH
NH(CH2OH)2(N-dimethylol derivatives)
c) Reaction with benzaldehyde (Schiff’s base are formed)
R- CH- COOH + C6H5-CHO R- CH- COOH + H2O
NH2 N=HC-C6H5
d) Reaction with nitrous acid – The amino acids react with HNO2 to liberate N2 and
to produce the corresponding α- hydroxy alcohol
R- CH- COOH + HNO2 R- CH- COOH + N2 + H2O
NH2 OH
e) Reaction with acylating agents (acylation) – Acylation is brought about by many
acid chlorides
4) Reaction involving both COOH and NH2 groups
a) Ninhydrin test- It is powerful oxidizing agent and causes oxidative
decarboxylation of α- amino acids producing CO2, NH3 and aldehyde with one less
carbon atom than the parent amino acids. The reduced Ninhydrin then react with the
liberated NH3 forming blue colored complex
9) Conjugate proteins
These proteins on hydrolysis yields amino acid plus some non-amino acid part called as
the prosthetic group. Depending up on the nature of the prosthetic group associated with
them, conjugate proteins are classified as follows.
a) Nucleoproteins ( histones)- These are associated with nucleic acids
b) Glycoproteins- These are associated with some carbohydrates
c) Chromoprotein – These proteins are associated with some coloring matter eg.
Chlorophyll, carotenoids
d) Lipoproteins – These are associated with lipids or fatty substances eg., cephalin,
lecithin
e) Iron-prophyrin proteins – These are associated with iron-prophyrin compound eg.,
cytochromes
f) Simple metal containing proteins- These are associated with some metals directly
eg., ferredoxin
g) Flavoprotein – These are associated with some Flavin compounds eg., FAD

10) Color reaction of proteins

a) Biuret test: compounds having peptide bonds produce a purple color on reaction with
alkaline copper sulfate solution. The color deepens as the number of peptide bonds
increases and proteins produce blue- violet
b) Xanthoproteic test: Yellow color develops on boiling proteins with concentrated
nitric acid due to the presence of benzene rings. Thus reactions is due to the nitration
of the phenyl rings (tyrosine)
c) Millon’s test: Red color develops when proteins are heated with silver nitrate in nitric
acid
d) Nitroprusside test: Red color develops with sodium Nitroprusside in dilute ammonia
(Cysteine specific)
e) Hopkins- Cole test: Violet rings develop on addition of concentrated sulphuric acid
at the junction of proteins and glyoxylic acid solution

11) Classification of proteins based on solubility

Simple proteins are those which on hydrolysis yields only amino acids. On the basis of
solubility property, simple proteins are classified as
a) Albumins – soluble in water and salt solution
b) Globulins- sparingly soluble in water but soluble in salt solution
c) Prolamins- soluble in 70-80% alcohol but insoluble in water and absolute alcohol
d) Glutelins- Insoluble in water, salt and alcohol but soluble in acid and alkali
e) Scleroproteins- insoluble in aqueous solvents (found in animals only)
12) Distinguish between RNA and DNA
Sl. no DNA RNA
1 Visually double stranded structure Single stranded structure
2 Bases are adenine, guanine, Uracil Bases are adenine, guanine, thymine
and cytosine and cytosine
3 Pentose sugar is β-D-Ribose Pentose sugar is β-D-2 deoxy ribose
4 Found only in the chromatin of the Found in cell cytoplasm
cell nucleus
5 Never present in free state May be present in free state
6 It is alkali stable It is alkali labile
7 It act as template for its synthesis It does not act as template for its
synthesis
8 It undergo mutation It does not undergo mutation
9 It is usual genetic material It is genetic material for some viruses
only
10 It stains green with dye pyronins It stained red with pyronins
13) Secondary structures
Polypeptide chain of the protein molecule is held in a coiled or helical shape by hydrogen
bonds which are established in between peptide linkages. This coiled or helical shape of
polypeptide chain constitutes the α- helix or secondary structure of proteins. Based on
the nature of hydrogen bonding, two regular types of secondary structure in proteins-
alpha helical and beta pleated sheet. Although hydrogen bonds are very weak but when
they are present in very large number all along the backbone of the polypeptide chain,
they reinforce one another to stabilize the helical structure eg., silk and wool
14) Amphoteric nature of proteins
Proteins act as acid or alkali or both. These migrate in an electric field and the direction
of migration depends on the net charge possessed by the molecule. The net charge is
influenced by the pH value. Each protein has a fixed value of isoelectric point at which
it will move in an electric field. Isoelectric point is the pH value at which the number of
cations and anions are equal. Thus, at isoelectric point, the net charge of a protein is
always zero. But the total charge of proteins at this point is always maximum. The
proteins are dipolar ions or Zwitter ions. At pH value less than the isoelectric point, the
proteins will have net positive charge and as a cation will migrate towards negative pole.
Similarly, at pH value higher than isoelectric point, the proteins will have a net negative
charge and as a anion will move towards positive pole
R Acidic R
H- C- COOH H- C—NH2 + H+
NH2 COO-
 R - HCl R
H- C- COOH H- C—NH3++ Cl-
NH2 + HCl COO-
Basic
15) Genetic code
The language of the genes. The set of triplet code words in DNA (or m-RNA) is the code
for the amino acids of proteins. Of the 64 possible codons, 61 are the codes for the amino
acids and the remaining being termination codons that are not translated. All the genetic
information is encoded in DNA which produces hereditary characters in all the living
beings. The sequence of 3 nucleotides in polynucleotide chains of DNA molecule is
called as triplet code. In m-RNA molecule, this sequence of 3 nucleotides is
complimentary to the sequence of nucleotides in DNA and is called as codon. There are
different codons for different amino acids. The latter are incorporated in a particular
protein through specific t-RNA molecules with specific anticodons. Anticodon is
complimentary to codon. A list of all the codons which specify amino acid constitutes
the coding dictionary or genetic code. Genetic code can degenerate. It is not overlapping.
The first and second letters of codon are more important than third in specifying an amino
acid.
16) Denaturation of proteins
Denaturation refers to the changes in the properties of a protein. In other words, it is the
loss of biological activity. Denaturation may be brought about by a variety of agent’s
viz., physical agents (heat, cooling and freezing, rubbing, UV ray) and chemical agents
(ionizing radiation, organic solvents). Denaturation mainly leads to the unfolding of the
peptide chain, thus causing disorganization of the internal structure of proteins.
Denaturation of proteins causes decrease in solubility, cessation of biological activity,
decrease in size and shape of molecule, change in optical rotation in the direction of
increased levorotations, alteration in the surface tension and loss of antigenicity. Some
proteins, when denatured cannot be brought back to the original state. Such cases
Denaturation is irreversible. The process of regaining normal protein properties by
denatured protein is called as Denaturation or refolding.
17. Solubility of proteins
The solubility of proteins is markedly influenced by pH. Solubility is lowest at isoelectric
point and increases with increasing acidity or alkalinity. This is because when the protein
molecules exists as either cations or anions, repulsive forces between ions are high since
all the molecules possess excess charges of the same sign. Thus, they will be more soluble
than in the isoelectric state. Globulins are sparingly soluble in water but their solubility
is greatly increased by the addition of neutral salts like NaCl. It is referred to as salting
in effect. Proteins are precipitated from aqueous solution by high concentration of neutral
 salts. This is the salting out process. Divalent and trivalent ions are more effective than
univalent ions.
ESSAY TYPES
1 How are proteins classified based on solubility and functions?
Proteins are classified based on solubility as follows
a) Albumins- It is soluble in water and dilute solutions of acids, bases and salts. It is
precipitated with neutral salts, coagulated by heat. It is widely distributed in nature and
more abundant in seeds.
b) Globulins- It is widely distributed in nature, insoluble in water, soluble in salt solution
c) Glutelins- Isolated from plant seeds, insoluble in water, salt solution but soluble in
acid and alkali, coagulated by heat eg., glutenin( Wheat)
d) Prolamins- It is insoluble in water and dilute salt solutions but soluble in dilute acids
and alkalies and also in 60-80% alcohol solution, not coagulated by heat eg., Hordein of
oats
e) Protamines- These are basic proteins and occur almost entirely in animals. It is
soluble in water, not coagulated by heat, form salt with acid and alkali
f) Scleroproteins- it occur almost entirely in animals. It is insoluble in water , dilute
solutions of acid, bases and salts, 60-80 % alcohol
Proteins based on function
1. Enzyme proteins- It is highly specialized protein having catalytic activity- the
enzymes. It catalyzes a variety of reactions. Most of the enzymes are globular proteins
eg., urease, amylase and catalase
2. Structural proteins- It is inert to biochemical reactions. The cell wall and primary
fibrous constituents of the cell have structural proteins eg collagen, keratin and fibroin
3. Transport or carrier proteins – Certain proteins in animals are involved in the
transport of many essential biological factors to various parts of the organisms eg.,
Haemoglobins
4. Nutrient or storage proteins. Ovalbumin is the major protein of egg white. The milk
protein casein stores amino acids. The seeds of many plants store nutrient proteins
required for the growth of the germinating seedlings
5. Contractile or motile proteins- Some protein endow cell and organisms with the
ability to contract to change shape or to move about eg., actin and myosin
6. Defense proteins – Many proteins defend organisms against invasion by other species
or protect from injury eg., Antibodies
7. Regulatory proteins- Some proteins help regulate cellular or physiological activity.
Among them are many hormones eg., insulin- regulate sugar metabolism
8. Toxic proteins- Some proteins acts as a toxic substance eg., snake venom
2) Describe the protein biosynthesis process or describe activation, initiation,
elongation and termination steps in protein synthesis
Protein synthesis in plants is under the direct control of DNA. The various steps involved
in protein synthesis in plants is as follows
 1) DNA in the nucleus directs the synthesis of m-RNA and provides with it with
necessary genetic information in the form of codons for the formation of specific
proteins. This process is called as transcription. m-RNA is synthesized in the presence
of enzyme RNA polymerase
2) m-RNA molecules moves into the cytoplasm where it causes the formation of specific
t-RNA molecules having specific anticodons complementary to codons
3) m-RNA becomes associated with the ribosomes which act as template for protein
synthesis. At this template energy is supplied by GTP ( Guanosine phosphate)
4) t-RNA molecules picks up a specific amino acid by its C_C_A end after the amino
acid has been activated by ATP in the presence of specific enzyme ( activation of amino
acid)
O
R- CH- COOH + ATP + enzyme Enz- (R-C H-C-AMP) + Pyrophosphate
NH2 NH2
+ t-RNA
R-C H-C- O- t-RNA+ enzyme + AMP
NH2¬ O
Amino acid attached to t-RNA
5) In bacteria E coli the 70S ribosomes dissociates into 30S + 50S subunits
6) 30 S subunits of the ribosomes recognizes the 51 terminal end of m-RNA from where
the protein synthesis ie., the formation of polypeptide chain starts.
7) 30S subunits also recognize t-RNA amino acid complex which is then transferred to
50S subunit
8) 30S and 50S subunits of the ribosomes unit in the presence of Mg2+ ions and become
associated with m-RNA
9) t-RNA amino acid complex attached to the ribosome is placed opposite to the specific
codon on m-RNA molecule due to the presence of its complementary anticodons in
t-RNA molecule
10) Ribosomes and the m-RNA move relative to each other. When ribosome reach second
codon, another specific t-RNA amino acid complex is attached to the ribosomes so that
its anticodon is placed opposite its complementary codon
11) A peptide bond is established between the carboxylic and amino group of two amino
acid in the presence of the enzyme peptide synthetase. The preceding t-RNA molecule
is released into the cytoplasm to become charge again with amino acid
12) In the same way, during the movement of the m-RNA and ribosome, a number of
specific amino acids are added one after another into the growing polypeptide chain
13) Polypeptide chain remain attached to the 50S subunit till it is complete
14) Termination of the polypeptide chain takes place when ribosomes come over the non-
sense codon in m-RNA molecule during its movement against m-RNA. Nonsense or
chain termination codons are UAA, UAG, UGA
 15) Polypeptide chain produced on the same m-RNA may be of one or more types
depending upon whether m-RNA is monocistronic and polycistronic
16) After formation of polypeptide chains, the m-RNA disintegrates and ribosome again
dissociates into its subunits which are cycled back into the cytoplasm
17) The process in which a particular nucleotide sequence on m-RNA is translated into a
particular amino acid sequence with the help of the ribosomes is called as translation
3) Describe amino acid classification with one example in each group
a) On the basis of the composition of the side chain or R group
1) Simple amino acids – No functional group in the side chain eg., Glycine, alanine
2) Hydroxy amino acids- These contain hydroxy group in their side chain- eg. Serine and
Threonine
3) S containing amino acids- These possess a sulfur atom in the side chain. Eg.
Methionine, Cystine
4) Acidic amino acids- These have carboxyl group in the side chain eg. Aspartic acid,
glutamic acid
5) Amino acid amides- These are derivatives of acidic amino acids in which one of the
carboxyl group has been transformed into an amide group eg. Asparagine, Glutamine
6) Basic amino acids- These possess an amino group in the side chain eg. Lysine, arginine
7) Heterocyclic amino acids- These amino acids have their side chain a ring which possess
at least one atom other than cation- Tryptophan, Histidine
8) Aromatic amino acid- They have benzene ring in the side chain eg. Phenylalanine,
Tryosine
b) On the basis of number of amino and carboxylic group
1) Mono amino-mono carboxylic amino acid- eg., Glycine, alanine
2) Mono amino dicarboxylic amino acid –eg. Aspartic acid, glutamic acid
3) Diamino mono carboxylic amino acid- eg, lysine, arginine
c) On the basis of the polarity of the side chain or R group
1) Amino acid with non-polar R group- This group includes five amino acids with
aliphatic R groups (alanine, valine, leucine, isoleucine, and Proline), two with aromatic
rings (Phenylalanine, Tryptophan) and one S containing amino acid (Methionine). The
R group in this category of amino acid is hydrocarbon in nature, hence hydrophobic
2) Amino acids with polar but uncharged R group- The r groups of these amino
acids are more soluble in water ie., more hydrophilic. This category includes 7 amino
acids- glycine, serine, Threonine, tyrosine, cysteine, asparagines, and glutamine. The
polarity of these amino acids may be due to either a hydroxyl group of a sulfide group
or an amide group.
c) Amino acids with positively charged R groups- These are diamino mono
carboxylic acids, in other words, their side chain contains an extra amino group which
imparts basic properties to them. Eg., Lysine , arginine and Histidine
4) Describe in detail about different types of ribonucleic acids
Ribonucleic acids (RNA) are along unbranched macromolecule consisting of nucleotides
joined by 3'-5' phosphoester bonds. The number of ribonucleotides in RNA ranges from as
few as 75to many thousands. Three general types of RNA are found a) Ribosomal b)
Transfer c) Messenger
a) Ribosomal RNA- It is the most stable form of RNA and is found in Ribosomes. It has
the highest molecular weight, Ribosomal RNA is the most abundant of all types of
RNA’s and makes up about 80% of the total RNA of a cell. Ribosomal RNA represents
about 40 to 60% of the total weight of ribosomes. r-RNA is found in ribosomes which
act as template for the synthesis of proteins
b) Messenger RNA (m-RNA). Molecular weight of m-RNA is higher among different
types of RNA. M-RNA is synthesized in nucleolus and after taking genetic information
from DNA goes into the cytoplasm and helps in the formation of specific proteins.
Sequence of 3 bases or nucleotides in m-RNA molecules constitutes a codon
c) Transfer RNA or soluble RNA( t-RNA or s-RNA)
These are comparatively very small with a molecular weight of about 25000. Basic
structure of all t-RNA molecules is of clover leaf pattern. t-RNA are found in cytoplasm
and consisted of about 80 bases. It constitutes 15-20% of total RNA. t-RNA contain
many unusual bases and nucleosides. All t=RNA molecules contain guanine (G) at 5
'end and 3 end always in base sequence. During protein synthesis these ends in fact
picks up the amino acids and transfer it to the growing polypeptide chain and hence
these RNA’s are called t-RNA. These t-RNA is also called as s-RNA or soluble RNA
because they are soluble in IM NaCl. There are different t-RNA molecules with specific
anticodons to pick up specific amino acids. However many t-RNAs may be specific to
a particular amino acid or a single t-RNA may be recognized several amino acids.
5) Write on chemistry of nucleotides.
Nucleic acid is unbranched long chain polymers of nucleotides. Each nucleotide consist of
3 parts
a) A purine or pyrimidine base
b) An aldopentose sugar
c) Orthophosphoric acid
Nitrogenous bases:
Two types of nitrogenous bases are found in all nucleic acid. These are derivatives of
purines and pyrimidines
a) Pyrimidines derivatives- The common pyrimidine derivatives found in nucleic acid are
1) Uracil- found in RNA only, white and crystalline
2) Thymine- found in DNA only
3) Cytosine- found both in RNA and DNA, white, crystalline
 b) Purine derivatives- These are all derived from their parent compound purines which
contain six membered pyrimidine ring fused to the five member imidazole ring.
1) Adenine- It is found in both RNA and DNA, white, crystalline base
2) Guanine- It is found in both RNA and DNA, colorless, insoluble, crystalline
Pentose sugar
The two types of nucleic acids are distinguished primarily by the basis of the 5 carbon keto
sugar or pentose which they possess. One possesses D-2- deoxy ribose, hence the name
DNA, while the other contain D- ribose, hence the name RNA. Both these sugars in nucleic
acids are present in the furanose form and are β configuration. The two sugars may be
different by means of specific color reactions. Ribose reacts with orcinol in hydrochloric
acid solution containing ferric chloride. Deoxy ribose reacts with diphenylamine in acid
solution. An important property of the pentoses is their capacity to form esters with
phosphoric acid
Phosphoric acid
The molecular formula of phosphoric acid is H3PO4. Combination of a base and pentose
sugar is called as nucleosides. If one of the C atom of the pentose sugar in nucleoside is
phosphorylated is called as nucleotide. The nucleotides are joined together by phosphorus
eater links between carbon number 3 and 5 of the pentose sugar to form long polynucleotide
chains that constitute the nucleic acid.
6) Describe double helix of DNA
Watson and Crick (1953) proposed a model for the structure of DNA molecule. The DNA
molecule is a double helix structure consisting of two long polynucleotide chains coiled
round each other around an imaginary axis and running opposite to each other. Each
polynucleotide chain consists of thousands of nucleotide units. The back bone of the two
helices of polynucleotide chains consists of Deoxy ribose phosphates while the bases are
present on the inner side. The bases of the one polynucleotide chain are complementary to
the bases of other polynucleotide chain and are joined together by hydrogen bonds. The
base pairing is very specific. The complementary bases are 1) Adenine and Thymine 2)
Guanine and Cytosine. The distance between two subsequent bases in the polynucleotide
chain is 3.4 Ao .Each turn of the two polynucleotide chain is completed after 10 bases. The
distance between the axis and the sugar phosphate region is about 10Ao.
7. Classify the proteins giving suitable examples for each group
A) Classification based on the shape of protein molecules:
1) Globular or Corpuscular proteins- They have an axial ratio of less than 10. Hence
possess a relatively spherical or ovoid shape. Usually soluble in water, acid, bases, salts
or alcohol. Eg. Amylase, urease
2) Fibrous proteins- These have axial ratio greater than 10. Hence resemble long fibers
or ribbons in shape, These are mainly of animal origin and insoluble in all common
solvents eg., Collagen
B) Based on composition and solubility
Based on composition, proteins are classified into simple, conjugate and derived
proteins
1) Simple proteins- This group includes proteins containing amino acid as structural
components. On decomposition with acids, these liberate constituent amino acids.
Based on solubility, simple proteins are classified into
a) Albumins- It is soluble in water and dilute solutions of acids, bases and salts. It is
precipitated with neutral salts, coagulated by heat. It is widely distributed in nature
and more abundant in seeds
b) Globulins- It is widely distributed in nature, insoluble in water, soluble in salt
solution
c) Glutelins- Isolated from plant seeds, insoluble in water, salt solution but soluble in
acid and alkali, coagulated by heat eg., glutenin( Wheat)
d) Prolamins- It is insoluble in water and dilute salt solutions but soluble in dilute acids
and alkalies and also in 60-80% alcohol solution, not coagulated by heat eg.,
Hordein of oats
e) Protamines- These are basic proteins and occur almost entirely in animals. It is
soluble in water, not coagulated by heat, form salt with acid and alkali
f) Scleroproteins- it occur almost entirely in animals. It is insoluble in water; dilute
solutions of acid, bases and salts, 60-80 % alcohol
2) Conjugate Proteins:
These proteins on hydrolysis yield amino acids plus some non- amino acid part called
as the prosthetic group. Depending upon the nature of the prosthetic group associated
with them, conjugate proteins are grouped into
1. Nucleoproteins ( histones)- These are associated with nucleic acids
2. Glycoproteins- These are associated with some carbohydrates
3. Chromoprotein – These proteins are associated with some coloring matter eg.
Chlorophyll, carotenoids
4. Lipoproteins – These are associated with lipids or fatty substances eg., cephalin,
lecithin
5. Iron-prophyrin proteins – These are associated with iron-prophyrin compound
eg., cytochromes
6. Simple metal containing proteins- These are associated with some metals
directly eg., ferredoxin
7. Flavoproteins – These are associated with some flavin compounds eg., FAD
 3) Derived proteins
These are derived proteins resulting from the action of heat, enzymes or chemical
reagents
a) Primary derived- The size of the proteins are not altered materially
1) Proteans- Insoluble in water eg., Myosan
2) Metaproteins- Insoluble in water, soluble in acid and alkali
3) Coagulated proteins- insoluble in water, produced by action of heat or alcohol
eg, coagulated egg white
b) Secondary derived- These are derivatives of proteins in which the hydrolysis
has certainly occurred
1) Proteoses- soluble in water, coaguable in heat eg, albumose
2) Peptones- Soluble in water, non- coaguable by heat produced by action of dilute
acids
3) Polypeptides- These are combinations of two or more amino acid units
8) Enumerate the physical and chemical properties of proteins
A) Physical properties
1) Taste and color- Proteins are colorless, homogenous and crystalline
2) Shape and size- Simple crystalloid, spherical to long fibrillar structures
3) Molecular weight- It has large molecular weight ranging from 5 x 103 to 1 x 106
4) Colloidal nature- Because of their giant size, the proteins exhibit many colloidal
properties
5) Denaturation- It refers to the changes in the properties of a protein
6) Amphoteric nature- They act as acid and alkali. Thus the proteins are dipolar or zwitter
ions
7) Ion binding capacity- Being Amphoteric in nature, the proteins can form salts with both
cations and anions based on their net charge.
8) Solubility - The solubility is markedly influenced by pH. It is lowest at isoelectric point
and increases with acidity or alkalinity.
9) Optical activity- All the protein solution rotate the plane of polarized light to the left
(levorotatory)
B) Chemical properties
1) Hydrolysis:
a) By acidic agents- Proteins up on hydrolysis with concentrated HCl at 100- 110oC
for 6 to 20 hours yield amino acid in the form of their hydrochlorides
b) By alkaline agents – Proteins may also be hydrolyzed by 2N NaOH
c) By proteolytic enzymes- Certain proteolytic enzymes like pepsin and trypsin
hydrolyze the proteins under certain conditions of temperature and acidity
2) Reaction involving COOH group
a) Reaction with alkalies (salt formation)- The carboxylic group of amino acids can
release H+ ion with the formation of carboxylate( COO-) ions. These may be
neutralized by Na, Ca to form salts
 R-CHNH2-COOH + NaOH R-CHNH2-COONa + H2O
b) Reaction with alcohol (Esterification) - Proteins reacts with alcohol to form
Corresponding esters. These esters are volatile than amino acid
R-CHNH2-COOH + C2H5OH R-CHNH2-COO. C2H5 + H2O
c) Reaction with amines – Amino acid reacts with amines to form amides
R-CHNH2-COOH + NH2-R1 R-CHNH2-CO-NH- R1 + H2O
3) Reaction involving amino group:
a) Reaction with mineral acids( Salt formation)- When free amino acids or proteins
are treated with mineral acids like HCl, the acid salts are formed
R-CHNH2-COOH + HCl R-CH-COO.H
NH2HCl
b) Reaction with formaldehyde- With formaldehyde, the hydroxy-methyl
derivatives are formed. These derivatives are insoluble in water and resistant to
microbial attack
R-CHNH2-COOH+ H- C-H= O R-CHNH-CH2OH-COOH (N monomethylol
Derivatives)
R-CHNH-CH2OH-COOH+ H- C-H= O R-CH-COOH
NH (CH2OH)2(N- dimethylol
derivatives)
c) Reaction with benzaldehyde (Schiff’s base are formed)
R- CH- COOH + C6H5-CHO R- CH- COOH + H2O
NH2 N=HC-C6H5
d) Reaction with nitrous acid – The amino acids react with HNO2 to liberate N2 and
to produce the corresponding α- hydroxy alcohol
R- CH- COOH + HNO2 R- CH- COOH + N2 + H2O
NH2 OH
f) Reaction with acylating agents (acylation)– Acylation is brought about by many
acid chlorides
R- CH- COOH + CH3COCl2 R- CH- COOH + N2 + HCl
NH2 NH- OCCH3
4) Reaction involving both COOH and NH2 groups
a) Ninhydrin test- It is powerful oxidizing agent and causes oxidative
decarboxylation of α- amino acids producing CO2, NH3 and aldehyde with one less
carbon atom than the parent amino acids. The reduced Ninhydrin then react with
the liberated NH3 forming blue colored complex.
 LIPIDS
Definition
Lipids are organic compounds formed mainly from alcohol and fatty acids combined together
by ester linkage. Lipids are naturally occurring molecules from plants or animals that are
soluble in nonpolar organic solvents

Lipids are insoluble in water, but soluble in fat or organic solvents (ether, chloroform, acetone,
benzene). Lipids include oils, waxes, fats and related compounds. They are widely distributed
in nature both in plants and in animals
Biological Importance of Lipids
They are more palatable and storable to unlimited amount compared to carbohydrates. They
have a high-energy value (25% of body needs) and they provide more energy per gram than
carbohydrates and proteins but carbohydrates are the preferable source of energy. (9, 4.4
Kcal/g). Supply the essential fatty acids that cannot be synthesized by the body. Supply the
body with fat-soluble vitamins (A, D, E and K). They are important constituents of the nervous
system. Tissue fat is an essential constituent of cell membrane and nervous system. It is mainly
phospholipids in nature that are not affected by starvation.
Stored lipids “depot fat” is stored in all human cells acts as:
- A store of energy.
- A pad for the internal organs to protect them from outside shocks.
- A subcutaneous thermal insulator against loss of body heat.
Lipoproteins: which are complex of lipids and proteins, are important cellular constituents that
present both in the cellular and subcellular membranes.
Cholesterol: enters in membrane structure and is used for synthesis of adrenal cortical
hormones, vitamin D3 and bile acids.
Lipids: provide bases for dealing with diseases such as obesity, atherosclerosis, lipid-storage
diseases, essential fatty acid deficiency, respiratory distress syndrome
CLASSIFICATION OF LIPIDS

Simple Lipids
A) Neutral fats or oils (Triglycerides)
Esters of fatty acids with glycerol and monohydric alcohols. Depending upon the constituent
alcohols they are further subdivided into fats or oils and waxes. Fats, also termed as
triacylglycerol are esters of fatty acids with glycerol e.g. Plants- vegetable oils; Animals-ghee
and butter. Waxes are esters of fatty acids and alcohols other than glycerol e.g., Plant wax-
carnauba wax;

Types of triglycerides
a) Simple triglycerides:
If the three fatty acids connected to glycerol are of the same type, the triglyceride is called
simple triglyceride
b) Mixed Triglycerides
If the three fatty acids connected to glycerol are of different type, the triglyceride is called
mixed triglyceride
Natural fats are mixture of mixed triglycerides with a small amount of simple triglycerides.
The commonest fatty acids in animal fats are palmitic, stearic and oleic acids. The main
difference between fats and oils is for oils being liquid at room temperature, whereas, fats are
solids. This is mainly due to presence of larger percentage of unsaturated fatty acids in oils
than fats that has mostly saturated fatty acids
B-Waxes
Waxes are solid simple lipids containing a monohydric alcohol (with a higher molecular weight
than glycerol) esterified to long-chain fatty acids. Examples of these alcohols are palmitoyl
alcohol, cholesterol, vitamin A or D. Waxes are insoluble in water, but soluble in fat solvents
and are negative for Acrolein test. Waxes are not easily hydrolyzed as the fats and are
indigestible by lipases and are very resistant to rancidity. Thus they are of no nutritional value
Physical properties of fat and oils
Freshly prepared fats and oils are colourless, odourless and tasteless. Any color, or taste is due
to association with other foreign substances, e.g., The yellow color of body fat or milk fat is
due to carotene pigments (cow milk). Fats have specific gravity less than 1(one) and, therefore,
they float on water. Fats are insoluble in water, but soluble in organic solvents as ether and
benzene. Melting points of fats are usually low, but higher than the solidification point,
Difference between fat and oil
They are lipids that contain additional substances, e.g., sulfur, phosphorus, amino group,
carbohydrate, or proteins beside fatty acid and alcohol.
Compound or conjugated lipids are classified into the following types according to the nature
of the additional group
a) Phospholipids
b) Glycolipids.
c) Lipoproteins
d) Sulfolipids and amino lipids
A-Phospholipids
Phospholipids or phosphatides are compound lipids, which contain phosphoric acid group in
their structure
Every animal and plant cell contains phospholipids. The membranes bounding cells and
subcellular organelles are composed mainly of phospholipids. Important role in signal
transduction across the cell membrane. They are source of polyunsaturated fatty acids for
synthesis of eicosanoids.
Sources: They are found in all cells (plant and animal), milk and egg yolk in the form of
lecithins.
Structure: phospholipids are composed of:
Fatty acids (a saturated and an unsaturated fatty acid).
Nitrogenous base (choline, serine, threonine, or ethanolamine).
Phosphoric acid.
Fatty alcohols (glycerol, inositol or sphingosine

Classification of Phospholipids
Are classified into 2 groups according to the type of the alcohol present into two types
A-Glycerophospholipids: They are regarded as derivatives of phosphatidic acids that are the
simplest type of phospholipids
Phosphatidic acids: those lipids which on hydrolysis give rise to one molecule of glycerol and
phosphoric acid and two molecules of fatty acids
 1. Lecithins
2. Cephalins.
3. Plasmalogens.
4. Inositides.
5. Cardiolipin

Lecithins
Lecithins are glycerophospholipids that contain choline as a base beside phosphatidic acid.
They exist in 2 forms a- and b- lecithins. The common fatty acids in lecithins are stearic,
palmitic, oleic, linoleic, linolenic, or arachidonic acids.
Cephalins
Cephalins resemble lecithins in structure except that choline is replaced by ethanolamine,
serine or threonine amino acids. Certain cephalins are constituents of the complex mixture of
phospholipids, cholesterol and fat that constitute the lipid component of the lipoprotein.
Inositides
They are similar to lecithins or cephalins but they have the cyclic sugar alcohol, inositol as the
base. They are formed of glycerol, one saturated fatty acid, one unsaturated fatty acid,
phosphoric acid and inositol
B-Sphingo phospholipids
Sphingophospholipids are found in the seeds of several plant species.
Sphingomyelins
Sphingomyelins are found in large amounts in brain and nerves and in smaller amounts in lung,
spleen, kidney, liver and blood. Sphingomyelins differ from lecithins and cephalins in that they
contain sphingosine as the alcohol instead of glycerol, they contain two nitrogenous bases:
sphingosine itself and choline
B-Glycolipids
Glycolipids are structurally characterised by the presence of one or more monosaccharide
residues and the absence of a phosphate. They are lipids that contain carbohydrate residues
with sphingosine as the alcohol and a very long-chain fatty acid (24 carbon series). The
monosaccharides commonly attached are D-glucose, D-galactose or N-acetyl D-galactosamine

.
Protein molecules associated with triacylglycerol, cholesterol or phospholipids are called
lipoproteins The protein part of lipoprotein is known as apoprotein. Lipoproteins occur in milk,
egg-yolk and also as components of cell membranes
Structural lipoproteins
These are widely distributed in tissues being present in cellular and subcellular membranes
Transport lipoproteins:
These are the forms present in blood plasma. They are composed of a protein called
apolipoprotein and different types of lipids. (Cholesterol, cholesterol esters, phospholipids and
triglycerides.

Sulfolipids are a class of lipids which possess a sulfur-containing functional group. The
predominant fatty acid present in sulpholipid is linolenic acid. The sulpholipid is mostly present
in chloroplasts, predominantly in the membranes of thylakoid. Plant sulfolipid is found in the
photosynthetic membranes of plastids and provides negative charge in the thylakoid membrane
where it is thought to stabilize photosynthetic complexes

They occur as such or are released from the other two major groups because of hydrolysis that
is are the building blocks for simple and complex lipids
They include fatty acid and alcohol , Fatty soluble vitamin A,D, E and K, hydrocarbon and
sterols.
Steroids
Steroids constitute an important class of biological compounds
The steroids do not contain fatty acids but are included in lipids as they have fat like properties
Composition: Contain a characteristic arrangement of 3 Cyclohexane ring, 1 Cyclopentane
ring, a total of 17-carbon atoms in four fused Carbon ring.
Classification
Sterol
• Also known as steroid alcohols
• occur naturally in plants, animals, and fungi, with the most familiar type of animal sterol
being cholesterol
• TYPES:
• Phytosterols – plant sterol (campesterol, sitosterol, and stigmasterol)
• blocks cholesterol absorption sites in the human intestine, thus helping to reduce cholesterol
in humans
• Zoosterol – animal sterol (cholesterol)
• Ergosterol – sterol present in the cell membrane of fungi
Examples of steroids:
I) Cholesterol:
• An important component of animal cell membrane.
• Precursor molecule of all hormones such as aldosterone, sex hormone and Vitamin D
• Aldosterone helps to regulate Na+ ions in the blood
• Sex hormones e.g. testosterones, progesterone, oestrogens help to maintain male and female
characteristics
Plant Fatty Acids
They are basic building blocks of lipids (simplest lipids). Fatty acids are carboxylic acids with
a long hydrocarbon chain attached
Definition:
Aliphatic mono-carboxylic acids that are mostly obtained from the hydrolysis of natural fats
and oils.
The general formula R-(CH2)n-COOH and mostly have straight chain (a few exceptions have
branched and heterocyclic chains). "n" is mostly an even number of carbon atoms (2-34)
Structure of fatty acids

A fatty acid consists of a hydrophobic hydrocarbon chain with a terminal carboxyl group
All of the lipid molecules in cell membranes are amphipathic (or amphiphilic) because they
have both polar (Hydrophilic) and non –polar (hydrophobic) portions in their structure
`

1-Saturated Fatty Acids

a. No double bonds with 2-24 or more carbons.
b. Solid at RT except if they are short chained.
c. May be even or odd numbered.
d. Molecular formula, CnH2n+1COOH
Saturated Fatty acids could be:
A-Short chain Saturated F.A. (2-10 carbon).
a - Short chain Saturated volatile F.A.(2-6 C).
b - Short chain Saturated non-volatile F.A.(7-10 C).
A- Saturated- short chain Volatile short -chain Fatty acids:
Liquid in nature and contain 1-6 C water-soluble volatile at room temperature
e.g., acetic, butyric, & caproic acids.
Acetic F.A. (2 C) CH3-COOH.
Butyric F.A. (4 C) CH3-(CH2)2-COOH.
Caproic F.A. (6C) CH3-(CH2)4-COOH
Non -volatile short - chain fatty acids:
Solids at room temperature, contain 7-10 carbons. Water-soluble, non-volatile at RT include
caprylic and capric F.A.
Caprylic (8 C) CH3-(CH2)6-COOH.
Capric (10 C) CH3-(CH2)8-COOH
B - Saturated - Long -chain fatty acids:
<10 carbon atoms.
In hydrogenated oils, animal fats, butter and coconut and palm oils.
Non-volatile, Water-insoluble
E.g. palmitic, stearic, & lignoceric F.A.
o Palmitic (16 C) CH3-(CH2)14-COOH
o Stearic (18 C) CH3-(CH2)16-COOH
o Lignoceric (24C) CH3-(CH2)22-COOH
2 –Unsaturated Fatty Acids
- Contain double bond
A. monounsaturated: they contain one double bond.
(CnH2n-1 COOH)
B. polyunsaturated; they contain more the one double bond
(CnH2n-# COOH).
A-Mono unsaturated fatty acids:
1-Palmitoleic acid:
It is found in all fats. It is C16:1Δ9, i.e., has 16 carbons and one double bond located at carbon
number 9 and involving carbon 10.
CH3-( CH2 )5CH = CH-(CH2)7 –COOH
2-Oleic acid
Is the most common fatty acid in natural fats?
It is C18:1Δ9, i.e., has 18 carbons and one double bond located at carbon number 9 and
involving carbon 10.
CH3-(CH2)7- CH=CH – (CH2)7-COOH
B -Poly unsaturated fatty acids
Definition:
They are essential fatty acids that cannot be synthesized in the human body and must be taken
in adequate amounts in the diet. They are required for normal growth and metabolism
Source: vegetable oils such as corn oil, linseed oil, peanut oil, olive oil, cottonseed oil, soybean
oil and many other plant oils, cod liver oil and animal fats.
Deficiency: Their deficiency in the diet leads to nutrition deficiency disease.
Symptoms: poor growth and health with susceptibility to infections, dermatitis, decreased
capacity to reproduce, impaired transport of lipids, fatty liver, and lowered resistance to stress.
1-Linoleic:
C18: 2D 9, 12.
It is the most important since other essential fatty acids can be synthesized from it in the body.
CH3-(CH2)4-CH = CH-CH2-CH= CH- (CH2)7-COOH
2-Linolenic acid:
C 18:3D 9, 12, 15,
In corn, linseed, peanut, olive, cottonseed and soybean oils.
CH3-CH2-CH=CH-CH2-CH=CH-CH2- CH=CH-(CH2)7- COOH
3-Arachidonic acid:
C20: 4D 5, 8, 11, 14.
It is an important component of phospholipids in animal and in peanut oil from which
prostaglandins are synthesized.
CH3-(CH2)4-CH=CH-CH2-CH=CH-CH2- CH=CH-CH2-CH=CH-(CH2)3-COOH
Common Fatty Acids
Unusual fatty acids
The unusual fatty acids are found only in few individual species or genus or a whole family.
 Castor bean (Ricinus communis) seed oil isrich in ricinoleic acid (90%) which is 12-
hydroxy oleic acid CH3(CH2)5-CH(OH)-CH2-CH=CH-(CH2)7-COOH.
 Rape seed (Brassica napus) is rich in Erucic acid
(cis-13- docosenoic acid)
CH3(CH2)7-CH=CH-(CH2)11-COOH).
 Hydnocarpic and chaulmoogricacids are found in chaulmoogra oil which is used in the
treatment of leprosy
The alkali salt of fatty acid resulting from saponification is soap.
 The soaps we use for washing consists of Na or K salts of fatty acids like palmitic,
stearic and oleic acid.
 The potassium soaps are soft and soluble whereas the sodium soaps are hard and less
soluble in water
The degree of unsaturation of the fatty acids present in triacylglycerol determines whether a fat
is liquid or solid at room temperature. The presence of more unsaturated fatty acids lower the
melting point. The presence of highly unsaturated fatty acids makes the oil more susceptible to
oxidative deterioration. The objective of hydrogenation is to reduce the degree of unsaturation
and to increase the melting point of the oil. The oil can be selectively hydrogenated by careful
choice of catalyst and temperature. Hydrogenation of unsaturated fats in the presence of a
catalyst is known as hardening.
Saturated fats resist rancidity more than unsaturated fats that have unsaturated double bonds.
Definition
Physico-chemical change development of unpleasant odor or taste or abnormal color
particularly on aging exposure to atmospheric oxygen, light, moisture, bacterial or fungal
contamination and/or heat.
1-Hydrolytic rancidity:
From slight hydrolysis of the fat by lipase. Bacterial contamination leading to the liberation of
free fatty acids and glycerol at high temp and moisture .Volatile short-chain fatty acids have
unpleasant odor. Caused by the breaking down of a lipid into its component fatty acids and
glycerol. C-O-CO-R + H2O → C-O-H + HO-CO-R
The water present in the food and the high temperature will increase the rate of hydrolysis to
fatty acids

2-Oxidative Rancidity
Oxidation of fat or oil by exposure to oxygen, light and/or heat producing peroxide derivatives
e.g., peroxides, aldehydes, ketones and dicarboxylic acids that are toxic and have bad odor.
due to oxidative addition of oxygen at the unsaturated double bond of unsaturated fatty acid of
oils.
FILL UP THE BLANKS
1. At room temperature, the liquid fat contains______
2. The chemical process used to in the manufacture of Vanaspati is ______
3. Saponification is ______ process
4. Hydrogenation of oils gives _______
5. Diester linkage are seen in _____-
6. The building blocks of fats are_______ and _______
7. Sterols contain characteristic cyclic nucleus made up of ____ six member ring and _____
five member ring
8. On hydrolysis, fat gives _____ and ________
9. Hydrolytic rancidity of fat is due to the production of ______
10. An example of essential fatty acid is _______
11. The solid fat contains _______ fatty acid
12. _______ is the chemical process involved in the manufacture of soap
13. The solid alcohol present in the plant is known as ______
14. Arachidonic acid contain _______ number of double bonds
15. Among the three compounds, carbohydrate, lipid and proteins, ______ has more calorific
value
16. The higher the unsaturated fatty acid content in oil, ______ will be the iodine value
17. Among oils, ______ has the highest viscosity
18. Vegetable oils are converted to solid fats by the addition of ____ to the double bonds of
the unsaturated fatty acids
19. Iodine number of coconut is ______
20. _______ is an example of antioxidant
21. Fat constant _______ is used to measure the free fatty acids in fat
22. Arachidic acid is saturated non-volatile fatty acids found mostly in _____oil
23. The bile of animals contain the steroid namely _____
24. Example of unsaturated fatty acids are _____ and _____-
25. Lecithin is an example of _____
26. Triacyl glycerol is the ester of _____ with glycerol
27. An example of plant sterol is _______
28. Iodine number indicates the degree of ______in a fatty acid
29. A neutral lipid contains _______ as alcohol
30. ____ and _____ are polyunsaturated fatty acids
31. _______ is used as an indicator in iodine value estimation and the end point is _____
32. The most abundant saturated and unsaturated fatty acids are _____ and _____
33. A fatty acid derivatives reacts with a carbohydrate and a ______ base to form ____lipid
34. The two types of glycolipids occurring in nature are______ and _____
35. As chain length of saturated fatty acid increases the ______ and ______ also increases
36. Chemical reaction of fatty acid due to COOH are ____ and _____
37. Oxidative and hydrolytic rancidity can be known by measuring _____ and ____
38. Naturally occurring fatty acids have ______ configuration
39. Fatty acids with less than 10 carbon atoms are ____ and those with more than 10
are_______
40. Metal salts of fatty acids are called _______
41. Functional group in fatty acid is called _____group
42. When fats are hydrolyzed the cleavage occurs at _____linkages
43. The processes involved in the drying of oils are ____ and _____
44. _____ and ______ are the most common fatty acids present in drying oils
45. The general formula of saturated fatty acid is ______ and unsaturated fatty acid is ____
46. The structural formula of mixed triglyceride is _____
47. Tocopherol is another name for _______
48. _____ is an important sterol which is converted to vitamin D on irradiation by sunlight
49. Simple lipids constitute the major groups ____ and _______
50. _______ is a fat solvent generally used for the extraction of lipids
51. Oxidative rancidity is observed more frequently in ____fat than in ____ fat
52. Hydrolytic rancidity of butter is caused by the action of ____ due to secretion by_____-
53. The antioxidants present in the vegetable oil is ____
54. ____ test forms the basis of presence of glycerol in fat molecule
55. Quantity of free fatty acid present in a fat is indicated by_____
56. Number of double bonds present in fatty acid molecule is noticed by_____
57. The acetyl number is a measure of the number of _______groups in the fat
58. Saponification number is highest in ______
59. The iodine number in linseed oil is ______
60. _____ amount of calories is provided by fat
61. _______ is referred to as essential fatty acid
62. Oils and fats are _____
63. Iodine value measures the extent of _____present in fats and oils
64. _____is used to estimate the amount of linoleic and linolenic acids in fats or oils
65. The development of off flavour in fats is known as ________
66. The enzyme responsible for conversion of fats into fatty acid and glycerol is ____
67. The essential fatty acid present in vegetable fat is _____
68. The fatty acid which contain double bond in its structure is referred to as ____
69. Palmitic acid is a ____fatty acid
70. The unsaturated fatty acid have _____melting point
71. Double bond is observed in ______fatty acid
72. Unsaturated fatty acids containing fats show _____isomerism due to presence of double
bond
73 In the manufacture of soap, the __________ process is involved
74 Richart-Meissel number measures__________ fatty acids
75 The process of hydrogenation of fatty acid yields _______
76 Waxes are __________ lipids
77 Saponification process yields ___________
78 Phospholipid contains ____, ______ and ________
79 Iodine number indicates degree of ________
80 Hydrogenation is_________ hydrogen
81 Manufacture of Vanaspati involves________ process
82 Capric acid occurs in ________ oil
83 The iodine value of groundnut oil ranges from _________ to ____
84 Complex compounds of fatty acid with carbohydrates are called _______
85 At room temperature oils are ________
86 Iodine number is ____ required to neutralize _______of fat
87 Lecithin is a __________ lipid
88 Esters containing fatty acids, alcohol, phosphoric acid and choline are called ____
89 Fat is estimated by ______ method
90 Soaps are products of________
91 Ergosterol is an example of _______
92 Oleic acid is an example of __________ fatty acid
93 When unsaturation is introduced in stearic acid the melting point _______
94 Arachidonic acid is present in _________
95 Fat is ester of fatty acid with _______
96 The name lipid was suggested by _____
97 Nitrogenous base in lecithin is _________
98 Choline is very _____ in reaction
99 Cephalin is a ______ lipid
100 An example of phospholipids is _______
101 _________ is an antioxidant to prevent oxidative rancidity in vegetable oils
102 ________ is common solvent
103 The most abundant member in the group of complex lipid is ______
104 The development of off flavors due to Aspergillus Niger is called as_____
105 The unsaturated fatty acid containing 4 double bond is________
106 The richest source of essential fatty acid is__________
107 The essential PUFA is ________
108 Examples of monosaturated fatty acid is _________
109 Number of double bond in arachidonic acid is _______
110 The fats and oils are rich in __________ and __________ fatty acids
111 __________ fatty acid has16 carbon atoms
112 __________ is a hydroxyl fatty acid
113 _______ storage form of lipid
114 In which form are most lipids found ______
115 The three-carbon "backbone" found in all triglycerides is called: _______
116 A glycerol backbone with one or two fatty acids plus another group, possibly a
phosphorus group, produces a: ________
117 Triglycerides that contain one or more double covalent bonds between carbon atoms of
their fatty acids are called __________
118 Bubbling hydrogen gas through polyunsaturated vegetable oil will cause the oil to
become more__________ and more_______
119 Chemically, fats and oils are _________
120 Palmitoleic acid (16:1) classified as __________ fatty acid.
121 _________ is classified as sterol
122 Most commonly occurring fatty acid in nature is ________
123 In most naturally occurring monounsaturated fatty acids, the double bond will be placed
between _______
124 The number of OH group in fatty acids can be expressed as________
125 The degree of unsaturation of lipids can be measured as _________

ANSWERS
Sl.No Answer Sl.N Answer
o
1 Unsaturated 34 Galactosyldyglyceride, sulpholipids
2 Hydrogenation 35 Carbon and Hydrogen
3 Alkali hydrolysis 36 hydrolysis and Saponification
4 Solid fats- ghee 37 Peroxide value and Lipase enzyme
5 Compound lipid 38 Monocarboxylic with even number of carbon
6 Fatty acid and glycerol 39 Unsaturated and saturated
7 Pyranose, Furanose 40 Soap
8 fatty acid and glycerol 41 COOH
9 Lipase 42 Fatty acid + glycerol
10 Linoleic/Oleic/Linolenic 43 oxidation and cross linking
11 Saturated 44 α linolenic and linoleic
12 Saponification 45 CH2(CH2)n R-CH=CH( CH2)n-COOH
13 Glycerol 46 CH3—OOC-R 1

CH-OOC-R2

CH2-OOC- R3
14 4 47 vitamin E
15 Lipids 48 Ergosterol
16 Greater 49 Fats and waxes
17 Castor oil 50 Ether
18 hydrogen 51 Animal fats, vegetable fat
19 7-10 52 Lipase and microbes
20 Tocopherol 53 Tocopherol
21 Acid value 54 Acrolein test
22 peanut/groundnut 55 Acid number
23 Cholic 56 Iodine number
24 Oleic and Linoleic 57 OH
25 Phosphoglyceride 58 Coconut
26 3 fatty acids 59 170-195
27 Ergosterol 60 9 Kcal
28 Unsaturation 61 PUFA
29 Glycerol 62 Simple
30 Arachidonic and Erucic 63 Unsaturation
31 Starch and blue to 64 Acid value
colourless
32 Palmitic acid, Oleic/linoleic 65 Rancidity
acid
33 Sulphur, Sulpholipid 66 Lipase
67 Linoleic 100 Lecithin
68 Unsaturated 101 Tocopherols
69 Saturated 102 Ethyl alcohol
70 Low 103 Sphingolipids
71 Unsaturated 104 Ketonic rancidity
 72 Cis-Trans 105 Arachidonic acid
73 Saponification 106 Linseed oil
74 Soluble 107 Linoleic acid
75 Dalda 108 Oleic acid
76 Simple 109 4
77 Soap 110 Saturated, unsaturated
78 Fatty acid and glycerol and 111 Palmitoleic acid
H3PO4
79 Degree of unsaturation 112 Ricinoleic acid
80 Addition 113 Cholesterol or triglycerides
81 Hydrogenation 114 triglycerides
82 Coconut oil 115 Glycerol
83 135-194 116 Phospholipid
84 Glycolipids 117 Unsaturated fatty acid
85 Liquids 118 Saturated , solid
86 Gram iodine, 100 g 119 Esters
87 Phospholipids 120 Monosaturated
88 Phospholipids 121 Cholesterol
89 Saponification 122 Lauric , oleic
90 Fat and alkali 123 Two carbon atoms
91 Plant sterol 124 Acetyl number
92 Unsaturated fatty acid 125 Iodine value
93 Decreases
94 Peanut
95 Glycerol
96 Bloor
97 Choline
98 Neutral
99 Phospho

WRITE SHORT NOTES ON:

1) Oxidative rancidity:
Oils containing highly unsaturated fatty acids are spontaneously oxidized by atmospheric
oxygen at ordinary temperature. The oxidation takes place slowly and results in the
formation of short chain fatty acids (C4- C10) and aldehydes which give a rancid taste and
oil or to the fats. This type of rancidity is called as oxidative rancidity and is due to a
reaction called auto oxidation. Oxidative rancidity is observed more frequently in animal
fats than in vegetable fats. This is due to the presence of natural antioxidants in vegetable
fats such as tocopherol, phenols, and napthols which check autoxidation. Vitamin E is
therefore sometimes added to foods to prevent rancidity. The action of antioxidants is
opposed by a group of compounds called as pro oxidants present in fats and oils which
 accelerate the oxidation of the parent compound and these compounds are formed during
the processing and refining of fats eg. Copper, nickel, lactic acid.
1) Phospholipids
It is most abundant membrane lipids, As the name implies, phospholipids contain
phosphorus in the form of phosphoric acid. In phospholipids, two of the OH groups in
glycerol are linked to fatty acid and third OH is linked to phosphoric acid. Phospholipids
are classified into a) Phosphoglycerates b) Phosphoinositides c) Phosphosphingosides.
Phosphoglycerates are the major phospholipids found in membrane and contain two fatty
acid molecules esterified to the first and second OH groups of glycerol and third OH forms
an ester linkage with phosphoric acid. Lecithin, Cephalin and plasmologens belong to this
group. Phosphoinositide is found in brain tissues and are considerable importance because
of their role in transport processes in cells. It is also called as glycolipids since it has much
carbohydrate residues. Phosphosphingosides are commonly found in nerve tissues and
apparently lack in plants and microbes. This differ from other phospholipids in their lack
of glycerol and the presence of another nitrogenous sphingosins besides choline in place
of glycerol.
3. Sterols
It is derived lipids. It does not contain fatty acids. So they are non saponifiable. All steroids
may be considered as derivatives of a fused and fully saturated ring system called as
steranes. Important steroids are sterols, bile acids and hormones. Among the sterols,
cholesterol is important (C27) found in animal fat followed by ergosterol (C28) found in
yeast which is precursor for vitamin D and tanosterol (C30) found in wool fat required for
biosynthesis of cholesterol. The bile acids include cholic acid (C29) present in intestine
and gall bladder required for absorption of fats and chenodeoxy cholic acid. The hormones
include progesterone (C21) found in corpus luteumm Deoxy corticosterone found in
aldrenal coster testosterone (C19) found in testes and esteradiol (C18) present in ovaries.
4. Chemical constants of oils/ fat or Quantitative test of fats or oils
The chemical determination on the nature of fatty acids and the number of hydroxyl groups
present in the fat molecule is referred to as chemical constants which includes the
following
1) Acid value- It is the number of milligrams of KOH required to neutralize I gram of the
oil or fat. It gives about the amount of free acid present in fat or oil
2) Saponification value- It is the number of milligrams of KOH required to neutralize the
fatty acid resulting from the complete hydrolysis of I gram of fat or oil. Higher the
molecular weight of fat or oil, smaller the Saponification value.
3) Iodine value- number of grams of iodine taken up by 100 grams of fat or oil. It gives
an idea on degree of unsaturation
4) RM value- Number of milliliter of 0.1N KOH solution required to neutralize the volatile
soluble acids obtained by the hydrolysis of 5 g of fat. It is used for finding the purity of
butter or ghee. It is lower for adulterated ghee than pure ghee
5) Polenske number- Number of milliliter of 0.1N KOH required to neutralize the
insoluble fatty acid obtained from 5 g fat
 6) Acetyl number- It is number of millilitres of 0.1N KOH required to neutralize the acetic
acid obtained by Saponification of 1 g fat after it has been acetylated. It is the measure of
number of OH groups in fat. Castor oil has got the highest acetyl number (146) because of
high content of hydroxy ricinoleic acid in it
5. Rancidity
Oils and fats on long storage in contact with heat, light, air and moisture develop an
unpleasant odor. Such oils and fats are known as rancid oils and fats. The rancidity
develops due to certain chemical changes taking place in fat. The changes include
1) Enzymatic hydrolysis- In presence of enzymes and microbes, the fats and oils form
bad smell lowering fatty acids
2) Air oxidation of unsaturated fatty acids- During air oxidation, the unsaturated fatty
acid portion of fats are oxidized at the site of the double bonds into aldehyde and ketones
with unpleasant odor
3) β oxidation of saturated fatty acids- The saturated fatty acids undergoes β oxidation
followed by decarboxylation to form ketones of unpleasant Odor
6. Functions of lipids/importance of lipids
1) Fats serve reserve food in seeds
2) Oils are used by human beings for various purposes
3) Lipids provides the structural frame work to the living tissues of plants and animals
4) Lipids provides as the prime fuel reserve for metabolism and provides more energy
than carbohydrates and proteins
5) Fats provides a bridge in filling the gap between water soluble and insoluble phases
6) Waxes give a protective covering on the upper surface of leaves, stems and fruits
7) Certain oils like castor oil, mustard oil, clove oils and coconut oils are used medicinally
8) Other oils are used in the preparation of soaps and vegetable ghee
9) Lipids acts as carrier of natural fat soluble vitamins A D E K
10) The sex hormones, adreno corticoids, cholic acids and vitamin D are all synthesized
from cholesterol
11) Phospholipids play an important role in the absorption and translocation of fatty acids
12) The fats are characterized for their high insulating capacity
7. Compound lipids
The compound lipids consists of phospholipids and glycolipids
A ) Phospholipids:
Phospholipids are those lipids which contains phosphorus. Phosphorus is present in the
form of esterified phosphoric acid. Based on the alcoholic component present, the
phospholipids are classified into
1) Phosphoglyceride (glycerol containing) - It is the largest and most wide spread class. It
is again subdivided into the following groups
i) Phosphatidyl cholines – lecithin, cephalin
ii) Phosphatidyl ethanolamine
iii) Phosphatidyl series
iv) Plasmologens
 v) Phosphatidyl glycerols
2) Phosphoinositides (Inositol containing) – It is made up of glycerol, fatty acid,
phosphoric acid and cyclic hexahydric alcohol mesoinositol. It is divided into i) Mono ii)
Di. Mono is found widely in both plants and animals while Di occur only in brain tissues
3) Phosphosphingosides- It contains a alcohol phytosphingosine in plants and
sphingosine in animals. It differs from phytosphingosine in having double bond
B) Glycolipids
Glycolipids are those lipids which contain carbohydrates. They have been isolated from
different plant sps. Galactosyl diglycerides and sulpholipids form the major Glycolipids in
plants. Galactosyl diglycerides may be mono or di and it has been isolated from chloroplast
of many plants. The plant sulpholipid was discovered by the use of radioactive sulfur by
Benson in the leaves of higher plants. It is made up of glycerol, fatty acid and sugar
quinovose which bears S containing group. The plant sulpholipids contains sulphonic acid
8) Lipoproteins
Lipoproteins are complexes which contain lipids and proteins in association. It is most
important complexes because in the living being they are found in the form of soluble lipid
drops and build the plasma membranes and membranes of various cell organelles. The
membranes of these cell –organelle possess a number of enzymes for biochemical
reactions. The lipoproteins of the membranes may be water soluble or fat soluble. They
help in the entry or exit of water and fat soluble compounds and also maintain the
concentration and equilibrium for such compounds in the cell. The lipoproteins complexes
are affected by agents that influence the purity of proteins such as heat, pH, and other
chemicals. Lipoproteins provide surface for biochemical reactions and energy production
and also help in the transportation of lipids and proteins to the various parts of the plant or
animal body.
9. Fats and oils
It is simple lipids. They are called as triglycerides. It is the most abundant of all lipids.
Chemically triglycerides are esters of glycerol and 3 fatty acids molecules.
CH2-OOCR1

CH2- OOCR2

CH2- OOCR3
In triglycerides, all the three fatty acids molecules may be identical or may be different.
All the fat contains glycerol in common but differs in amount and types of fatty acids.
Triglycerides which contain saturated fatty acids are solid at room temperature and are
called as fats. Other triglycerides which contain unsaturated fatty acids are liquid at room
temperature and are called as oils. Oils can be converted to solid fats by saturating the fatty
acids. This process is utilized in the manufacture of vegetable ghee from oils. The animal
fat such as meat, milk and eggs contain high amount of saturated fatty acids and high
melting point. So it is solid in state. The plant fats contains high amount of polyunsaturated
fatty acids and low melting point, so it is liquid at state.
10. Action of lipase enzyme
The fats are hydrolyzed by the enzyme lipases to yield fatty acid and glycerol. The lipases
catalyses this reaction at a slightly alkaline pH (7.5-8.6) in a step wise manner. The fats
are first split into produce diglycerides, part of these are then split to monoglycerides.
Finally part of the monoglycerides split to yield fatty acids and glycerol
CH2-OOCR1 Lipase CH2-OOCR1
CH2- OOCR2 + H2O CH2- OOCR2 + R3COOH
CH2- OOCR3 H2C- OH
Triglycerides diglycerides fatty acid
CH2-OOCR1 Lipase CH2-OOCR1
CH2- OOCR2 + H2O H2C- OH + R2COOH
H2C- OH H2C- OH
Diglycerides Monoglycerides fatty acid
CH2-OOCR1 Lipase H2C-OH
H2C- OH + H2O H2C-OH + R1COOH
H2C- OH H2C- OH
Monoglycerides Glycerol fatty acid
11) Saponification
Hydrolysis of fat by alkali such as NaOH or KOH leads to the formation of sodium or
potassium salts of fatty acid. These salts are known as soaps and process of its formation
is known as Saponification. The soaps are of two types a) hard b) soft. Hard soap such as
bar soaps is sodium salts of higher fatty acids. Soft soaps are the potassium salts of higher
fatty acids and marketed as semisolids or pastes
CH2-OOCR Lipase H2C-OH
CH2- OOCR + 3 NaOH H2C-OH + 3RCOONa
CH2- OOCR H2C-OH
Fat Glycerol Na salts of fatty acid (Soap)
12. Hydrogenation of fats
Oils containing unsaturated fatty acids can be hydrogenated in the presence of high
temperature, pressure and finally divided nickel. Unsaturated fatty acids either free or
combined in lipids react with gaseous hydrogen to yield the saturated fatty acids. The
addition of hydrogen takes place at the C-C double bonds. Thus one mole of oleic, linoleic
or linolenic acid react with 1,2 or 3 moles of hydrogen respectively to form Stearic acid .
Pu/Pd/Ni
CH3 (CH2)7CH (CH2)7COOH + H2 Catalyst CH3 (CH2)7CH2 –CH2( CH2)7COOH
 This reaction is of great commercial importance since it permits transformation of
inexpensive and unsaturated liquid vegetable fats into solid fats. The latter are used in the
manufacture of candles, vegetable shortening and margarine
13. Physical properties of fats
1) State – Fats containing saturated fatty acid are solid and fats containing unsaturated
fatty acids are liquid at room temperature
2) Color, Odor and Taste- Fats are colorless, odorless and has bland taste
3) Solubility- Fats are soluble in organic solvents like ether, chloroform, benzene and
insoluble in water
4) Melting point- Saturated glycerides containing fat require high temperature for melting
and unsaturated glycerides containing fats require lower melting point.
5) Specific gravity – The specific gravity of fats is less than 1 and therefore they float on
the water surface
6) Geometric isomerism- Unsaturated fatty acids containing fats show cis-trans
isomerism due to presence of double bond
7) Insulation- They are bad conductors of heat
8) Surface tension – Fats redues surface tension
14. Chemical properties
1) Hydrolysis- Fats undergo hydrolysis when they are treated with mineral acids, alkalies,
or fat splitting enzyme lipase or hydrolases to yield glycerol and fatty acid
2). Hydrogenation- Oils containing unsaturated fatty acids can be hydrogenated in the
presence of high temperature, pressure and finally divided nickel. By this oils are
converted to solid fats
3) Hydrogenolysis- Oils and fats are converted to glycerol and a long chain aliphatic
alcohol when excess of hydrogen is passed through them under pressure and in the
presence of copper chromium catalyst. The splitting of fat by hydrogen is called
Hydrogenolysis
4) Halogenation- When unsaturated fatty acids are treated with halogens such as iodine
and chlorine, they take up halogens at the double bond site. This process of taking
iodine is called as halogenation and it is an indication of unsaturation.
5) Rancidity- Oils and fats on long storage in contact with heat, light, air and moisture
develop an unpleasant odor, such oils and fats are called as rancid fats and oils.
6) Emulsification- The process of breaking of large size fat molecules in to smaller ones
is known as emulsification
ESSAY TYPES
1. What are essential fatty acids? Define different chemical constants and their
significance in relation to fatty acid composition in fats and oils
Essential fatty acids are group of polyunsaturated fatty acids produced by plants, but not
by humans, required in the human diet. Following are the chemical constants which give
 valuable information about the chemical nature of fatty acids and number of hydroxyl
groups present in the fat molecule
1. Acid value- It is the number of milligrams of KOH required to neutralize I gram of the
oil or fat. It gives about the amount of free acid present in fat or oil
2. Saponification value- It is the number of milligrams of KOH required to neutralize the
fatty acid resulting from the complete hydrolysis of I gram of fat or oil. Higher the
molecular weight of fat or oil, smaller the Saponification value.
3. Iodine value- number of grams of iodine taken up by 100 grams of fat or oil. It gives
an idea on degree of unsaturation
4. RM value- Number of milliliter of 0.1N KOH solution required to neutralize the
volatile soluble acids obtained by the hydrolysis of 5 g of fat. It is used for finding the
purity of butter or ghee. It is lower for adulterated ghee than pure ghee
5. Polenske number- Number of milliliter of 0.1N KOH required to neutralize the
insoluble fatty acid obtained from 5 g fat
6. Acetyl number- It is number of milliliters of 0.1N KOH required to neutralize the
acetic acid obtained by Saponification of 1 g fat after it has been acetylated. It is the
measure of number of OH groups in fat. Castor oil has got the highest acetyl number ( 146)
because of high content of hydroxy ricinoleic acid in it
2. Write on neutral lipids and their important chemical reactions
The neutral lipids or triglycerides are esters of the trihydric alcohol, glycerol and fatty acids.
In nature, three molecules of fatty acids combines with one molecule of glycerol with the
elimination of three molecules of water. The enzyme lipase catalyses the reaction
CH2 – OH C15H31- COOH CH2OOCC15H31
CH2- OH + C15H31- COOH Lipase CH2OOCC15H31 + 3H2O
CH2- OH C15H31 - COOH CH2OOCC15H31
Glycerol Palmitic acid Tripalmitic acid (fat)
In triglycerides, all the three fatty acids molecules may be identical or may be different. All
the fats contain glycerol in common, but differ in amount and types of fatty acids. The
triglycerides which contain saturated fatty acids are solid at room temperature and are
called fats. Other triglycerides which contain unsaturated fatty acids are liquid at room
temperature are called oils. Most animal fats are rich in saturated fatty acid while plant fats
contain a large proportion of unsaturated fatty acids.
The important chemical reactions are
1) Hydrolysis- Fats undergo hydrolysis when they are treated with mineral acids, alkalies,
or fat splitting enzyme lipase or hydrolases to yield glycerol and fatty acid.
CH2OOCC15H31 CH2 – OH
CH2OOCC15H31 + 3H2O Lipase CH2 – OH + 3 C15H31COOH
CH2OOCC15H31 CH2 – OH
Tripalmitic acid (fat) Glycerol Palmitic acid
 2). Hydrogenation- Oils containing unsaturated fatty acids can be hydrogenated in the
presence of high temperature, pressure and finally divided nickel. By this oils are converted
to solid fats
3) Hydrogenolysis- Oils and fats are converted to glycerol and a long chain aliphatic
alcohol when excess of hydrogen is passed through them under pressure and in the presence
of copper chromium catalyst. The splitting of fat by hydrogen is called Hydrogenolysis
4) Halogenation- When unsaturated fatty acids are treated with halogens such as iodine
and chlorine, they take up halogens at the double bond site. This process of taking iodine
is called as halogenation and it is an indication of unsaturation.
5) Rancidity- Oils and fats on long storage in contact with heat, light, air and moisture
develop an unpleasant odor, such oils and fats are called as rancid fats and oils.
6) Emulsification- The process of breaking of large size fat molecules in to smaller ones
is known as emulsification
7) Saponification- Hydrolysis by alkali such as NaOH or KOH leads to formation of
sodium or potassium salts of fatty acids called as soaps and process of its formation is
known as Saponification
CH2-OOCR Lipase H2C-OH
CH2- OOCR + 3 NaOH H2C-OH + 3RCOONa
CH2- OOCR H2C-OH
Fat Glycerol Na salts of fatty acid (Soap)
3. Explain the classification of lipids with suitable examples
Bloor (1943) classified the lipids based on the chemical composition
A) Simple lipids or homolipids
Simple tripalmitin
a) Fats and oils (Triglycerides)
Mixed

b) Waxes Sperm whale wax

B) Compound lipid or heterolipids
Phosphoglycerides- Lecithin, cephalin
Phospholipids Phosphoinositides-
Phosphosphingosides
Steroids
C) Derived Lipids Terpens- Mono, Di, tri, tetra and poly
Carotenoids- lycopene, carotenes, xanthophylls
4. List the important properties of fatty acids
Physical properties of fats
1) State – Fats containing saturated fatty acid are solid and fats containing unsaturated
fatty acids are liquid at room temperature
2) Color, Odor and Taste- Fats are colorless, odorless and has bland taste
3) Solubility- Fats are soluble in organic solvents like ether, chloroform, benzene and
insoluble in water
4) Melting point- Saturated glycerides containing fat require high temperature for melting
and unsaturated glycerides containing fats require lower melting point.
5) Specific gravity – The specific gravity of fats is less than 1 and therefore they float on
the water surface
6) Geometric isomerism- Unsaturated fatty acids containing fats show cis-trans isomerism
due to presence of double bond
7) Insulation- They are bad conductors of heat
8) Surface tension – Fats redues surface tension
Chemical properties
1) Hydrolysis- Fats undergo hydrolysis when they are treated with mineral acids, alkalies,
or fat splitting enzyme lipase or hydrolases to yield glycerol and fatty acid
2). Hydrogenation- Oils containing unsaturated fatty acids can be hydrogenated in the
presence of high temperature, pressure and finally divided nickel. By this oils are converted
to solid fats
3) Hydrogenolysis- Oils and fats are converted to glycerol and a long chain aliphatic
alcohol when excess of hydrogen is passed through them under pressure and in the presence
of copper chromium catalyst. The splitting of fat by hydrogen is called Hydrogenolysis
4) Halogenation- When unsaturated fatty acids are treated with halogens such as iodine
and chlorine, they take up halogens at the double bond site. This process of taking iodine
is called as halogenation and it is an indication of unsaturation.
5) Rancidity- Oils and fats on long storage in contact with heat, light, air and moisture
develop an unpleasant odor, such oils and fats are called as rancid fats and oils.
6) Emulsification- The process of breaking of large size fat molecules in to smaller ones
is known as emulsification
5. List the saturated fatty acids with their molecular formula and suitable examples
1) Butyric acid- CH3 (CH2)2COOH- butter
2) Caproic acid- CH3 (CH2)4COOH – Butter, palm oil, coconut oil
3) Caprylic acid- CH3 (CH2)6COOH- Palm oil, coconut oil
4) Capric acid - CH3 (CH2)8COOH – Palm oil, coconut oil
5) Lauric acid - CH3 (CH2)10COOH – Lauraceae, palm oil, coconut oil
6) Myristic acid - CH3 (CH2)12COOH – Seed fats, butter
7) Palmitic acid - CH3 (CH2)14COOH – peanut oil, palm oil
8) Stearic acid - CH3 (CH2)16COOH – Plant and animal fat
9) Arachidic acid - CH3 (CH2)18COOH- Peanut oil
10) Lerotic acid- CH3 (CH2)24COOH – Beewax
Definition
1. Lipids: Lipids are chemically heterogeneous group of compounds that are insoluble in
water but soluble in non-polar solvents such as chloroform
2. Fat: Any of a group of natural esters of glycerol and various fatty acids, which are solid
at room temperature and are the main constituents of animal and vegetable fat
3. Oil: An oil is any neutral, nonpolar chemical substance that is a viscous liquid at ambient
temperatures and is both hydrophobic and lipophilic
4. Fatty acid: A carboxylic acid consisting of a hydrocarbon chain and a terminal carboxyl
group, especially any of those occurring as esters in fats and oils.
5. Saturated fatty acid: A saturated fat is a type of fat in which the fatty acid chains have
all or predominantly single bonds
6. Unsaturated fatty acid: An unsaturated fat is a fat or fatty acid in which there is at least
one double bond within the fatty acid chain
7. Essential fatty acid: An unsaturated fatty acid that is essential to human health, but
cannot be manufactured in the body. Abbreviated EFA
8. Triglyceride: An ester formed from glycerol and three fatty acid groups. Triglycerides
are the main constituents of natural fats and oils.
9. Simple lipids: Lipids containing only fatty acids and glycerol or long chain alcohols
10. (Monohydric) are called as simple lipids which include fats, oils and waxes
11. Compound lipids: Esters of fatty acids with alcohol and possess additional groups also.
These group of lipids include glycerophospholipids, sphingo phospholipids, glycolipids,
sulpholipids and lipoproteins
12. Lecithin: Lecithin contains glycerol, fatty acids, phosphoric acid and a nitrogenous base,
choline
13. Sterols: Any of a group of naturally occurring unsaturated steroid alcohols, typically
waxy solids
14. Rancidity: Development of disagreeable odour and taste in fat or oil upon storage is
called rancidity.
15. Hydrolytic rancidity: Hydrolytic rancidity refers to the Odor that develops when
triglycerides are hydrolysed and free fatty acids are released.
16. Oxidative rancidity: The unsaturated fatty acids are oxidised at the double bonds to
form peroxides, which then decompose to form aldehydes and acids of objectionable
odour and taste.
17. Ketonic rancidity: Some moulds (Penicillium and Aspergillus spp.) attack fats
containing short‐chain fatty acids and produce ketones with a characteristic odour and
taste. Butter, coconut, and palm kernel oils are most susceptible.
18. Hydrogenation: Unsaturated fatty acids may be converted to saturated fatty acids by the
relatively simple hydrogenation reaction.
19. Hardening: Hydrogenation of unsaturated fats in the presence of a catalyst is known as
hardening.
20. Saponification number: It is defined as milligrams of KOH required to saponify 1 gm
of fat or oil.
21. Iodine Number: It is defined as the number of grams of iodine taken up by 100 grams
of fat or oil.
22. Reichert-Merisel number: Number of millilitres of 0.1 N alkali required to neutralise
23. the soluble volatile fatty acids contained in 5 gm of fat.
24. Polanski number: Number of millilitres of 0.1 N potassium hydroxide solution required
to neutralise the insoluble fatty acids (not volatile with steam distillation) obtained from
5 gm of fat.
25. Acetyl number: Amount in millilitres of potassium hydroxide solution required to
neutralise the acetic acid obtained by saponification of 1 gm of fat or oil after acetylation.
26. Acid number/Acid value: The milligram of potassium hydroxide required to neutralise
27. the free fatty acids present in one gram of fat or oil.
28. Iodine value: Measure of the degree of unsaturation of an oil, fat, or wax; the amount of
iodine, in grams, that is taken up by 100 grams of the oil, fat, or wax.
29. Peroxide value: The peroxide value is defined as the amount of peroxide oxygen per 1
kilogram of fat or oil
 METABOLISM
Metabolism, the sum of the chemical reactions that take place within each cell of a
living organism and that provide energy for vital processes and for synthesizing new organic
material
Two types of metabolic reactions take place in the cell: 'building up' (anabolism) and
'breaking down' (catabolism
Catabolism is the breaking down of things - a series of chemical reactions that break
down complex molecules into smaller units; catabolic processes usually release energy. the
breaking down of organic matter for example, the breaking down of glucose to pyruvate, by
cellular respiration,
Anabolism: The build-up of complex organic molecules from simpler ones, reactions
are called anabolic or biosynthetic. They involve dehydration synthesis (release water) and are
endergonic. The building up of components of cells such as proteins and nucleic acids
The chemical reactions of metabolism are organized into metabolic pathways, in which
one chemical is transformed through a series of steps into another chemical, by a sequence of
enzymes. Enzymes are crucial to metabolism because they allow organisms to drive desirable
reactions that require energy that will not occur by themselves, by coupling them to
spontaneous reactions that release energy. Enzymes act as catalysts that allow the reactions to
proceed more rapidly. Enzymes also allow the regulation of metabolic pathways in response to
changes in the cell's environment or to signals from other cells.
Connection between catabolic and anabolic pathways

The Relationship between Photosynthesis and Respiration

Photosynthesis generates the oxygen and glucose used by the mitochondria of eukaryotes as
fuel for: cellular respiration. Cellular respiration breaks down glucose into simpler substances
and releases the stored energy. Some of this energy is used to make ATP from ADP. Some of
this energy is lost as heat. The waste products of respiration, carbon dioxide and water are the
raw materials for photosynthesis.
H. IMPORTANT NOTE: While only green plants carry out photosynthesis, ALL living things
carry out respiration
Sun

Heat

CARBOHYDRATES
Cellular Respiration
The term cellular respiration refers to the biochemical pathway by which cells release energy
from the chemical bonds of food molecules and provide that energy for the essential processes
of life. All living cells must carry out cellular respiration. It can be aerobic respiration in the
presence of oxygen or anaerobic respiration
The energy currency of these cells is ATP, and one way to view the outcome of cellular
respiration is as a production process for ATP.

Carbohydrate metabolism is a fundamental biochemical process that ensures a constant supply

of energy to living cells. The most important carbohydrate is glucose, which can be broken
down via glycolysis, enter into the Kreb's cycle and oxidative phosphorylation to generate
ATP.
Further important pathways in carbohydrate metabolism include the pentose phosphate
pathway (conversion of hexose sugars into pentoses), glycogenesis (conversion of excess
glucose into glycogen, stimulated by insulin), glycogenolysis (conversion of glycogen
polymers into glucose, stimulated by glucagon) and gluconeogenesis (.a metabolic pathway
that results in the generation of glucose from non-carbohydrate carbon substrates such as
lactate, glycerol, and glucogenic amino acids.

Preparatory
stage

Pay off stage

Definition:
Glycolysis can be defined as the sequence of reactions for the breakdown of Glucose (6-carbon
molecule) to two molecules of pyruvic acid (3-carbon molecule) under aerobic conditions; or
lactate under anaerobic conditions along with the production of small amount of energy
In glycolysis, also referred to as the Embden-Meyerhof-Parnas pathway, each glucose molecule
is split and converted to two three-carbon units (pyruvate).
It is derived from Greek word glycose -sweet or sugar, lysis- dissolution.
Site: Cytosolic fraction of cell
Glycolysis literally means "splitting sugars" and is the process of releasing energy within
sugars. In glycolysis, glucose (a six carbon sugar) is split into two molecules of the three-
carbon sugar pyruvate. This multi-step process yields two molecules of ATP (free energy
containing molecule), two molecules of pyruvate, and two "high energy" electron carrying
molecules of NADH. Glycolysis can occur with or without oxygen

Glycolysis, which consists of 10 reactions, occurs in two stages:

(Preparatory stage and Pay off stage)
1 Glucose is phosphorylated twice and cleaved to form two molecules of glyceraldehyde-3-
phosphate (G-3-P). The two ATP molecules consumed during this stage are like an investment,
because this stage creates the actual substrates for oxidation in a form that is trapped inside the
cell.
2 Glyceraldehyde-3-phosphate is converted to pyruvate. Four ATP and two NADH molecules
are produced. Because two ATP were consumed in stage 1, the net production of ATP per
glucose molecule is 2.
The glycolytic pathway can be summed up in the following equation:
D-Glucose + 2 ADP + 2 Pi + 2 NAD → 2 pyruvate + 2 ATP + 2 NADH + 2H + 2H2O

Step 1
The enzyme hexokinase phosphorylates (adds a phosphate group to) glucose in the
cell's cytoplasm. In the process, a phosphate group from ATP is transferred to glucose
producing glucose 6-phosphate.
Glucose (C6H12O6) + hexokinase + ATP → ADP + Glucose 6-phosphate (C6H13O9P)

Step 2
The enzyme phosphoglucoisomerase converts glucose 6-phosphate into its isomer fructose 6-
phosphate. Isomers have the same molecular formula, but the atoms of each molecule are
arranged differently.
Glucose 6-phosphate (C6H13O9P) + Phosphoglucoisomerase → Fructose 6-phosphate
(C6H13O9P)
Step 3
The enzyme phosphofructokinase uses another ATP molecule to transfer a phosphate group to
fructose 6-phosphate to form fructose 1, 6-bisphosphate.
Fructose 6-phosphate (C6H13O9P) + phosphofructokinase + ATP → ADP + Fructose 1, 6-
bisphosphate (C6H14O12P2
Step 4
The enzyme aldolase splits fructose 1, 6-bisphosphate into two sugars that are isomers of each
other. These two sugars are dihydroxyacetone phosphate and glyceraldehyde phosphate.
Fructose 1, 6-bisphosphate (C6H14O12P2) + aldolase → Dihydroxyacetone phosphate
(C3H7O6P) + Glyceraldehyde phosphate (C3H7O6P)
Step 5
The enzyme triose phosphate isomerase rapidly inter-converts the molecules dihydroxyacetone
phosphate and glyceraldehyde 3-phosphate. Glyceraldehyde 3-phosphate is removed as soon
as it is formed to be used in the next step of glycolysis.
Dihydroxyacetone phosphate (C3H7O6P) → Glyceraldehyde 3-phosphate (C3H7O6P)
Step 6
The enzyme triose phosphate dehydrogenase serves two functions in this step. First the enzyme
transfers a hydrogen (H-) from glyceraldehyde phosphate to the oxidizing agent Nicotinamide
adenine dinucleotide (NAD+) to form NADH. Next triose phosphate dehydrogenase adds a
phosphate (P) from the cytosol to the oxidized glyceraldehyde phosphate to form 1, 3-
bisphosphoglycerate. This occurs for both molecules of glyceraldehyde 3-phosphate produced
in step 5.
A. Triose phosphate dehydrogenase + 2 H- + 2 NAD+ → 2 NADH + 2 H+
B. Triose phosphate dehydrogenase + 2 P + 2 glyceraldehyde 3-phosphate (C3H7O6P) → 2
molecules of 1,3-bisphosphoglycerate (C3H8O10P2)
Step 7
The enzyme phosphoglycerokinase transfers a P from 1,3-bisphosphoglycerate to a molecule
of ADP to form ATP. This happens for each molecule of 1,3-bisphosphoglycerate. The process
yields two 3-phosphoglycerate molecules and two ATP molecules.
2 molecules of 1, 3-bisphoshoglycerate (C3H8O10P2) + phosphoglycerokinase + 2 ADP → 2
molecules of 3-phosphoglycerate (C3H7O7P) + 2 ATP
Step 8
The enzyme phosphoglyceromutase relocates the P from 3-phosphoglycerate from the third
carbon to the second carbon to form 2-phosphoglycerate.
2 molecules of 3-Phosphoglycerate (C3H7O7P) + phosphoglyceromutase → 2 molecules of 2-
Phosphoglycerate (C3H7O7P)
Step 9
The enzyme enolase removes a molecule of water from 2-phosphoglycerate to form
phosphoenolpyruvate (PEP). This happens for each molecule of 2-phosphoglycerate
2 molecules of 2-Phosphoglycerate (C3H7O7P) + enolase → 2 molecules of
phosphoenolpyruvate (PEP) (C3H5O6P
Step 10
The enzyme pyruvate kinase transfers a P from PEP to ADP to form pyruvate and ATP. This
happens for each molecule of phosphoenolpyruvate. This reaction yields 2 molecules of
pyruvate and 2 ATP molecules.
2 molecules of phosphoenolpyruvate (C3H5O6P) + pyruvate kinase + 2 ADP → 2 molecules
of pyruvate (C3H3O3-) + 2 ATP
The glycolytic pathway can be summed up in the following equation:
D-Glucose + 2 ADP + 2 Pi + 2 NAD → 2 pyruvate 2 ATP + 2 NADH + 2H + 2H2O

Overview of Glycolysis
Advantages and Disadvantages of Glycolysis
Glycolysis only produces a gain of 2 ATP per molecule of glucose, but the process is so fast
that 1000’s of ATP are produced in just a few milliseconds. Another advantage is that
glycolysis does not require oxygen Energy can be produced for the cell even if no oxygen is
present. Disadvantage: If the cell relied only on glycolysis for ATP production, the cell would
quickly run out of NAD+ to accept the hydrogen electrons. Without NAD+, the cell cannot
keep glycolysis going and ATP production would stop. To keep glycolysis going, the NADH
must deliver their high-energy cargo of electrons to another pathway, and then return to
glycolysis to be used again

The Fate of Pyruvic Acid – What happens to it?

If oxygen is present:
In the presence of oxygen, the pyruvic acid will enter the mitochondria and undergo aerobic
respiration. Aerobic respiration includes the stages known as the kerb cycle and the electron
transport chain. Aerobic respiration will yield many more ATP than glycolysis.
If no oxygen is present
In the absence of oxygen, the pyruvic acid will enter the anaerobic pathways of fermentation.
Fermentation yields no additional ATP and Occurs in the cytoplasm

Gluconeogenesis

What are the two major stages of aerobic respiration?

 Aerobic respiration has two major stages:
 The Krebs cycle
 The electron transport chain
The Krebs cycle occurs in the matrix of the mitochondria and the electron transport chain
occurs along the cristae membranes. At the end of glycolysis, about 90% of the chemical energy
that was available in the glucose molecule is still unused. This energy is locked in: the high-
energy electrons of pyruvic acid.
The Bridge Reactions:
As the pyruvic acid enters the mitochondria, the following reaction occurs.
Steps in the Bridge Reaction:
1) Pyruvic acid enters the mitochondria. 2) The 3-C Pyruvic acid is converted to 2-C
acetate. This is accomplished by removing a
molecule of CO2 from each molecule of
pyruvic acid. The carbon dioxide is released
in air released into the air.

2 acetates

3) For each pyruvic acid that is converted to acetate, 4) Co enzyme attaches to acetate to form
one molecule of NAD+ is converted to NADH acetyl CoA . The acetyl CoA will be
released into Kerb cycle
5) This reaction is often referred to as “bridge reaction”.
It is the bridge between: the cytoplasm and the
Mitochondria anaerobic and aerobic respiration
Glycolysis and the Krebs cycle.
Oxidative decarboxylation of pyruvic acid to Acetyl CoA

The Krebs cycle

A. The Krebs cycle is a biochemical pathway that uses the acetyl CoA molecules from the
bridge reaction to produce: hydrogen atoms, ATP, carbon dioxide.
B. This set of reactions occurs in the matrix of the mitochondria.
C. Krebs cycle is so named to honour Hans Krebs. He was a German –
British scientist who was largely responsible for working out the pathway in
the 1930’s

a) Formation of citric acid

The acetyl- CoA combines with oxaloacetic acid to form citric acid. It contains 6 carbon
atoms. This reaction is catalysed by an enzyme called citric acid synthetase.
b) Dehydration
Citric acid undergoes dehydration and forms cis-aconitic acid. This reaction is catalysed by
the enzyme aconitase
c) Hydration
The aconitic acid is hydrated and it forms isocitric acid. This reaction is catalysed by the
enzyme aconitase
d) Dehydrogenation I
Isocitric acid undergoes dehydrogenation in the presence of isocitric acid dehydrogenase to
form Oxalo succinic acid. In this reaction 2 hydrogen atoms are released. They are accepted
by NAD+ to form NADH.
e) Decarboxylation
The Oxalo succinic acid undergoes decarboxylation to form a-ketoglutaric acid. This
reaction is catalysed by decarboxylase. In this reaction one CO2 is eliminated. Hence the a-
ketoglutaric acid has only 5 carbon atoms
f) Oxidative decarboxylation
During oxidative decarboxylation a-ketoglutaric acid is converted into succinyl CoA. This
reaction is catalysed by a-ketoglutaric acid dehydrogenase. Two hydrogen atoms are
released and they are transferred to NAD. The NAD is converted into NADH. In the next
step, the succinyl CoA is decarboxylated to succinic acid. This step is catalysed by succinic
acid Thiokinase. CoA is liberated.
g) Oxidation
Succinic acid is oxidised to fumaric acid by the removal of 2 hydrogen atoms. The reaction
is catalysed by succinic acid dehydrogenase. The hydrogen atoms are accepted by FAD and
it forms FADH2
Hydration
Fumaric acid undergoes hydration to form malic acid. This reaction is catalysed by fumarase
Dehydrogenation
It is the final step in Krebs cycle. Oxalo acetic acid is regenerated from malic acid by a process
of dehydrogenation. This reaction is catalysed by malic acid dehydrogenase in the presence of
NAD. The 2 hydrogen atoms removed are accepted by NAD and it forms NADH. The
oxaloacetic acid formed in the above reaction condenses with the acetyl CoA to form citric
acid again and thus the cycle is repeated
D. Summary of the Krebs cycle
NAD+ and FAD are electron carrier. NAD+ and FAD will deliver high energy electrons of
hydrogen to electron transport chain
2. What is the total amount of CO2, ATP, NADH, and FADH2 that is produced during one
turn of the Krebs cycle?
a) 2 CO2
b) 1 ATP
c) 3 NADH
d) 1 FADH2
The above totals are for one molecule of pyruvic acid.
Now remember that during glycolysis, glucose was broken down into two molecules of
pyruvic acid. Therefore, one glucose molecule causes two turns of the Kreb’s cycle
What is the total amount of CO2, ATP, NADH, and FADH2 that is produced per molecule of
glucose in the Krebs cycle?
a) 4 CO2
b) 2 ATP
c) 6 NADH
d) 2 FADH2
What happens to each of these products?
The carbon dioxide is released when you exhale.
The ATP is used for cellular activities.
The NADH and the FADH2 will be used in the next stage to generate huge amounts of ATP.
Most of the energy contained in the original glucose molecule still has not been transferred to
ATP. This transfer of energy will occur in the next step, the electron transport chain
Key Difference between Glycolysis and Krebs Cycle
Electron Transport Chain

The reduced coenzymes NADH and FADH2 produced from glycolysis, oxidation of pyruvate,
and the citric acid cycle are oxidized to provide the energy for the synthesis of ATP.
In electron transport or the respiratory chain,
Hydrogen ions and electrons from NADH and FADH2 are passed from one electron acceptor
or carrier to the next until they combine with oxygen to form H2O. The energy released during
electron transport is used to synthesize ATP from ADP and Pi during oxidative phosphorylation

In the electron transport system, there are five protein complexes, which are numbered I, II,
III, IV, and V. two electron carriers, coenzyme Q and cytochrome c, attached to the inner
membrane of the mitochondrion, carry electrons between these protein complexes bound to the
inner membrane. In electron transport, the oxidation of NADH and FADH2 provides hydrogen
ions and electrons that eventually react with oxygen to form water.
In complex I,
Electron transport begins when hydrogen ions and electrons are transferred from NADH to
complex I. loss of hydrogen from NADH regenerates NAD+ to oxidize more substrates in
oxidative pathways such as the citric acid cycle. Hydrogen ions and electrons are transferred
to the mobile electron carrier CoQ, forming CoQH2. CoQH2 carries electrons from complexes
I and II to complex III.
Complex II consists of the enzyme succinate dehydrogenase from the citric acid cycle. In
complex II, CoQ obtains hydrogen and electrons directly from FADH2. This produces CoQH2
and regenerates the oxidized coenzyme FAD, which becomes available to oxidize more
substrates.

Complex II consists of the enzyme succinate dehydrogenase from the citric acid cycle.
In complex II, CoQ obtains hydrogen and electrons directly from FADH2 and becomes
CoQH2. two electrons are transferred from the mobile carrier CoQH2 to a series of iron-
containing proteins called cytochromes. electrons are then transferred to two cytochrome c,
which can move between complexes III and IV.
At complex IV, Four electrons from four cytochrome c are passed to other electron carriers.
Electrons combine with hydrogen ions and oxygen (O2) to form two molecules of water. energy
is used to pump H+ from the mitochondrial matrix into the intermembrane space, further
increasing the hydrogen ion gradient.

The final stage of aerobic respiration is the electron transport chain, which is located on the
inner mitochondrial membrane The inner membrane is arranged into folds (cristae), which
increases the surface area available for the transport chain. The electron transport chain releases
the energy stored within the reduced hydrogen carriers in order to synthesise ATP. This is
called oxidative phosphorylation, as the energy to synthesise ATP is derived from the oxidation
of hydrogen carriers
Oxidative phosphorylation occurs over a number of distinct steps:
 Proton pumps create an electrochemical gradient (proton motive force)
 ATP synthase uses the subsequent diffusion of protons (chemiosmosis) to synthesise
ATP
 Oxygen accepts electrons and protons to form water
ATP Accounting
Let’s summarize what has happened prior to the electron transport
chain
. Glycolysis 2ATP
Krebs cycle 2ATP
Electron Transport Chain 34 ATP
One molecule of glucose has produced 38 ATP.
Only about 40% of the energy contained in the glucose molecule has been converted to ATP.
The remaining 60% is given off as heat
BREAKDOWN OF STARCH BY AMYLASES
Molecules of starch consist of links of glucose polymers formed by glycosidic bonds. The
enzyme amylase breaks glycosidic bonds and turns the starch into glucose molecules. Amylase
is an enzyme present in human saliva designed to break down starch present in foods like
potatoes, rice and cereal grains. The main effect of amylase on starch is to break it down into
simple sugars, which are used as an immediate energy source for the body. Another source of
amylase production is the pancreas, which catalyzes the breakdown of dietary starch in the
body for energy use.
Starch amylase dextrine+maltose amylase 2 glucose

Pentose Phosphate Pathway

Pentose phosphate pathway is an alternative pathway to glycolysis and TCA cycle for oxidation
of glucose.
It is a shunt of glycolysis. It is also known as hexose monophosphate (HMP) shunt or
phosphogluconate pathway. It occurs in cytoplasm of both prokaryotes and eukaryotes. Pentose
phosphate pathway starts with glucose and it is a multi-steps reaction. Breakdown of
carbohydrates (glucose) takes place in the body by glycolysis followed by tricarboxylic acid
cycle (Kreb’s cycle) resulting in yield of energy in the form of ATP. Glucose can alternatively
also undergo a different pathway to produce other products required by the cells. One of these
alternate pathway is the pentose phosphate pathway or also called as hexose monophosphate
pathway in which oxidation of glucose 6-phosphate takes place to produce pentoses. The fate
of glucose whether to undergo glycolysis or the hexose monophosphate pathway is decided by
the relative concentrations of NADP+ and NADPH.
This metabolic pathway is fragmented into two phases taking place in the cytosol as all the
enzymes required are present there: the oxidative and the non-oxidative phase
Glucose is phosphorylated to glucose-6-phosphate as in EMP pathway. Glucose-6-phosphate
is oxidized to 6 phosphogluconate with NADP+ is reduced to NADPH (Glucose -6- phosphate
dehydrogenase). 6-phosphogluconate is converted to ketopentose sugar- ribulose-5-P with the
liberation of one molecule of CO2 for every sugar molecule coenzyme NADP is reduced to
NADPH2 (6-phosphogluconate dehydrogenase). Ribulose-5-phosphate is changed to
aldopentose sugar Ribose-5-P( phosphoribose isomerase). Two molecules of ribose-5-P
combine to form one molecule of Sedoheptulose and another glyceraldehyde -3- phosphate
(Transketolase). The 3 carbon atom chain from Sedoheptulose is linked with 3 carbon atom of
3-phosphoglyceraldehyde with the formation of hexose phosphate- fructose-6- P
(Transaldolase). A second molecule of fructose-6-P is formed by linking 4 carbon atom
(Erythrose-4-P) from Sedoheptulose with 2 carbon fragment pentose molecules (Xylulose-5-
P) along with the formation of 3- phosphoglyceraldehyde (Transketolase) Two molecules of
3- phosphoglyceraldehyde like to form fructose 1-6 diphosphate which after dephosphorylation
form fructose -6-P
Thus with the formation of fructose-6-P, the cycle is complete in which 6 molecules of glucose
enter, but only one of them is completely oxidized liberating 6 molecules of CO 2 and the rest
are five reformed with 12 molecules of NADPH2
6 Glucose-6-P + 12 NADP+ + 7H2O 6-Fructose-6-P + 6CO2 + 12NADPH2 + H3PO4
NADPH2 undergo oxidation by atmospheric O2 via electron transport system where 3
molecules of ATP are produced per NADPH2 oxidized. Thus the oxidation of 12 NADPH2
molecules will produce 12 x 3 = 36 ATP molecules. Therefore this pathway is as efficient as
EMP Kreb’s cycle.
Significance
It provides alternative route for carbohydrate breakdown and provision of energy
It provides ribose sugar for synthesis of nucleic acid
It plays important role in fixation of CO2 in photosynthesis through ribulose -5-P
AMINO ACID METABOLISM
The catabolic pathways for the 20 amino acids vary considerably, but all amino acids are
degraded to one of seven metabolites:
 pyruvate,
 α ketoglutarate,
 succinyl-CoA,
 fumarate,
 oxaloacetate,
 acetyl CoA, or
 Acetoacetate.
 What is the fate of each of these metabolites?
Catabolic Pathway of Amino Acids
 Transamination
 Deamination
 Transamidination
 Transamidation
 Decarboxylation
1. Transamination
Transamination means transfer of amino group from α-amino acid to α-keto acid with
formation of a new α-amino acid and a new –α keto acid. All amino acids can be
transaminated except lysine, threonine, proline and hydroxy proline. All transamination
reactions are reversible. It is catalysed by aminotransferases (transaminases). It needs
pyridoxal phosphate as a coenzyme

Examples of transaminases
A. Alanine transaminase B. Aspartate transaminase C. Glutamate transaminase
Deamination
Deamination means the removal of amino group from α-amino acid in the form of ammonia
with formation of α-keto acid
Deamination may be oxidative or non-oxidative
A. Oxidative deamination
It is catalysed by one of the following enzymes:
1. L-1. Amino acid oxidases
2. D-amino acid oxidases
3. Glutamate dehydrogenase
B. Non-oxidative deamination
It is catalysed by one of the following enzymes:
1. Dehydratases
2. Desulfhydrases
Most of the naturally occurring α-amino acids are catabolized by transamination with α-
ketoglutaric acid followed by deamination of the produced glutamic acid, a condition called
trans deamination
Transamidination
Transamidination means the transfer of amidine group from a donor molecule to an acceptor
molecule It is catalyzed by transamidinase enzyme
An example of transmidination reaction is the transfer of amidine group from arginine (donor)
to glycine (acceptor) in creatine biosynthesis
Transamidation
Transamidation means transfer of amide group nitrogen from a donor molecule to an acceptor
molecule. It is catalyzed by transamidase enzyme. Examples of transmidation reaction include:
Transfer of amide nitrogen from glutamine (donor) to fructose (acceptor) 1.to form
glucosamine
Glucosamine biosynthesis

Decarboxylation
Decarboxylation means removal of CO2 from amino acid with formation of corresponding
amines. It is catalyzed by decarboxylase enzyme. It needs pyridoxal phosphate as a coenzyme

Ammonia assimilating enzymes

Ammonia Assimilation: Conversion of ammonia generated from nitrate assimilation or
photorespiration into amino acid.
2 pathways –
i. Primary Pathway ii. Alternative Pathway
 LIPID METABOLISM
Lipid metabolism is the synthesis and degradation of lipids in cells. Lipid metabolism is the
break down or storage of fats for energy; these fats are obtained from consuming food and
absorbing them or they are synthesized by an animal's liver.
Phospholipase: An enzyme that catalyzes the splitting of a phospholipid molecule by the
addition of water. Also called a lecithinase.
There are a number of phospholipases. They are grouped on the basis of the specific chemical
bond they split. The phospholipases include phospholipase A1 (PLA1), phospholipase A2
(PLA2), phospholipase C, and phospholipase D.
β oxidation is the chief process by fatty acid degradation in plants. This is one of the methods
of oxidation of fatty acid. The β oxidation mechanism is well established for saturated fatty
acid. The β oxidation takes place in mitochondria and involves sequential removal of 2 C in
the form of acetyl CoA from the carboxyl end of the fatty acid. This is called as β oxidation
because β –C of the fatty acid is oxidized during the process.
Stages of fatty acid oxidation
1. Activation of fatty acids takes place on the outer mitochondrial membrane
2. Transport into the mitochondria
3. Degradation to two-carbon fragments (as acetyl CoA) in the mitochondrial matrix (b-
oxidation pathway
BIOSYNTHESIS OF FAT
Synthesis of glycerol
Glycerol portion of the fat is synthesized from Dihydroxy acetone phosphate which is produced
from fructose 1-6 diphosphate in the presence of Aldolase and cofactor Zn2+ and Cu2+, as an
intermediate product in glycolysis. It is done in 2 steps
 Dihydroxy acetone phosphate is reduced to ά -
glycerophosphate by enzyme ά- glycerophosphate
dehydrogenase and coenzyme NADH2
 ά – Glycerophosphate is then hydrolyzed by
phosphatase to liberate phosphoric acid and
glycerol
Ii. Fatty acid synthesis
Fatty acid synthesis is the creation of fatty acids from acetyl-CoA and NADPH through the
action of enzymes called fatty acid synthases. This process takes place in the cytoplasm of the
cell. Most of the acetyl-CoA which is converted into fatty acids is derived from carbohydrates
via the glycolytic pathway. Fatty acid synthesis is somewhat of a complicated cytoplasmic
pathway
Fatty Acid Synthesis
Acetyl CoA is produced in the mitochondria by the oxidation of pyruvate, fatty acids,
degradation of carbon skeleton of certain amino acids & from ketone bodies. Mitochondria are
not permeable to acetyl CoA Acetyl CoA condenses with oxaloacetate in mitochondria to form
citrate. Citrate is freely transported to cytosol by tricarboxylic acid transporter. In cytosol it is
cleaved by ATP citrate lyase to liberate acetyl CoA & oxaloacetate. Oxaloacetate in the cytosol
is converted to malate. Malic enzyme converts malate to pyruvate. NADPH & CO 2 are
generated in this reaction. Both of them are utilized for fatty acid synthesis

Acetyl CoA, the starting point with two keto acid carbons, is first converted to malonyl CoA
with three keto acid carbons
The elongation phase of fatty acid synthesis starts with the formation of acetyl ACP and
malonyl ACP. Acetyl transacylase and malonyl transacylase catalyze these reactions.

Acetyl ACP and malonyl ACP react to form acetoacetyl ACP. The acyl-malonyl ACP
condensing enzyme catalyzes this condensation reaction.

In the condensation reaction, a four-carbon unit is formed from a two carbon unit and a three-
carbon unit, and CO2 is released.

Malonyl CoA reacts with another molecule of acetyl CoA in the presence of fatty acid
synthetase and coenzyme NADPH2 to form coenzyme-A derivative of butyric acid (4 C atoms)

Butryl CoA in the next step will combine with malonyl CoA to form CoA derivative of fatty
acid containing 6 C atoms. This process will be repeated till coenzyme A derivative of long
chain fatty acid (which may contain up to 16-18 C atoms-palmitic acid) is produced. For
example This process is then repeated six times, each time a malonyl CoA molecule is added,
each time CO2 is released, and each time the product is processed into a 2-carbon longer fatty
acid inked to ACP After six repeated cycles, palmitoyl (16-carbon fatty acid)-ACP, a typical
fatty acid is generated . This is treated with a thioesterase to remove ACP and the fatty acid
palmitic acid is released. The enzyme involved is fatty acid synthetase is not simple but a
complex of many enzymes and an acyl carrier protein called ACP is used for catalyze the
reaction. The synthesis of fatty acid involves 3 categories namely initiation reaction, chain
elongation reaction and termination reaction
Condensation of fatty acids and glycerol
The fats or triglycerides are synthesized not from glycerol and free fatty acids but from ά-
glycerophosphate and CoA derivatives of fatty acid
The glycerol is phosphorylated to form L-ά – glycerophosphate ά – glycerophosphate undergo
condensation with 2 molecules of acyl CoA to form ά- phosphatidic acid (Acyltransferase). ά-
phosphatidic acid undergo dephosphorylation in the presence of phosphatase to form ά, β-
diglyceride
Condensation of one molecule of an acyl –CoA with free hydroxyl group of the ά, β-
diglyceride takes place in the presence of enzyme diglyceride acyl transferase to form
triglyceride

FILL UP THE BLANKS

1) The citric acid cycle reaction takes place in ____ cell
2) Adenosine triphosphate has two _______ phosphate
3) Number of ATP molecules produced when one molecule of glucose gets oxidized to CO2
and water are______
4) The initiating codon in protein synthesis is _______
5) The type of RNA which gets involved in the transfer of amino acid in protein synthesis
is ___
6) Carotenoids give maximum absorption at _______ nm
7) NADPH is produced is ___ pathway
8) Complete oxidation of a glucose molecule yields ______ ATP molecules in nett
9) The other names of citric acid cycle are _______ and _______
10) In double helical DNA, the number of adenine is equal to ______ which are connected
by _______ bonds
11) In non- cyclic electron transport, molecular O2 is released by photo oxidation of _____
12) Cyclic photophosphorylation takes place only in ______
13) Non- Cyclic photophosphorylation takes place both in ______ and _______
14) The first stable product of dark reaction of photosynthesis is _______
15) C4 plants belongs to ______ family
16) CO2 fixation in C3 plants follow _____ pathway
17) CO2 fixation in C4 plants follow _____ pathway
18) Number of ATP molecules produced in every cycle of β –oxidation of fatty acid is
______
19) Number of ATP molecules produced for complete oxidation of acetyl CoA into H2O in
kreb cycle is ______
20) Complete oxidation of a glucose molecule results in the gain of _____ ATP molecules
21) The two phases in which photosynthesis can takes place is _____ and ________
22) The primary CO2 acceptor in Calvin cycle is _______
23) The first stable compound in C4 cycle is ________
24) One molecule of glucose after oxidation liberates _____
25) The process of conversion of glucose to pyruvic acid is known as ______
26) Aerobic oxidation of pyruvic acid into CO2 and H2O takes place through ______ cycle
27) The product formed from pyruvic acid under anaerobic condition is ______
28) The glycolysis pathway of oxidation of glucose to pyruvic acid was studied by _______
scientists
29) The process of glycolysis takes place in _____ and does not require ______ at any stage
30) All the reactions of Kreb’s cycle takes place inside the_____
31) The common pathway for the metabolism of carbohydrates, fats and proteins is ______
32) ____ act as a connecting link between glycolysis and Kreb’s cycle
33) Synthesis of ATP during oxidation of coenzymes in electron transport system of aerobic
respiration is called ________
34) Biosynthesis of protein in the plant is done under the direction of ____
35) The process of formation of mRNA from DNA is known as ________
36) The process of formation of protein from the language available in the form of mRNA is
known as ______
37) The terminating codon to stop the chain formation is ______-
38) The main pathway of saturated fatty acid synthesis in plants, animals is through ______
39) Biosynthesis of triglycerides is through condensation of _______ and _______
40) Oxidation of fatty acid takes place through __ and _______
41) The end product in the β- oxidation of fatty acid is ______
42) Number of ATP molecules produced during β- oxidation of fatty acid depends on
_______
43) One molecule of ATP is equal to _____ calories
44) Biosynthesis of fatty acid in plant, animal or bacteria takes place through ______
pathway
45) Number of ATP molecules produced on complete oxidation of acetyl CoA to CO2 and
H2O is equal to ________
46) The dominant pathway of oxidation of fatty acid is _____
47) In non-cyclic photophosphorylation, molecular oxygen is released through _____
48) ______ process act as a link between glycolysis and kreb’s cycle
49) The two phases that occur is during photosynthesis is _____ and______-
50) The two basic mechanisms in the synthesis of amino acids are ______ and _____
51) The first amino acid produced during biosynthesis of amino acids is ____
52) The transfer of amino group of amino acid to carboxyl group of keto acid is called ______
53) The ammonia assimilating enzymes are______, _______ and _______
54) An example of carotenoids is ______
55) The coenzyme used in biosynthesis of fatty acid is ________
56) The coenzyme required for transamination is_________
57) Number of ATP molecules formed when one molecule Palmitic acid get oxidized to CO2
and water is_______
58) Synthesis of carbohydrates in green plants using sunlight, CO2 and water is known as
_____
59) Carbon dioxide fixation in C3 plants occurs through________
60) The number of ATP molecules produced on complete oxidation of glucose is______
61) The end product is glycolysis is________
62) The common pathway for the metabolism of fats, carbohydrates and amino acid is____
63) The process of glycolysis takes place in______
64) The citric acid cycle takes place in ______ cell
65) The terminal product in the glycolysis pathway is________
66) In glycolysis, one molecule of glucose produces _____ molecules of pyruvic acid
67) The oxidation of pyruvic acid in aerobic condition takes place through________
68) Oxidative phosphorylation takes place inside ________
69) The process of formation of mRNA from DNA is known as______
70) The mechanism of reduction of NADP into NADPH + H+ may be called as______
71) The mechanism of production of ATP molecules from ADP and inorganic phosphate (iP)
is called as _________
72) Oxidation of glucose-6-phosphate to 6-phospho gluconic acid without entering
glycolysis is called as _____
73) _______ cycle is the final common pathway for oxidation of fuel molecules
74) Glycolysis takes place by a linear sequence of ______ number of enzyme catalyzed
reaction
75) Citric acid cycle proceeds in a cyclic way by _____ number of enzyme catalyzed reaction
76) The fatty acid Stearic acid to break down completely into CO2 and H2O , the number of
cycle of β oxidation needed is_____
77) The acetyl CoA to convert into CO2 and H2O has to enter______
78) Reaction between pyruvic acid and NH3 will give_________
79) The first Amino acid synthesized by reductive amination_______
80) ______ is the process which forms link between glycolysis and kreb cycle
81) The carrier of citric acid cycle is ______
82) NADPH is produced in _______ pathway
83) The four membered aldose sugar phosphate formed in HMP shunt pathway is ___
84) During glycolysis, Fructose 1, 6 diphosphate is decomposed by the enzyme______
85) Under anaerobic conditions the glycolysis of one mole of glucose yields ______moles
of ATP.
86) Tricarboxylic acid cycle to be continuous requires the regeneration of _______
87) The number of molecules of ATP produced by the total oxidation of acetyl CoA in TCA
cycle is ______
88) Acetyl CoA is not used for the synthesis of _______
89) During each cycle of β-oxidation ________ carbon atom is removed from ______end of
fatty acid
90) In deamination, amino acid is converted in to ________
91) Transamination is catalyzed by ________
92) Process of breakdown of amino acids to α keto acids is called __________
93) The key enzyme in the regulation of fatty acid synthesis is _______
94) Fatty acid synthesis takes place in _________
95) Number of ATPs are formed during complete oxidation of palmitate is _______
96) ______ link glycolysis and β-oxidation to citric acid cycle

ANSWER
Sl.No Answer Sl.No Answer
1 Mitochondria 34 DNA
2 Terminal 35 Transcription
3 38 36 Translation
4 AUG 37 UAA/UAG/UGA
5 tRNA 38 Malonyl CoA
6 45 39 fatty acid and glycerol
7 Cyclic Photophosphorylation 40 α, β
8 38 41 Acetyl CoA
9 Kreb cycle ( TCA cycle) 42 Number of carbon atoms
10 Thymine, Hydrogen 43 7600
11 H2O 44 Malonyl CoA
12 PS-1 45 12
13 PS-1, PS-11 46 β
14 3 phosphoglyceric acid 47 Photo oxidation of H2O
15 Gramineae 48 Oxidative decarboxylation
16 Calvin cycle 49 Light, dark
17 Hatch- Slack 50 reductive amination, transamination
18 3 51 Glutamic acid
19 12 52 Transamination
20 38 53 GDH, GS, GOGAT
 21 Light reaction, dark reaction 54 β-carotene
22 Ribulose diphosphate 55 NADPH
23 Oxaloacetic acid 56 Pyridoxal phosphate
24 673 57 130
25 Glycolysis 58 Photosynthesis
26 Kreb’s cycle 59 Calvin Cycle
27 Alcohol 60 38
28 Embden, Meyerhoff and Parnes 61 Pyruvic acid
29 Cytoplasm , Oxygen 62 Kreb’s cycle
30 Mitochondria 63 Cytoplasm
31 Kreb’s cycle 64 Mitochondria
32 Acetyl CoA 65 Pyruvic acid
33 Oxidative phosphorylation 66 Two
Sl.No Answer Sl.No Answer
67 Kreb cycle 82 Pentose phosphate
68 Mitochondria 83 Erythrose
69 Transcription 84 Aldolase
70 Electron transport system 85 2
71 Photophosphorylation 86 Oxaloacetate
72 Pentose phosphate pathway 87 12
73 TCA cycle 88 Glucose
74 10 89 2, carbonyl
75 12 90 keto acid
76 8 91 aminotransferase
77 TCA cycle 92 transamination
78 Phenylalanine 93 acetyl CoA carboxylase
79 Glutamic acid 94 cystol
80 Oxidative decarboxylation 95 129
81 oxaloacetate 96 Acetyl CoA

WRITE SHORT NOTES ON:

1. β-Oxidation
Long chain fatty acids may have up to 16-18 atoms are broken down by the process of β-
oxidation which ultimately produces the active 2 C units. Β oxidation is the chief process
of fatty acid degradation in plants. Β oxidation takes place in mitochondria and involves
sequential removal of 2 C in the form of acetyl CoA molecules from the carboxyl end of
the fatty acid .This is called β- oxidation because β- C of the fatty acid is oxidized during
the process. The various steps include as follows
 Fatty acid Fatty acyl- CoA α-β- unsaturated acyl CoA β hydroxy acyl CoA
β keto acyl CoA Fatty acyl CoA Acetyl-CoA
The acetyl CoA produced again reenters the β oxidation spiral at step 2 losing further 2 C
units. This sequence is continued until whole molecule is degraded. Thus for each turn of
β- oxidation generates 5 ATP molecules except in the first turn where one ATP molecule
is consumed resulting it in net gain of 4 ATP molecules.
2. Synthesis of sucrose
Sucrose is synthesized in plants by two reactions involving UDP-D glucose. In the first
reaction sucrose synthetases catalyzes the transfer of glucose residue of UDP- glucose to
fructose with the formation of sucrose and UDP
UDP-D-Glucose + D-fructose sucrose synthetase Sucrose + UDP
In the second reaction, sucrose phosphate synthetase catalyzes the reaction of UDP-D-
glucose and D-Fructose -6-P to form sucrose phosphate and UDP. Sucrose phosphate
undergo dephosphorylation to sucrose in the presence of phosphatases
UDP-D-Glucose + D-Fructose -6-P Sucrose synthetase Sucrose –P + UDP
Sucrose –P Sucrose + Pi
3. Bioenergetics of glucose oxidation
In glucose oxidation, one molecule of glucose gives 2 molecules of pyruvic acid. In this
four molecules of ATP are formed ( 2 ATP during conversion of 1-3 diphospho glyceric
acid to 3 phosphoglyceric acid and 2 ATP during conversion of 2 phopshoenol pyruvic
acid to pyruvic acid while 2 ATP molecules are consumed during phosphorylation, Thus
during glycolysis there is net gain of 2 ATP molecules( 4 ATP- 2 ATP = 2 ATP). Two
molecules of NAD are reduced to two molecules of NADH2 which later on oxidized
aerobically to yield six molecules of ATP (one NAD molecule after oxidation produces 3
molecules of ATP). Thus the total gain of ATP molecules during glycolysis in presence of
O2 will be increased to eight instead of two. The energy of glucose become stored partly in
ATP molecules and partly in ATP molecules and partly in NADH2 molecules
3. Chlorophyll
Chlorophyll is photosynthetic pigments. Chlorophyll is insoluble in water and can be
extracted only with organic solvents. Chlorophyll consists of a, b, c, d, e. Chlorophyll a is
present in all the photosynthesizing plants, chlorophyll b is present in higher plants and
green algae, chlorophyll c present in diatoms and brown algae, chlorophyll d in some red
algae. Chlorophylls are magnesium porphyrin compounds. The porphyrin rings consists of
four pyrol rings joined together by CH bonds. A long chain of C atoms called as phytol
chain is attached to porphyrin rings. Molecular formula of chlorophyll a is C55 H12O5N4Mg
and Chl b C55H70O5Mg. Chl a and b consists of Mg porphyrin head which is hydrophilic
and a phytol tail which lipophilic. The two chlorophyll differ with respect to Chl a -CH2
 group and Chl b –CHO group in 3rd carbon atom in II pyrol ring. Chlorophyll is formed
from proto chl in light,
4. C4 plants
C4 plants leaves possess special anatomy called Kranz type. The chloroplasts in C 4 plants
are dimorphic present in mesophyll cells of normal type and chloroplast in bundle sheath.
PEP Carboxylase enzyme occurs in mesophyll cells. C 4 cycle is performed in mesophyll
cells. C4 plants possess two types of CO2 acceptor 1) Phosphoenol pyruvate (in mesophyll
cells) 2) Ribulose diphosphate (in bundle sheath cells). C4 plants are found in subtropical
and tropical regions. They grow fast at high temperature and in more light intensities.
Therefore C4 plants are called efficient plants. In C4 plants, the O2 has no inhibitory effect.
They lack photo respiration.
5. Dark reaction
It is also known as Blackman’s reaction or thermo chemical reaction or path of carbon in
photosynthesis. It does not require light i.e., it takes place in presence and absence of light.
It mainly occurs in the stroma portion of chloroplast. The different steps in dark reaction
were studied by Calvin and coworkers. Calvin represented different steps of dark reaction
in the form of cycle. Therefore, it is called as Calvin cycle. The dark reaction of
photosynthesis is purely enzymatic and slower than the primary photochemical reaction.
The various steps in Calvin cycle are as follows
Six molecules of CO2 combine with ribulose 1, 5- diphosphate to form 12 molecules of 3
phosphoglyceric acid 1, 3 diphosphoglyceric acid 3 phosphoglyceraldehyde
Dihydroxyacetone phosphate + 3 phosphoglyceraldehyde Fructose 1, 6 diphosphate
Fructose 6 P + 3 phosphoglyceraldehyde Xylulose 5 P (2) + Erythrose 4 P (2) + 3
phosphoglyceraldehyde(2) Sedoheptulose 1,7 diphosphate
Sedoheptulose – 7- phosphate + 3- phosphoglyceraldehyde Xylulose – 5-P +
ribose- 5-P Ribulose -1, 5- diphosphate. Thus completing the cycle.
7. Transamination
This term denotes the reversible transfer of the amino group from an amino acid to a ά-
keto acid. There is no liberation of NH3 unlike during deamination. Transamination is a
very important reaction for the formation of amino acid as well as the transformation they
undergo. Transaminases are universally distributed and large in number, but two of them
are particularly abundant in animal tissues, they catalyse the following two reactions
L-Glutamic acid + Oxalo acetic acid ά –ketoglyceric acid + L-aspartic acid
L-Glutamic acid + pyruvic acid ά –ketoglyceric acid + L-alanine
Glutamic acid is a major participant in transamination reaction. Transamination is a transfer
of primary amino group of a donor ά- amino acid to an acceptor ά – amino acid.
 Transamination can take place on a primary amino group situated at the end of a chain of
amino acid.
8. Oxidative Phosphorylation
Synthesis of ATP during oxidation of coenzyme in electron transport system of aerobic
respiration is called oxidative phosphorylation. It occurs during respiration and takes place
inside mitochondria. It occurs inside the F1 particles present on the inner membrane of
cristae of mitochondria. It requires molecular oxygen for terminal oxidation.
Phosphorylation occurs in electron transport system where pigments are not involved. ATP
molecules are released into the cytoplasm which is used for various metabolic processes.
The complete oxidation of one molecule of glucose in aerobic condition produces 38 ATP
molecules (30 ATP molecules in Kreb’s cycle and 8 ATP molecules during glycolysis.
9. Significance of Kreb’s cycle
Kreb’s cycle occupies a central and very important place in the metabolism of plants. It
provides energy in the form of ATP molecules through oxidative phosphorylation for
various metabolic activities. It is directly related with nitrogen metabolism (ά- keto glutaric
acid, an intermediate product of Kreb’s cycle, is the first acceptor molecule of NH 2 in
forming of amino acid, the glutamic acid). It is from the glutamic acid that various
transamination reaction begins to form different amino acid which ultimately condenses to
form proteins. It is also intimately related to fat metabolism (Dihydroxy acetone phosphate
produced in glycolysis may be converted into glycerol via ά-glycerophosphate and vice
versa.). Glycerol is important constituent of fats. After β- oxidation, fatty acid gives rise to
active 2-C units, the acetyl CoA which may enter Kreb’s cycle. Other metabolic processes
are related to Kreb’s cycle through its intermediates in one or the other way.
10. Oxidative decarboxylation of pyruvate
Oxidative decarboylation is completed in several steps catalyzed by a enzyme complex
pyruvate dehydrogenase. The enzyme complex includes enzyme- pyruvic acid
decarboxylase, dihydroxy lipoyl transacetylase, dihydrolipoyl dehydrogenase, coenzymes-
thiamine pyrophosphate (TPP), lipoic acid, coenzyme A and NAD. Different steps of
oxidative decarboxylation involves
1) Pyruvic acid is converted to acetaldehyde by the enzyme pyruvic acid decarboxylase
2) Acetaldehyde is converted into active acetaldehyde
3) Active acetaldehyde reacts with lipoic acid to form acetyl lipoic acid by the enzyme
dihydroxylipoyl transacetylase
4) Acetyl lipoic acid reacts with coenzyme A resulting in to formation of acetyl CoA and
reduced lipoic acid by enzyme dihydrolipoyl dehydrogenase
CH3CO.COOH + Co.A.SH + NAD CH3CO.S.CoA + CO2 + NADH2
Pyruvic acid Coenzyme A Acetyl Coenzyme A
11. Ammonia assimilating enzymes
Rhizobium during symbiosis fixes the atmospheric nitrogen in the root nodules of the plant.
During free living state, bacteria must be able to assimilate nitrogen for their own growth.
There are two possible primary pathways for ammonia assimilation into amino acid which
depends on bacteria active in a particular species. availability of ammonia and energy. In
higher concentration of ammonia, assimilation is catalyzed by glutamate dehydrogenase.
The reaction is as follows
ά-ketoglutarate + NH4+ Glutamate (LDH) dehydrogenase L- Glutamate
NADH

In the case of limiting ammonia concentration, it occurs with the ATP driven glutamate
synthatase and glutamate synthase system
L- Glutamate + NH4 + ATP Glutamate Synthetase ( GS) Glutamine + ADP + iP
L- Glutamine + ά-ketoglutarate Glutamine Synthase (GOGAT) 2L-Glutamate
NADPH

In all legumes, glutamine synthatase (GS) appears to be primarily responsible for the
assimilation of ammonia produced by nodule nitrogenase fixation nitrogen. The
assimilation of ammonia by GS requires glutamate as substrate for the production of
glutamine. Substrate glutamate may be produced by glutamate synthase (GOGAT) which
transfer amide nitrogen from glutamine to L- ά-ketoglutarate to produce two glutamate, the
substrate of GS. Thus these enzymes GS and GOGAT may work in a cycle that yields
glutamate. Glutamate dehydrogenase (GDH) has the capacity to assimilate NH4 + in legume
nodules. However it is usually considered to be secondary to the GS_GOGAT cycle in
assimilating ammonia.
CARBOHYDRATE METABOLISM
1. Enumerate the reactions sequence of pentose phosphate pathway. What is its
significance?
Glycolysis is the principal route of the conversion of carbohydrates into pyruvic acid in
many biology systems. It has been observed that inhibitors such as iodoacetate, fluorides,
aresenates etc. inhibit certain steps in glycolysis. This has led to discovery of alternate route
of carbohydrate breakdown in plants. One such alternative route is pentose phosphate
pathway. It involves the oxidation of glucose- 6—phosphate to 6- phosphogluconic acid
which is converted into pentose phosphates. It is directly oxidized without entering
glycolysis, hence it is also called direct oxidation pathway or hexose monophosphate unit
1) Glucose is phosphorylated to glucose-6-phosphate as in EMP pathway
2) Glucose-6-phosphate is oxidized to 6 phosphogluconate with NADP+ is reduced to
NADPH( Glucose -6- phosphate dehydrogenase)
 3) 6-phosphogluconate is converted to ketopentose sugar- ribulose-5-P with the liberation
of one molecule of CO2 for every sugar molecule coenzyme NADP is reduced to
NADPH2 ( 6-phosphogluconate dehydrogenase)
4) Ribulose-5-phosphate is changed to aldopentose sugar Ribose-5-P( phosphoribose
isomerase)
Glucose
1 ADP 6NADP+ 6NADPH + H+
ATP
Dihydroxyacetone-P Glucose- 6-P 6-phosphogluconic acid
2 NADP+

3
Fructose-6diP NADPH+ H
CO2
Ribulose-5-P

Glyceraldehyde-3-P Xylulose-5-P 4

Fructose-6-P Glyceraldehyde-3-P
٨ ٨ 5
Xylulose-5-P Erythrose-4-P Sedoheptulose-7-P Ribose-5-P
6 5
Pentose- Phosphate Pathway

5) Two molecules of ribose-5-P combine to form one molecule of Sedoheptulose and

another glyceraldehyde -3- phosphate ( Transketolase)
6) The 3 carbon atom chain from Sedoheptulose is linked with 3 carbon atom of 3-
phosphoglyceraldehyde with the formation of hexose phosphate- fructose-6-
P(Transaldolase)
7) A second molecule of fructose-6-P is formed by linking 4 carbon atom (Erythrose-4-P)
from Sedoheptulose with 2 carbon fragment pentose molecules( Xylulose-5-P) along
with the formation of 3- phosphoglyceraldehyde( Transketolase)
8) Two molecules of 3- phosphoglyceraldehyde like to form fructose 1-6 diphosphate
which after dephosphorylation form fructose -6-P
Thus with the formation of fructose-6-P, the cycle is complete in which 6 molecules of
glucose enter, but only one of them is completely oxidized liberating 6 molecules of CO 2
and the rest are five reformed with 12 molecules of NADPH2
6 Glucose-6-P + 12 NADP+ + 7H2O 6-Fructose-6-P + 6CO2 + 12NADPH2 + H3PO4
NADPH2 undergo oxidation by atmospheric O2 via electron transport system where 3
molecules of ATP are produced per NADPH2 oxidized. Thus the oxidation of 12 NADPH2
molecules will produce 12 x 3 = 36 ATP molecules. Therefore this pathway is as efficient
as EMP Kreb’s cycle.
 Significance
1) It provides alternative route for carbohydrate breakdown and provision of energy
2) It provides ribose sugar for synthesis of nucleic acid
3) It plays important role in fixation of CO2 in photosynthesis through ribulose -5-P
2 Explain cyclic and non –cyclic photophosphorylation and their importance in
photosynthesis
The mechanism of reduction of NADP into NADPH + H+ may be called as electron
transport system in photosynthesis while the mechanism of production of ATP from ADP
and inorganic P with the help of light energy is called photophosphorylation. Two types of
photophosphorylation is present namely non-cyclic and cyclic photophosphorylation.
A) Non- Cyclic photophosphorylation.
Pigment system 1 and II are involved in non-cyclic photophosphorylation
1. The pigment molecules of PS I absorb light of higher wavelength and become photo
excited and energy is trapped by Chl a 700( P700) and gets excited and loses its outer
valence electron to primary acceptor( X) of PS1
2. The reduced unknown substance X ( P430) then reduces ferredoxin ( Fd) by ferredoxin
reducing substance( FRS)
3. The electrons from ferredoxin then pass to NADP+ to reduce it by the enzyme
Ferredoxin NADP- reductase
4. The reduced NADP+ participate in CO2 assimilation
5. Simultaneously PS II also absorb photons and get photo excited and energy is
transferred to reaction center Chl a 673 which takes part in primary photochemical
reaction. The Chl a 673 oxidized water to free O2 and reduce unknown substance Q
6. Photo excited P673 emits outer valence electron and electron is trapped by Q substance
which is primary acceptor of PS II
7. Reaction center of PS II on transferring its electron to Q becomes oxidized and oxidized
pigment molecule is reduced by trapping electrons from H2O and this step is known as
photo oxidation of water and result in evolution of molecular O2
2 H2O 4e- + 4 H+ + O2
8. Molecular oxygen and 4H+ are released inside the thylakoid membrane
9 The reduced Q or C550, transfer electrons to cytochrome b550
10. Reduced cyt b559 transfers electrons to plastoquinone (PQ) which is H+ carrier
11. Reduced PQ then transfers electrons to cytochrome causing the reduction and oxidation
of PQ and ADP is converted to ATP
12. The reduced Cyt F transfers its electron to plastocyanin (PC) and PC is reduced and Cyt
F is oxidized
13.The reduced PS transfers electron to PS-1. The PS is oxidized and P700 is reduced
In the above scheme, electron ejected from PS II did not return to its place of origin.,
instead it was passed on PS1. Similarly the electrons emitted from PS 1 did not cycle
 back but was used to reduce NADP+ to NADPH + H+. Hence it is called as non-cyclic
photophosphorylation
B) Cyclic photophosphorylation
Cyclic photophosphorylation takes place only in PS1 and formation of NADPH2 does
not take place. This situation is created by blocking the activity of PS II through certain
inhibitors. Under such conditions, only PS 1 is active, photolysis of water does not take
place, blockage of non-cyclic ATP formation cause a drop in CO2 assimilation in dark
reaction and shortage of oxidized NADP. When P700 molecule in PS 1 gets oxidized
by absorbing photons of light, ejected electron is captured by ferredoxin via FRS. From
ferredoxin, the electrons cannot be drained off to dark reaction due to shortage of NADP
and ultimately it falls back to P700 through number of intermediate electron carriers
like cytochrome b6, cytochrome f7 plastocyanin. At two places during electron
transport, i.e. between ferredoxin and cytochrome b6¬ and cytochrome f7 there is
phosphorylation of one ADP molecule to form one ATP molecule. Since in the above
electron transport system, the electron which was emitted from P700 molecule is cycled
back, the process is called as cyclic photophosphorylation.
3. Explain Calvin cycle/ enumerate the CO2 assimilation pathway in Calvin cycle/ Calvin
cycle and its significance
The dark reaction of photosynthesis is purely enzymatic slower than the primary
photochemical reaction. It takes place in stroma portion of the chloroplast and is
independent of light. The conversion of CO2 to carbohydrate with the help of assimilatory
power (NADPH2 + ATP) in dark reaction of photosynthesis is most thoroughly studied.
The different steps of dark reaction were studied by Calvin and Coworkers and represented
in the form of cycle is known as Calvin cycle
The Importance of the Calvin Cycle
1. PGAL, the product of the Calvin Cycle can be converted into all sorts of other molecules.
2. Glucose phosphate is one result of PGAL metabolism; it is a common energy molecule.
3. Glucose phosphate is combined with fructose to form sucrose used by plants.
4. Glucose phosphate is the starting point for synthesis of starch and cellulose.
5. The hydrocarbon skeleton of PGAL is used to form fatty acids and glycerol; the addition
of nitrogen forms various amino acids
Various steps are
1) The CO2 is accepted by ribulose 1-5 Diphosphate to form 6 carbon compound ,being
unstable converted into 2 molecules of 3 phosphoglyceric acid by hydrolysis and
dismutation
2) 3-Phosphoglyceric acid is reduced to 3 phosphoglyceraldehyde by enzyme triose
phosphate dehydrogenase
 3) Some molecules of 3 phosphoglyceraldehyde isomerizes into Dihydroxy acetone
phosphate and both of which join together in the presence of Aldolase to form fructose
1-6 diphosphate
4) Fructose 1-6 diphosphate is converted into fructose 6- phosphate in the presence of
phosphatase
5) Fructose 6-P is converted into sucrose
Carboxy Triose phosphate

Dismutase dehydrogenase
Ribulose 1, 5 + CO2
Diphosphate 6 C Compound 3 phospho 3 phospho
H2O Glyceric acid NADPH glyceraldehyde
ATP

Phospho triose isomerase

Phospho pento Fructose 1-6
kinase Aldolase Diphosphate

Ribose-5-P Dihydroxy acetone phosphate

Phosphatase

Ribulose 5-P phospho pento Fructose-6-P

isomerase
Transketolase

Erythrose-4-P Sucrose

Aldolase

Transketolase
Sedoheptulose
Sedoheptulose 1-7 diphosphate
7P Phosphatase
H2O
Phospho keto pentose epimerase
Xylulose-5-P

Fig: Calvin cycle

6) Some molecules of 3 phosphoglyceraldehyde reacts with fructose 6-P in the presence of

transketolase to form Erythrose -4-P ( 4 C atom sugar) and Xylulose -5-P ( 5 C atom
sugar)
7) Erythrose -4-P reacts with Dihydroxy acetone phosphate in the presence of Aldolase to
form Sedoheptulose 1-7 diphosphate( 7 C atom)
8) Sedoheptulose 1-7 diphosphate is converted to Sedoheptulose 7-phosphate by
phosphatase
 9) Sedoheptulose 7 P reacts with 3 phosphoglyceraldehyde in the presence of transketolase
to form Xylulose -5-P and Ribose -5-P ( 5 carbon atom)
10) Xylulose -5-P is converted into ribulose 5-P in the presence of phospho keto pentose
epimerase
11) Ribose -5-P is converted into ribulose 5 phosphate in the presence of phospho pentose
isomerase
12) Ribulose -5-P is converted into Ribulose 1-5 diphosphate in the presence of phospho
pentose kinase and ATP, thus completing the cycle
Because first visible product of this cycle is 3 phosphoglyceric acid which is 3 C
Compound, Calvin cycle is known as C3 pathway
4. Why C4 plants are more efficient than C3 plants?
1. In C4 plants, it increases the photosynthetic yield two or three times more than C3
Plants.
2. In C4 plants, it performs a high rate of photosynthesis even when the stomata are
nearly closed
3. It increases the adaptability of C4 plants to high temperature and light intensities
4. It increases the rate of CO2 fixation at 25-30o C in C4 plants as compared to C3 plants
5. It reduced the rate of photo respiration at 25-30oC
6. C4 plants leaves possess special type of anatomy called Kranz type
7. Chloroplast in C4 leaves are dimorphic
8. PEP carboxylase enzyme occur in mesophyll cells
9. C4 cycle is performed in mesophyll cells
10. They possess two types of CO2 acceptor -1) Phosphoenol pyruvate 2) Ribulose
diphosphate
11. First stable compound formed is oxaloacetic acid
12. C4 plants are found in tropical and sub-tropical regions
13. C4 plants, the O2 has no inhibitory effect. Hence C4 plants are called as efficient plants
5. Write the structure of chlorophyll and carotenes. Explain their role in photosynthesis
Chlorophylls and carotenoids are insoluble in water and can be extracted only with organic
solvents. Carotenoids include carotenes and xanthophylls. Different pigments absorb light
of different wavelength and show characteristic absorption peaks. Chlorophylls are of
different types. Chlorophyll a is present in all photosynthezing plants, chlorophyll b in
higher plants and algae, chlorophyll c in diatoms and brown algae, chlorophyll d in some
red algae.
Chlorophylls are magnesium porphyrin compounds. The porphyrin ring consists of four
pyrrol rings joined together by CH bridges. A long chain of C atoms called as phytol chain
is attached to porphyrin ring. Both chlorophyll a and b have Mg porphyrin head which is
hydrophilic and a phytol tail which is lipophilic. Chlorophyll is formed from proto
chlorophyll in light.
Carotenes consist of an open chain conjugated double bond system ending on both sides
with ionone rings. They are hydrocarbon. Different carbons differ only in their arrangement
of their molecules in space
Chlorophyll is vital for photosynthesis, which allows plants to absorb energy from light.
Chlorophyll molecules are specifically arranged in and around photosystems that are
embedded in the thylakoid membranes of chloroplasts. In these complexes, chlorophyll
serves two primary functions. The function of the vast majority of chlorophyll (up to several
hundred molecules per Photosystem) is to absorb light and transfer that light energy
by resonance energy transfer to a specific chlorophyll pair in the reaction center of the
photosystems.
The two currently accepted photosystem units are Photosystem II and Photosystem I, which
have their own distinct reaction center chlorophylls, named P680 and P700,
respectively.[3] These pigments are named after the wavelength (in nanometers) of their
red-peak absorption maximum. The identity, function and spectral properties of the types
of chlorophyll in each photosystem are distinct and determined by each other and the
protein structure surrounding them. Once extracted from the protein into a solvent (such
as acetone or methanol),[4][5][6] these chlorophyll pigments can be separated in a
simple paper chromatography experiment and, based on the number of polar groups
between chlorophyll a and chlorophyll b, will chemically separate out on the paper. The
function of the reaction center chlorophyll is to use the energy absorbed by and transferred
to it from the other chlorophyll pigments in the photosystems to undergo a charge
separation, a specific redox reaction in which the chlorophyll donates an electron into a
series of molecular intermediates called an electron transport chain. The charged reaction
center chlorophyll (P680+) is then reduced back to its ground state by accepting an electron.
In Photosystem II, the electron that reduces P680+ ultimately comes from the oxidation of
water into O2 and H+ through several intermediates. This reaction is how photosynthetic
organisms such as plants produce O2 gas, and is the source for practically all the O2 in
Earth's atmosphere. Photosystem I typically works in series with Photosystem II; thus the
P700+ of Photosystem I is usually reduced, via many intermediates in the thylakoid
membrane, by electrons ultimately from Photosystem II. Electron transfer reactions in the
thylakoid membranes are complex, however, and the source of electrons used to reduce
P700+ can vary. The electron flow produced by the reaction center chlorophyll pigments is
used to shuttle H+ ions across the thylakoid membrane, setting up a chemiosmotic potential
used mainly to produce ATP chemical energy; and those electrons ultimately reduce
NADP+ to NADPH, a universal reductant used to reduce CO2 into sugars as well as for
other biosynthetic reductions.
6. Write the components of electron transport chain in sequence and indicate sites of
ATP molecules.
NADH2 ATP ATP ATP
Or FAD Cyt b Cyt c Cyt a Cyt a
NADPH2 oxidized Fe2+ Fe2+ Fe2+ Fe3+ H2O

NAD or
NADP
ADP +iP FADH2
Reduced Cyt b Cyt c Cyt a Cyt a
Fe3+ ADP + iP Fe3+ Fe3+ ADP + iP Fe2+ 1/2 O2

The respiratory breakdown of glucose in the presence of oxygen is an oxidative process.

During aerobic respiration, simple carbohydrates and intermediates are oxidized. Each
oxidative step involves release of a pair of hydrogen atom ( 2H) which dissociate into two
protons ( 2H+) and two electrons( 2e-). The pair of hydrogen atom ( 2H++ 2e-) released in
each oxidative step of Kreb’s cycle do not combine directly with oxygen but pass through
a series of coenzymes and cytochromes which form electron transport chain before reacting
with O2 to form H2O. During the transfer of hydrogen atoms from one coenzyme to another
coenzyme a large amount of energy is released which is picked up by ADP to form ATP
with the help of inorganic phosphate. Electron transport system is made up of coenzymes
NAD+ and NADP+ , FAD, coenzyme Q, cytochromes b, C1,C2, a, a1. The transfer of
electrons in all the compounds takes place first in NAD+ or NADP+ and later FAD. Three
ATP molecules are produced for each NADH + H+ or NADPH + H+ molecules. Only two
ATP molecules are produced for each FADH2 molecules. The reduction of various
cytochromes requires only electrons and no protons. The formation of one molecule of
water require ½ O2 + 2e- + 2H+ , while reduction of one molecule of O2 requires 4e- + 4H+.
The reduction and oxidation of coenzymes and cytochromes takes place in sequence and
step wise because in electron transport system, they are arranged according to their redox
potential. The first coenzyme (NAD+) possesses low redox potential while last cytochrome
(cyt a2) is highest. This transfer of electrons proceeds from compounds with low redox
potential to those in high redox potential. Complex oxidations of glucose molecules need
38 ATP molecules. Because huge energy is generated in mitochondria, it is referred to as
power house of the cell wall
7. How acetyl CoA is oxidized to CO2 in TCA cycle/ describes Kreb’s Cycle. What is its
significance?
Pyruvic acid produced during glycolysis enters into Kreb’s cycle for further oxidation.
Kreb’s cycle is also called as citric acid cycle or tricarboxylic acid cycle. It takes place in
mitochondria, where all the necessary enzymes s are found in cristae
1. Pyruvic acid reacts with CoA and NAD and oxidatively decarboxylated and is
converted into acetyl CoA
2. Acetyl CoA condenses with oxaloacetic acid in the presence of condensing enzyme
 3. Citric acid is dehydrated in the presence of aconitase to form Cis-aconitic acid
4. Cis-aconitic acid reacts with water to form iso-citric acid
5. Iso-citric acid is oxidized to Oxalo Succinic acid in the presence of iso-citric
dehydrogenase. Coenzyme II NADH is reduced
6. Oxalic Succinic acid is decarboxylated in the presence of Oxalo-Succinic
decarboxylase to form ά- ketoglutaric acid
7. ά- ketoglutaric acid reacts with CoA and NAD in the presence of ά- ketoglutaric acid
dehydrogenase to form succinyl CoA
8. Succinyl CoA react with water molecule to form Succinic acid, GDP is converted to
GTP
9. Succinic acid is oxidized to fumaric acid in the presence of Succinic dehydrogenase.
FAD is reduced
10. Fumaric acid reacts with H2O in the presence of Fumarase to form malic acid
11. Malic acid is oxidized to form oxaloacetic acid in the presence of malic dehydrogenase
NAD is reduced. Thus cycle is repeated with another molecule of acetyl CoA.
Significance of Kreb’s Cycle
Kreb’s cycle occupies a central and very important place in the metabolism of plants. It
provides energy in the form of ATP molecules through oxidative phosphorylation for
various metabolic activities. It is directly related with nitrogen metabolism ( ά- keto glutaric
acid, an intermediate product of Kreb’s cycle , is the first acceptor molecule of NH 3 in
forming of amino acid, the glutamic acid. It is from the glutamic acid that various
transamination reactions begin ultimately condensing to form proteins. It is also intimately
related to fat metabolism (Dihydroxy acetone phosphate produced in glycolysis may be
converted into glycerol via ά- glycerophosphate and vice versa). Glycerol is important
constituent of fats. After β-oxidation, fatty acid give rise to active 2-C units, the acetyl CoA
which may enter the Kreb’s cycle. Other metabolic processes are related to Kreb’s cycle
through its intermediates in one or other way.
8. Enumerate the reaction sequence from glucose to pyruvic acid/ Explain glycolysis
1) Glucose react with ATP in the presence of hexokinase to form Glucose -6-P
2) Glucose-6-P is isomerised to fructose-6-P by phosphohexoisomerase
3) Fructose-6-P react with ATP in the presence of phosphohexokinase to form Fructose 1-6-
diphosphate
4) Fructose 1-6-Diphosphate is converted into two trioses 3-Phosphoglyceraldehyde and
dihydroxy acetone phosphate in the presence of aldolase
5) 3-Phosphoglyceraldehyde react with H3PO4 to form 1,3- diphosphoglyceraldehyde
6) 1,3- diphosphoglyceraldehyde in the presence of triose phosphate dehydrogenase and
coenzyme NAD to form 1,3 diphosphoglyceric acid
7) 1,3- diphosphoglyceric acid reacts with ADP in the presence of phosphoglyceric trans
phosphorylase to form 3 phosphoglyceric acid and ATP
Pyruvic acid
NAD CoA
CO2
NADH2 Acetyl CoA
Condensing enzyme
+ H2O, - CoA
Oxalo acetic acid
NAD Citric acid
Malic dehydrogenase + H2O Aconitase
NADH2
Malic acid Cis-aconitic acid
H2O
Fumerase
+ Isocitric acid
H2O NAD
Iso-citric
Fumaric acid NADH2 Dehydrogenase

Oxalo succinic acid

FADH2 Oxalo Succinic
CO2 Decarboxylase
Succinic
dehydrogenase ά-Ketoglutaric acid
FAD NAD
α ketoglutaric acid
GDP GTP NADH2 Dehydrogenase
+

Succinic acid Succinyl CoA+ CO2

Fig. TCA Cycle

8) 3- phosphoglyceric acid is isomerised into 2-phosphoglyceric acid in the presence of
phosphoglyceromutase
9) 2- phosphoglyceric acid is converted into 2 phosphoenol pyruvic acid in the presence of
enolase
10. - 2-phosphoenol pyruvic acid reacts with ADP to form pyruvic acid and ATP
` The Pyruvic acis so formed unger go either aerobic decpmosition or anarobic
decomposition depending on the availability of oxygen. In the absence of oxygen, pyruvic
acid is converted into alcochol( alcoholic fermentation) or lactic acid ( lactic acid
fermentation). In the presence of oxygen, pyruvic acid undergo oxidation by entering
Kreb’s cycle.
 Glucose ( 6C)

ATP Hexokinase
ADP Mg2+
Glucose-6-P( 6C)
Phosphohexo
Isomerase

Fructose-6-P

ATP phosphohexokinase
2+
Mg
ADP
Fructose 1-6- Diphosphate( 6C)

Aldolase

3 Phosphoglyceraldehyde( 3C) Phosphotriose isomerase Dihydroxy acetone phosphate( 3C)

H3PO4
1,3- Diphosphoglyceraldehyde( 3C)
NAD Triosephosphate
Dehydrogenase
NADH2

1,3- Diphosphoglyceric acid( 3C)

2 ATP
Phosphoglycero
2 ADP kinase

3 Phosphoglyceric acid ( 3C)

Phosphoglyceromutase

2 Phosphoglyceric acid ( 3C)

Mg2+ H2O Enolase

2 Phosphoenol pyruvic acid (3C)

2ADP
Pyruvatekinase
2ATP

Pyruvic acid( 3C)

9. Discuss the synthesis of starch
Synthesis of starch involves the simultaneous synthesis of amylose (with ά (1,4) glycosidic
linkage) and amylopectin ( with (ά 1,6 glycosidic linkage), two important constituent of
starch
A) Synthesis of amylose
Synthesis of amylose may take place by any one of the following way
1) Amylose can be synthesized in the presence of enzyme starch phosphorylase from
glucose 1-phosphate and an acceptor molecule containing of about 3 to 20 glucose units
together by ά (1-4) glycosidic linkage
n (Glucose -1-phosphate + acceptor) Amylose + n(iP)
Starch phosphorylase
1) Formation of ά(1-4) glycosidic linkage may also take place in the presence of enzyme
UDPG trans glycosylase( amylose synthatase) by their transfer of glucose from UDPG
( uridine diphosphate glucose) to an acceptor molecule consisting of 2 to 4 or more
glucose units joined together by ά(1-4) glycosidic linkages
UDPG + Acceptor Amylose synthetase UDP + ά(1-4) glucosyl- acceptor

2) Formation of ά (1-4) glycosidic linkage leading to the synthesis of amylose may also
take in the presence of D-enzyme by the transfer of two or more glucose units from
malto dextrin to a variety of acceptors such as malto triose
B) Synthesis of amylopectin (ά 1, 6 glycosidic linkages)
It takes place in the presence of Q-enzyme by the transfer of small chains of glucose
units joined together by ά (1-4) glycosidic linkages to an acceptor molecule consisting
of at least four ά (1-4) linked glucose units. The (ά 1, 6 glycosidic bonds established
between C1 of the terminal glucose units of the donor molecule and C4 of one of the
glucose unit of the receptor.
FAT METABOLISM
1) How is Palmitic acid is biosynthesized?
1) The main pathway of saturated fatty acid synthesis in plants and animals takes place
through malonyl CoA pathway. Long chain saturated fatty acid is synthesized in plants
from active two carbon units, the acetyl CoA. Synthesis of fatty acids from CH 3CO.CoA
takes place step by step. In each step fatty acid chain is increased by two carbon atoms
Acetyl CoA + CO2 Acetyl CoA Carboxylase Malonyl- CoA + ADP + iP
2) Malonyl CoA reacts with another molecule of acetyl CoA in the presence of fatty acid
synthetase and coenzyme NADPH2 to form coenzyme-A derivative of butyric acid ( 4 C
atom)
Malonyl CoA + Acetyl CoA + 2NADPH2 Butryl CoA + CoA+ CO2+ H2O+ 2NADP
 3) Butryl CoA in the next step will combine with malonyl CoA to form CoA derivative of
fatty acid containing 6 C atoms. This process will be repeated till coenzyme A derivative
of long chain fatty acid (which may contain up to 16-18 C atoms-palmitic acid) is produced
The enzyme involved is fatty acid synthetase is not simple but a complex of many enzymes
and an acyl carrier protein called ACP is used for catalyze the reaction
The biosynthesis of saturated fatty acid involves 3 steps 1) Initial reaction when acetyl CoA
transfers its acetyl group to one of the SH group of multi enzyme complex fatty acid
synthetase
CH3CO.SCoA + HS HS
Enz Enz + Co.ASH
HS CH3Co.S
2) Chain elongation reaction- Here six different reactions are involved a) Malonyl transfer
b) Condensation 3) Reduction 4 Dehydration 5) Reduction 6) Acyl transfer
3) Termination reaction- When the fatty acid residue has attained a desired length, the
chain elongation stops at a reaction (reduction) and cycle is not repeated.
2. Explain β oxidation and its importance/ How Palmitic acid is is oxidized through β
oxidation
β oxidation is the chief process by fatty acid degradation in plants. This is one of the
methods of oxidation of fatty acid. The β oxidation mechanism is well established for
saturated fatty acid. The β oxidation takes place in mitochondria and involves sequential
removal of 2 C in the form of acetyl CoA from the carboxyl end of the fatty acid. This is
called as β oxidation because β –C of the fatty acid is oxidized during the process. Various
steps of β oxidation are

1. Activation of fatty acid in the presence of ATP and enzyme Thiokinase, Co.ASH is
consumed and CoA derivative of fatty acid is produced
2. Two hydrogen atom are removed between ά, β –C atoms and a trans ά, β unsaturated
fatty acid acyl CoA is formed which catalyzed by FAD containing enzyme acyl CoA
dehydrogenase
3. Addition of water molecule across the double bond to form β-hydroxyacyl CoA in the
presence of enoylhydrase
4. β-hydroxy acyl-CoA is dehydrogenated in the presence of NAD, specific β-
hydroxyacyl-CoA dehydrogenase to form β-keto fatty acyl CoA
5. β keto acyl CoA is cleaved by enzyme β-keto acyl thiolase to form 2C unit of acetyl
CoA and a fatty acyl-CoA molecule which is shorter by two carbon atoms than when
entered the β- oxidation spiral
 R-CH2-CH2-COOH (Fatty acid)
Fatty acid ATP
Thiokinase CoA SH
O
II
R-CH2-CH2-C-S-CoA
NAD+
Fatty acid –CoA
Dehydrogenase NADH
O
II
R-CH=CH-C-S-CoA
O ά , β-unsaturated acetyl CoA
II
H2C-C-S-CoA Enoylhydrase H2 O
Acetyl CoA
O
+ C1 II
C2 R-CHOH-CH2-C-S-CoA
O C3 O β-hydroxyacyl-CoA
II II
R-C-S-CoA H2C-C-S-CoA β- hydroxyacyl
Fatty acyl CoA Acetyl CoA dehydrogenase NAD+
β- Keto thiolase
O O NADH
CoA SH II II
R-C-CH2-C-S-CoA
β- Keto fatty acid acyl CoA

β-Oxidation spiral of fatty acid

The fatty acyl CoA produced again reenters the β- oxidation of fatty acid may be
completely oxidized to CO2 and H2O through TCA cycle and may also be converted
into carbohydrate s by glyoxylate cycle. This conversion takes place only in case of
plants. In each turn of β- oxidation generates 5 ATP molecules and however in the first
turn there is compensation of 1 ATP in the first step, hence there will be only 4 ATP
molecules. Complete oxidation of one acetyl CoA molecule in TCA cycle to CO 2 and
H2O will result 12 ATP molecules.

Importance of β- oxidation is that sufficient amount of utilizable energy is produced for

example. Complete oxidation of palmitic acid produced through β- oxidation and TCA
cycle produces 130 ATP molecules. Each ATP molecule represents a gain of about
7600 calories of free energy. Thus the complete oxidation of one molecule of palmitic
acid by β- oxidation and TCA cycle will show a gain of 7600 x 136 = 9, 88,000 calories
of utilizable energy.
3. Explain the chemistry of seed germination/ Explain glyoxylate cycle
Many fatty seeds convert their fats into carbohydrates through glyoxylate cycle. This
conversion takes place as the seeds germinate, where fat content is decreased with a
simultaneous increase in sucrose.
1 Acetyl CoA produced after β – oxidation of fatty acid condenses with Oxalo acetic
acid to form citric acid
2. Citric acid is dehydrated to produce cis-aconitic acid in the presence of aconitase
3. Cis-aconitic acid reacts with one molecule of H2O to form iso-citric acid
4. Iso-citric acid is broken down into glyoxylic acid and Succinic acid by the enzyme
iso citratase
5. Glyoxylic acid combines with acetyl CoA in the presence of malate synthetase to
produce malic acid
6. Malic acid is oxidized into oxaloacetic acid in the presence of malic dehydrogenase
and coenzyme NAD
7. Succinic acid is converted into Oxalo acetic acid through fumaric acid and malic
acid
8. Oxaloacetic acid produced is decarboxylated in the presence of inosine triphosphate
to form Phosphoenol pyruvic acid
9. Phosphoenol pyruvic acid by the reverse reaction of glycolysis is converted into
glucose and fructose phosphate
10. Finally glucose and fructose phosphate are converted into sucrose

Fatty acid β- oxidation

Sucrose

Oxaloacetic acid

NAD Citric acid Glucose + Fructose Phosphate

Malate
dehydrogenase Aconitase
NADH2
Cis- aconitic acid Phosphoenol pyruvate + CO2

H2O + iP

Malic Acid Iso citric acid Oxaloacetic acid

Malate NAD Malate

Synthetase Glyoxylic acid Dehydrogenase
NADH2
Acetyl CoA Malic acid
+ H2O
Fumarase
Succinic acid Succinic Fumaric acid
Dehydrogenase

FAD FADH2

Glyoxylate Cycle
 The significance of glyoxylate cycle is that the germination of fatty seeds, the fats which are
insoluble is hydrolyzed into fatty acid and glycerol. Fatty acids after β- oxidation produce
acetyl CoA units which synthesis sucrose which is supplied to different growing regions of
the young germinating seedlings. Those microorganisms which can grow on ethyl alcohol
or acetates as a sole source of energy and carbon, make use of this cycle in synthesizing
longer carbon chains
4. Give brief note on fat synthesis
Fats are synthesized in plants through following steps
1. Synthesis of glycerol
Glycerol portion of the fat is synthesized from Dihydroxy acetone phosphate which is
produced from fructose 1-6 diphosphate in the presence of Aldolase and cofactor Zn2+ and
Cu2+, as an intermediate product in glycolysis. It is done in 2 steps
1) Dihydroxy acetone phosphate is reduced to ά - glycerophosphate by enzyme ά-
glycerophosphate dehydrogenase and coenzyme NADH2
2) ά – glycerophosphate is then hydrolyzed by phosphatase to liberate phosphoric acid and
glycerol
2. Synthesis of fatty acids
Long chain saturated fatty acids are synthesized in plants from active 2 Carbon atom
units acetyl CoA. Synthesis of fatty acids from acetyl CoA takes place step by step. In each
step the fatty acid chain is increased by two carbon atoms.
Acetyl CoA + CO2 Acetyl CoA Carboxylase Malonyl- CoA + ADP + iP
2) Malonyl CoA reacts with another molecule of acetyl CoA in the presence of fatty acid
synthetase and coenzyme NADPH2 to form coenzyme-A derivative of butyric acid (4 C
atoms)
Malonyl CoA + Acetyl CoA + 2NADPH2 Butryl CoA + CoA+ CO2+ H2O+ 2NADP
3) Butryl CoA in the next step will combine with malonyl CoA to form CoA derivative of
fatty acid containing 6 C atoms. This process will be repeated till coenzyme A derivative
of long chain fatty acid (which may contain up to 16-18 C atoms-palmitic acid) is produced
The enzyme involved is fatty acid synthetase is not simple but a complex of many
enzymes and an acyl carrier protein called ACP is used for catalyze the reaction. The
synthesis of fatty acid involves 3 categories namely initiation reaction, chain elongation
reaction and termination reaction
3. Condensation of fatty acids and glycerol
The fats or triglycerides are synthesized not from glycerol and free fatty acids but from
ά- glycerophosphate and CoA derivatives of fatty acid
1) The glycerol is phosphorylated to form L-ά – glycerophosphate
2) ά – glycerophosphate undergo condensation with 2 molecules of acyl CoA to form ά-
phosphatidic acid ( Acyltransferase)
3) ά- phosphatidic acid undergo dephosphorylation in the presence of phosphatase to form
ά, β- diglyceride
 4) Condensation of one molecule of an acyl –CoA with free hydroxyl group of the ά, β-
diglyceride takes place in the presence of enzyme diglyceride acyl transferase to form
triglyceride

PROTEIN METABOLISM
1. What are the different amino acids that constitute proteins in plants? Give an account
of their biosynthesis
Plant protein consists of over 20 different types of amino acids. Amino acids are grouped
into three groups
a) Aliphatic amino acids
1) Mono amino monocarboxylic amino acids- alanine, valine, leucine
2) Sulfur containing amino acid- Methionine, cystine cysteine
3) Mono amino dicarboxylic amino acids- Aspartic acid, asparagine, glutamic
acid, glutamine
4) Basic amino acid- lysine, arginine, histidine
b) Aromatic amino acid – Phenylalanine, tyrosine
c) Heterocyclic amino acid –tyrptophan, proline, hydroxy proline
Biosynthèses of Amino acids
Amino acids are synthesized in plants in the following ways
1) Inorganic nitrogen in the form of NH3 reacts with ά- ketoglutaric acid (an intermediate
of Kreb’s cycle) in the presence of enzymes glutamic dehydrogenase and reduced
coenzyme NADPH2 to form n amino acid , the glutamic acid
COOH-CH2-CH2-C=O-COOH + NADPH2 + NH3 Glutamic COOH-CH2-CH2-CHNH2-COOH + NADP + H2O
ά- Ketoglutaric acid Dehydrogenase Glutamic acid
It is called as reductive amination since the above process involve conversion of the
inorganic nitrogen (NH3) into organic nitrogen (amino acid) is accompanied by aminations
and reduction at the keto group of the organic acid
2) Transamination
The various other amino acids which ultimately condense to form proteins are produced
by transamination reactions involving the transfer of amino group from glutamic acid to
the keto position of the corresponding keto acid. Amino group from other amino acid
except glutamic acid may also be transferred to other keto acids forming corresponding
amino acids. Transamination reaction takes place in the presence of enzymes
transaminases which require coenzyme pyridoxal phosphate

The coenzyme pyridoxal phosphate act as carrier of amino group. It picks up the amino group
from the donor amino acid and is converted into Pyridoxamine phosphate. The latter transfer
this amino group to the acceptor keto acid forming a new amino acid and itself is converted
into pyridoxal phosphate for example
Glutamic acid + Oxalo acetic acid ά- ketoglutaric acid + aspartic acid
Glutamic acid + Pyruvic acid ά- ketoglutaric acid + ά- alanine
Aspartic acid + pyruvic acid oxaloacetic acid + ά- alanine
COOH Pyridoxal COOH
Phosphate
CHNH2 CHNH2

R R
Donor amino acid New amino acid
COOH COOH

C= O C=O

R R
Keto acid Pyridoxamine Acceptor Keto acid
Phosphate

2. Explain how proteins undergo oxidation?

The oxidation of proteins involves two steps 1) Hydrolysis or degradation of proteins to
amino acids 2) oxidation of amino acids

Leucine Glutamate
Arginine
Lysine Glutamine
Phenylalanine Histidine
Tryptophan ά- Ketoglutarate Proline
Tyrosine
Isoleucine
Succinyl CoA Methionine
Threonine
Valine
Acetoacetyl-CoA
Succinate
Phenylalanine
Isocitrate KREB’S
Tyrosine
CYCLE Fumarate

Citrate Malate

Acetyl- CoA Oxaloacetate

Pyruvate
Isoleucine
Leucine
Asparagine Alanine
Tryptophan Cysteine
Asparatate
Glycine
Serine
Tryptophan
Fig Entry points of standard amino acid into TCA cycle
The hydrolysis of proteins can be done by acids, alkalies or enzymes. The hydrolysis of proteins by
enzyme is called as enzymolysis and the enzymes are called as proteolytic enzymes. The enzyme
peptidases attack on peptide linkage of polypeptides and produce amino acids. Twenty standard amino
acids which make up protein have twenty different pathways for its degradation. The twenty catabolic
pathways converge to form only five products all of which enter the citric acid cycle. All or part of the
carbon skeletons of ten of the amino acid are finally broken down to acetyl CoA, five amino acids are
converted to ά- ketoglutaric acid , four into succinyl CoA, two into fumarate and two into oxaloacetate.
The strategy of amino acid degradation is to form major metabolic intermediates that can be converted
into glucose or to be oxidized by the citric acid cycle.

Definition
1. Glycolysis: Glycolysis is the sequence of reactions that convert glucose into pyruvate
with the concomitant trapping of the energy as ATP.
2. Citric acid cycle: The citric acid cycle (CAC) – also known as the tricarboxylic acid
(TCA) cycle or the Krebs cycle – is a series of chemical reactions used by all aerobic
organisms to release stored energy through the oxidation of acetyl-CoA derived from
carbohydrates, fats, and proteins into carbon dioxide and chemical energy in the form of
adenosine triphosphate (ATP)
3. Hexose Monophosphate Shunt: A sequence of metabolic reactions by which NADPH
is synthesized, together with ribose phosphate, part of the synthesis of nucleic acids
4. Gluconeogenesis: Gluconeogenesis (GNG) is a metabolic pathway that results in the
generation of glucose from certain non-carbohydrate carbon substrates
5. Glycogenesis: Glycogenesis is the process of glycogen synthesis, in which glucose
molecules are added to chains of glycogen for storage.
6. Glyoxylate cycle. The glyoxylate cycle, a variation of the tricarboxylic acid cycle, is an
anabolic pathway occurring in plants, bacteria, protists, and fungi. The glyoxylate cycle
centers on the conversion of acetyl-CoA to succinate for the synthesis of carbohydrates
7. Electron transport Chain: the stepwise transfer of electrons from one carrier molecule,
as a flavoprotein or a cytochrome, to another along the respiratory chain and ultimately
to oxygen during the aerobic production of ATP.
8. Oxidative phosphorylation: The synthesis of ATP by phosphorylation of ADP for
which energy is obtained by electron transport and which takes place in the mitochondria
during aerobic respiration
9. Alpha oxidation: Alpha-Oxidation is a process in which fatty acids are shortened by one
carbon atom. The alpha-oxidation sequence of 3-methyl-branched fatty acids starts with
an activation to the corresponding CoA-ester. Subsequently this acyl-CoA-ester
undergoes a 2-hydroxylation by the peroxisomal phytanoyl-CoA hydroxylase (PAHX).
10. β-Oxidation of fatty acids: Beta-oxidation is the catabolic process by which fatty acid
molecules are broken down in the cytosol in prokaryotes and in the mitochondria in
eukaryotes to generate acetyl-CoA, which enters the citric acid cycle, and NADH and
FADH2, which are co-enzymes used in the electron transport
11. Transamination: a chemical reaction that transfers an amino group to a keto acid to form
new amino acids.
12. Oxidative deamination: An amino acid is converted into the corresponding keto acid by
the removal of the amine functional group as ammonia and the amine functional group
is replaced by the ketone group.
13. Non-oxidative deamination: Amino acids such as serine and histidine are deaminated
non-oxidatively
 ENZYMES

What is an enzyme?
Globular protein which functions as a biological catalyst, speeding up reaction rate by lowering
activation energy without being affected by the reaction it catalyse.

Characteristics
1. Enzymes speed up the reaction by lowering the activation energy of the reaction.
2. Their presence does not effect the nature and properties of end product.
3. They are highly specific in their action that is each enzyme can catalyze one kind of
substrate.
4. Small amount of enzymes can accelerate chemical reactions.
5. Enzymes are sensitive to change in pH, temperature and substrate concentration.
6. Turnover number is defined as the number of substrate molecules transformed per minute
by one enzyme molecule.
7. Catalase turnover number = 6 x106/min

Active site
The active site of an enzyme is the region that binds substrates, co-factors and prosthetic groups
and contains residue that helps to hold the substrate. Active sites generally occupy less than
5% of the total surface area of enzyme. Active site has a specific shape due to tertiary structure
of protein. A change in the shape of protein affects the shape of active site and function of the
enzyme.
Enzymes are highly specific for the type of the reaction they
catalyze and for their substrate
Enzymes are highly specific with varying degrees of specifity.
 Absolute specifity – they act on one substrate and only on that substrate.
 Stereospecifity – such enzymes that can detect the difference between optical isomers
(mirror images) and select only one of such isomers.
 Reaction specifity – enzymes that catalyze certain types of reactions.
 Group specifity – enzymes that catalyzes a group of substances that contain specific
compounds
APOENZYME and HOLOENZYME
Coenzymes are small organic molecules
that are often required to prepare the active
site for proper substrate binding and/or
participate in catalysis. Because they are
not destroyed during the reaction,
coenzymes are only required in small
quantities

Classification and Nomenclature of Enzymes

Naming Enzymes
 The name of an enzyme in many cases end in –ase
For example, sucrase catalyzes the hydrolysis of sucrose
 The name describes the function of the enzyme
For example, oxidases catalyze oxidation reactions
 Sometimes common names are used, particularly for the digestion enzymes such as
pepsin and trypsin
 Some names describe both the substrate and the function
For example, alcohol dehydrogenase oxides ethanol
Enzymes are classified into six functional Classes (EC number Classification) by the
International Union of Biochemists (I.U.B.). on the Basis of the Types of Reactions That They
Catalyze
EC 1. Oxidoreductases
EC 2. Transferases
EC 3. Hydrolases
EC 4. Lyases
EC 5. Isomerases
EC 6. Ligases
EC 1. Oxidoreductases
Biochemical Activity:
Catalyse Oxidation/Reduction Reactions Act on many
chemical groupings to add or remove hydrogen atoms.
Examples: Lactate dehydrogenase. Glucose Oxidase.
Peroxidase. Catalase.
Phenylalanine hydroxylase.

EC 2. Transferases
Biochemical Activity:
Transfer a functional groups (e.g. methyl
or phosphate) between donor and acceptor
molecules. Examples: Transaminases
(ALT & AST). Phosphotransferases
(Kinases). Transmethylases.
Trans peptidases. Transacylase.
Catalyze group transfer reactions
EC 3.Hydrolases
Biochemical Activity:
Catalyse the hydrolysis of various bonds Add
water across a bond.
Examples: Protein hydrolysing enzymes
(Peptidases).Carbohydrases (Amylase,
Maltase, Lactase). Lipid hydrolysing enzymes
(Lipase).Deaminases. Phosphatases.
EC 4. Lyases
Biochemical Activity:
Cleave various bonds by means other than hydrolysis and
oxidation .Add Water, Ammonia or Carbon dioxide
across double bonds, or remove these elements to produce
double bonds. Examples: Fumarase. Carbonic anhydrase.
EC 5.Isomerases
Biochemical Activity:
Catalyse isomerization changes within a
single molecule. Carry out many kinds of
isomerization: L to D isomerizations
.Mutase reactions (Shifts of chemical
groups). Examples: Isomerase. Mutase
EC 6. Ligases
Biochemical Activity:
Join two molecules with covalent bonds
Catalyse reactions in which two chemical
groups are joined (or ligated) with the use of
energy from ATP. Examples: Acetyl~CoA
Carboxylase. Glutamine synthetase

Mechanism of Action of Enzymes

The enzymatic reactions takes place by binding of the substrate with the active site of the
enzyme molecule by several weak bonds.
E + S ‹--------› ES --------› E + P
Formation of ES complex is the first step in the enzyme catalyzed reaction then ES complex
is subsequently converted to product and free enzyme.
Enzyme-Substrate Interactions:
Formation of Enzyme substrate complex by:
 Lock-and-Key Model
 Induced Fit Model

Induced Fit Model

Enzyme Catalyzed Reactions
When a substrate (S) fits properly in an active site, an enzyme-substrate (ES) complex is
formed:
E + S  ES
Within the active site of the ES complex, the reaction occurs to convert substrate to product
(P):
ES  E + P
The products are then released, allowing another substrate molecule to bind the enzyme
- This cycle can be repeated millions (or even more) times per minute
The overall reaction for the conversion of substrate to product can be written as follows:
E + S  ES  E + P
Enzyme-substrate complex

What Affects Enzyme Activity?

Three factors:
1. Environmental Conditions
2. Cofactors and Coenzymes
3. Enzyme Inhibitors
.1. Environmental Conditions
 Temperature, Hydrogen ion concentration (pH), Substrate concentration
 Enzyme concentration, Products of the reaction, Presence of activator/inhibitor,
 Allosteric effects. Time
Rate of the reaction or velocity is directly proportional to the Enzyme Concentration when
sufficient substrate is present

Accumulation of Product in a reaction causes inhibition of enzyme activity.

Substrate Concentration and Reaction Rate
The rate of reaction increases as substrate concentration increases (at constant enzyme
concentration). Maximum activity occurs when the enzyme is saturated (when all enzymes are
binding substrate)
What is Km and Vmax?
Km is the concentration of substrate which permits the enzyme to achieve half Vmax. An
enzyme with a high Km has a low affinity for its substrate, and requires a greater concentration
of substrate to achieve Vmax."

Enzyme Inhibition
Competitive enzyme inhibition

Succinate dehydrogenase
Malonate is a competitive
Inhibitor

Non-Competitive Inhibition
Un-competitive Inhibition

Un-competitive Inhibition
Binds only to the enzyme-substrate complex. Does not have the capacity to bind to the free
enzyme. Not overcome by increasing substrate concentration. Both the Km and Vmax are
reduced. Only binds when the ES complex is formed ii) reduces the amount of ES available,
and thus less [S] to create the half of ES --> apparent lower Km iii) reduced the amount of
available ES that aren't bound to the ESI, so at the high [S] concentrations, we have Vmax also
lowering
Isoenzyme
Isoenzymes or isozymes are multiple forms of same enzyme that catalyze the same chemical
reaction. These enzymes usually display different kinetic parameters (e.g. different KM
values), or different regulatory properties. The existence of isozymes permits the fine-tuning
of metabolism to meet the particular needs of a given tissue or developmental stage. Isozymes
are usually the result of gene duplication, but can also arise from polyploidisation or nucleic
acid hybridization. An example of an isozyme is glucokinase, a variant of hexokinase which is
not inhibited by glucose 6-phosphate. Isozymes (and allozymes) are variants of the same
enzyme.
Zymogen
Zymogens (proenzymes) are inactive forms of enzyme. They are activated by removal of
peptide sections. Digestive enzymes are produced as zymogens, and are then activated when
needed. For example, proinsulin is converted to insulin by removing a 33-amino acid peptide
chain. The digestive enzymes must be stored as zymogens because otherwise they would
damage the pancreas

Allosteric Enzyme
Some of the enzymes possess additional sites, known
as allosteric sites (Greeek; allo-other) besides the
active site. Such enzymes are known as allosteric
enzyme. The allosteric sites are unique places on the
enzyme molecules; Allosteric enzyme have one or
more allosteric sites Allosteric sites are binding sites
distinct from an enzyme active site or substrate
binding site Molecule that bind to allosteric sites are
called effector or modulator. Effector may be positive
or negative, this effector regulate the enzyme activity.
The enzyme activity is increased when a positive
allosteric effector binds at the allosteric site known as
activator site. On the other hand, negative allosteric
effector bind at the allosteric site called inhibitor site
and inhibit the enzyme activity. Binding to allosteric sites alter the activity of the enzyme.
An allosteric inhibitor binds to the enzyme, inducing it to assume an inactive form. All non-
competitive inhibition is allosteric inhibition, but not all allosteric inhibition is non-competitive
inhibition because certain forms of allosteric inhibition can prevent the substrate from binding
to the active site.

FILL UP THE BLANKS

1. _______ is one of the enzyme involved in carbohydrate metabolism
2. Enzymes are_____-
3. NADPH is an universal ______ source
4. Enzymes which break the linkage between C_C bond and C-N bond are_______
5. An example of Co enzyme is ______
6. ______ enzyme splits peptides of proteins
7. The zymogens are inactive enzymes precursor is converted into an active enzyme
by__ compounds
8. The enzyme which catalyst the transfer of hydrogen from one molecule to another is
called _____
9. The enzyme that hydrolyze sucrose is _____-
10. Enzymes are located in _______
11. Vitamin B1 and B6 form coenzymes with ____ and _______
12. Enzymes is a ____ which _______ the activation energy of a reaction
13. _______ is a metallo enzyme
14. The coenzymes of niacin are ____ and ______-
15. Enzymes which are present inside the living cells and act within is called as ______
16. The prosthetic group of complex proteins enzyme is called as ______
17. Apo enzyme and coenzyme put together is called as _______
18. The enzyme that catalyses hydrolysis reactions is known as ______
19. _____ enzymes hydrolyze lipids
20. _____ is an example of oxidation-reduction enzymes
21. An enzyme which catalyse L- alanine to D-alanine is ______
22. ____ is an example of coenzyme
23. Multiple forms of the enzyme which catalyze the same reaction is called as _____-
24. _____ is an example of simple protein enzyme
25. Catalase is an example of __ enzyme
26. Coenzymes accounts for about ____% of the entire enzymes molecule
27. In Apo enzyme, if the prosthetic group includes the metal ions, then it is called as ____
28. The catalytic power of an enzyme is measured by_______
29. Number of substrate molecules converted into products per unit time, when the enzyme
is fully separated with substrate is known as _______
30. The specific region of the enzyme on which substrates binds is known as _____
31. _____ proposed enzyme substrate complex theory about mechanism of enzyme action
32. Emil Fischer proposed _____model regarding the action of enzymes substrate
33. The catalytic power of certain enzymes is reversibly altered by certain inorganic and
organic molecules called ______
34. The inactive forms of enzymes are called ______
35. Compounds which convert the enzymes into inactive substances and adversely
affect enzymatically catalyzed reaction is known as ______-
36. The inhibitors due to a compound which is totally different structure from the
substrate of the enzymes is called as ______
37. Malonic acid which inhibit the activity of the enzyme sucrose dehydrogenase is
referred to as _____-inhibitor
38. Lock and Key hypothesis on mechanism of enzyme action was proposed by______
39. ______ is a fat soluble vitamins
40. _____- is a water soluble vitamins
41. Irradiation of ergosterol results in the formation of ______
42. Evening blindness is caused by the deficiency of _______
43. In 1912 _____ coined the term vitamin
44. __________ is another anti beri- beri factor
45. ______ is a water soluble vitamin present in cow’s milk
46 Isomerases involve in ______
47 Enzymes which add or remove phosphoric acid is called as_______
48 Carboxylase is _________
49 Enzyme is a _______
50 In arresting the activities of enzymes, the non- competitive enzyme inhibitor may
combine ________ with enzyme
51 The protein part of enzyme is called as _________
52 Invertase is an enzyme which hydrolyze _________
53 Trypsin is a _______
54 The coenzyme required for transamination is _______
55 The coenzyme used in the biosynthesis of fatty acid is _________
56 Succinate dehydrogenase is a _______
57 An example of plant proteolytic enzyme is_______
58 Non-protein part in complex protein enzyme is known as______
59 β-carotene is precursors of _________
60 Ergosterol is a precursor of_______
61 An example of carotenoids is________
62 Enzymes fast up the velocity of a biochemical reaction by _____
63 Km values are not altered by _____________ type of inhibitor
64 The low value of Km indicates_________
65 Zinc is present in ___ enzymes
66 An allosteric modulator influences enzyme activity by______
67 The enzyme which catalyse R-CH2OH + O2 → R-CHO + H2O2 is _______
68 The enzyme that catalyse Glucose + ATP → Glucose -6-phosphate + ADP is ______
69 The typical saturation curve for an enzyme catalyzed reaction is sigmoidal. This
indicates that the enzyme is _________
70 Michaelis menten equation is given by _______
71 Both Vmax and Km values are altered in _________ inhibition
72 A competitive inhibitor of an enzyme ____ Km and ______Vmax
73 A competitive inhibitor binds to ______
74 The inactive precursor of an active enzyme is called __________
75 The inhibition of succinate dehydrogenase by malonate is an example for _____
76 The uncompetitive inhibitor binds with_________
77 Isoenzymes are generally separated by ________method
78 Non-competitive inhibitor binds with________
79 Sigmoidal graph indicates _________
80 The coenzyme present in transaminase is ________
81 The low value of Km indicates _______
82 According to IUB enzymes are classified into _________ classes
83 The conversion of ATP to cAMP is catalyzed by______
84 Substrate binding site on the enzyme is called as___
85 Urease is a _______ type of enzyme
86 .J.B.Sumner isolated the _____ enzyme
87 Enzymes bringing about hydrolysis of esters and peptide bonds are_______
88 Most modern hypothesis about enzyme action is called _______
89 Fitting of substrate in active site is called as ________
90 In case of induced fit model _______ changes its shape slightly
91 Substrate binds to specific region of enzyme called ______
92 Enzymes do not change the _____
93 Catalytic region in which small portion of molecules are involved in catalysis is
called__
94 Regulators of enzymatic reactions are classified as _______ and ____
95 Model proposed by Emil Fischer is known as________
96 Kind of molecules at which enzymes act are classified as ____
97 Apoenzyme plus co factor is known as ______-
98 Majority of enzymes are inactive at ______ temperature
99 Substance that accelerates the rate of a chemical reaction is called a(an)_______
100 Haemoglobins has _________ structure
101 The key regulated enzymes in glycolysis are ___, ______and __
Sl.No Answer Sl.No Answer
67 Alcohol oxidase 100 Quaternary
68 Hexokinase 101 Hexokinase, Phosphofructokinase, Pyruvate kinase
69 Allosteric
70

71 Uncompetitive
72 Increases , no effect
73 Substrate
74 Zymogen
75 Competitive inhibitor
76 Enzyme substrate complex
77 electrophoresis and ion-
exchange chromatograph
78 Enzyme substrate complex
79 Allosteric regulation
80 pyridoxal-phosphate,
81 High substrate affinity
82 Six
83 adenylyl cyclase
84 Active
85 Hydrolase
86 Urease
87 Hydrolase
88 Induce fit
89 Lock and key
90 enzyme
91 Active site
92 Eq
93 Active site
94 Activator and inhibitor
95 Deduction
96 Substrate
97 Holoenzyme
98 Above 40oC
99 Catalyst
WRITE SHORT NOTES ON:
1. Enzyme as a catalyst
Most of the chemical reactions in the cell take place in the presence of specific
proteinaceous substances called as enzyme. It is referred to as biological catalyst. The
enzymes do not alter the chemical equilibrium point of a reversible reaction but only the
speed of the reaction is changed. It is produced from the living cells and being protainaceous
in nature cannot last indefinitely in a reaction system as they often become damaged or
inactivated by the reaction they catalyze. They must be replaced constantly by further
synthesis in the body. Most individual enzymes are very specific in that they act either on a
single or at most on some structurally related substrates. Since the enzymes are highly
specific as to the reaction they catalyze, names of the enzymes are suitably changed for
example hydrolyases (hydrolysis), isomerases (isomerization), oxidases (oxidation) ,
dehydrogenases( dehydrogenation), transminases ( transamination) , transaldolases (
translocation) etc.,
2. Co-enzyme
Certain enzymes in addition to their protein structure have a non-protein group attached to
them. The non-protein part of the enzyme is called as prosthetic group or co enzymes. The
coenzymes are small molecular weight, organic, dialyzable, thermostable compounds
required for the catalytic activity of one or a group of enzymes. Some of the common
examples of coenzymes are NAD+, NADP, FAD, FMN CoA, Pyridoxals. Coenzymes are
momo or dinucleotides. Most of the coenzymes are the members of vitamin B complex
group. Based on the reaction in which they participate coenzymes are classified as hydrogen
transferring group_. The coenzymes usually occur in living cells in low concentrations. The
coenzyme is as essential a reactant as the substrate that is activated by the enzyme
Substrate (A) + Coenzyme Enzyme (A) Substrate (A) derivative + Coenzyme derivatives
Substrate (B) + coenzyme derivative Enzyme (B) Substrate (B) - derivative + Coenzyme
3. Isoenzymes
Many enzymes occur is more than one molecular form in the same species, in the same
tissue or even in the same cell. In such cases, the different forms of the enzyme catalyze the
same reaction but since they possess different kinetic properties and different amino acid
composition, they can be separated by appropriate techniques such as electrophoresis. Such
multiple forms of the enzymes are called Isoenzymes. It is widespread in nature. Over a
hundred enzymes are known to be of isoenzymic nature and consequently occur in two or
more molecule form eg. Lactic dehydrogenase which catalyze the reaction of pyruvate to
lactate, occurs, occurs in five different forms
Lactate + NAD+ LDH Pyruvate + NADH + H+
4. Competitive Inhibition
There are certain products which inhibit the enzyme activity which are known as enzyme
inhibitors. Enzyme inhibitors are of two types namely irreversible and reversible. Reversible
inhibition is of three types viz., competitive, non-competitive and uncompetitive inhibitors.
Competitive inhibitors depend on the fact the inhibitors have structural similarity with the
substrate both of which compete for the same active site of the enzyme. The inhibition is
 removed by increasing the concentration of the substrate. An example of competitive
inhibition is the inhibition of succinic dehydrogenase by malonic acid. Inhibition of the
activity of this enzyme is due to the structural similarity between malonic acid and succinic
acid.
5. How does enzyme work?
There is physical contact between enzyme and substrate. As only a specific key fits in a
particular lock to open it, similarly a specific substrate combines with the active site of the
specific enzyme to form enzyme substrate complex. This enzyme substrate complex break
after the substrate has been converted into the products and the enzyme is again set free.
The lock and key theory is supported from the study of the competitive inhibition of the
enzyme activity. Another theory is induced fit theory proposed by Koshland. According to
this theory when a suitable substrate approached the active site of the enzyme and as it forms
the enzyme substrate complex, substrate induces some configurational changes in the
enzyme. As a result, the attractive groups form a complementary structure so that the
catalytic group of the active site is in proximity of the bond to be broken. After the suitable
enzyme substrate complex has been formed, the substrate molecule held by the hydrogen
bonds is converted into the products and the enzyme is set free.
6. Specificity of an enzyme
The enzyme is specific in their action. The specificity lies in the fact that they may act.
1) Absolute specificity – Some enzyme are capable of acting on only one substrate eg.
Urease act only on urea
2) Group specificity- Some enzymes are capable of catalysing the reaction of a structurally
related group of compounds eg. Lactic dehydrogenase catalyze the interconversions of
pyruvic acid and lactic acid
3) Optical activity- A particular enzyme will react with only one of the two optical isomers
eg. Arginase act only on L arginine and not on its D- isomer
4) Geometrical specificity – Some enzymes exhibit specificity towards the cis and trans
forms eg., Fumarase catalyze the inter conversion
7. Factors influencing enzyme action
1) Temperature- The activity of enzyme is optimum at normal body temperature. At low
temperature, enzyme activity is minimum. An increase in temperature up to certain limit
increases the enzyme activity. Maximum being at about 45oC after which enzyme
activity is retarded.
2) pH- Enzymes is active only over a limited range of pH
3) Water- In absence pf water, the enzyme activity is suppressed. Proper hydration of the
cells is necessary for the enzyme activity
4) Substrate concentration- Enzyme activity increases with the substrate concentration
till the active sites of the enzyme are saturated with substrate
5) Enzyme concentration- Increase in concentration of the enzyme will increase the rate
of reaction catalysed by it provided there is enough concentration of substrate
6) Inhibitors – Presence of inhibitors in the reaction mixture inhibits the activity of the
enzymes partially or completely depending up on the nature of the inhibitors.
8. Lock and key hypothesis
Emil Fischer proposed the lock and key hypothesis to explain the mode of action of enzyme.
Interaction of substrate and enzyme is visualized in terms of lock and key model. Union
between the substrate and the enzyme takes place at the active site more or less in a manner
in which a key fits a lock and results in the formation of an enzyme substrate complex.
Enzyme substrate complex depends on a reciprocal fit between the molecular structure of
the enzyme and the substrate. This complex is unstable and almost immediately this
complex decomposes to produce the end products of the reaction and to regenerate the free
enzyme.
9 Inhibitors
There are certain products which inhibit the enzyme activity. These are known as enzyme
inhibitors. During the reactions, the active sites of the enzymes are filled up with these
substances instead of substrate molecules. Thus, the activity of the enzyme is lot. There are
two types of enzyme inhibitors viz., reversible and irreversible. Irreversible inhibition
results from the formation of a stable enzyme inhibitor ( EI) complex which results in
complete inhibition of the enzyme. Reversible inhibition is of three types – competitive
inhibition, non-competitive inhibition and uncompetitive inhibition. Incompetitive
inhibition,, inhibitor competes with the true substrate for the active site in the enzyme which
is removed by increasing the concentration of substrate. In non-competitive inhibitions, the
inhibitors react with enzyme to reduce catalytic activity without preventing the formation
of enzyme substrate complex. In case of uncompetitive inhibitions, the inhibitor is thought
to combine with forms of the enzyme, but they do not combine actually with the substrate.
In the case of allosteric inhibition, the inhibitor is structurally different from substrate is
bound at a site other than the active site of the enzyme. This alters the configuration of the
enzyme protein and thereby prevents it from binding of the substrate.
10. Allosteric enzyme
It is found that when a series of reaction is catalysed by a number of enzymes in sequence,
the accumulation of the final end product may cause inhibition in the activity of the first
enzyme of the series. This inhibition due to a compound which is totally different in
structure from the substrate of the enzyme is called as allosteric inhibition or feedback
inhibition and such as enzyme is called as allosteric enzyme. This type of inhibition takes
place due to presence of allosteric sites on the surface of the of the allosteric enzyme away
from the active site. The final end product molecule fits in the allosteric site and in some
way brings about a change in shape of the enzyme so that the active site of the enzyme
becomes unfit for making complex with the substrate. The allosteric inhibition id
reversible. When the concentration of the final end product in the cell falls, it leaves the
allosteric site and the activity of the allosteric enzyme is restored.
11. Active site
Since the substrate molecules are comparatively much smaller than the enzyme molecules,
there should be some specific regions on the enzyme for binding with the substrate. Such
specific regions are variously called as active site or catalytic site or substrate sites. The
active site present in different enzymes has the following common feature
 a) Active site occupies very small portion of the enzyme molecule
b) The active site is neither a point or a line or even a plane in a 3D entity
c) The arrangement of atoms in the active site is well defined resulting in the marked
Specificity of the enzymes
d) The active site binds the substrate molecules by relatively weak force
e) The active site in the enzyme molecules are grooves or cervices from which water is
``largely excluded
12. Enzyme modifiers
The catalytic activity of certain enzymes is reversibly altered by certain inorganic and
organic molecules called modifiers. Those molecules which increase the enzyme activity
are called positive modifiers or activators and those which decrease the enzyme activity
are negative modifiers or inhibitors. Many metals act both as positive and negative
modifiers, whereas certain organic molecules retard enzyme activity, thus acting as
negative modifiers. The inorganic modifiers (enzyme activators) are mostly metals.
Certain enzymes apart from a requirement of coenzymes also need a metal ion for full
activity. Removal of metal often results in partial or total loss of enzyme activity. The
activity is however restored by replacing the metal ions. Such metal ions include K+,
Cu+, Fe2+, Mg2+, Ca2+, Mn2+, Zn2+ etc., . For eg, Fe, Cu and Mo are required in oxido
reduction reaction. Mg is needed for phosphate reaction. The mechanism on how metal
ion brings about activation include as direct participation in catalysis, formation of
metallo substrate, formation of metalloenzymes. Alteration of equilibrium constant and
conformational change in the enzyme. Organic modifiers (enzyme inhibitors) are of two
types reversible and irreversible. Reversible inhibition include competitive, non-
competitive and uncompetitive.
ESSAY TYPES
1. Explain in detail about classification of enzymes
Enzymes may be classified according to the type of reaction that they catalyze
a) Oxido reductases- These enzymes catalyze reaction in which one substrate is oxidize,
acting as hydrogen donor, and another substrate is reduced. The Oxido reductases
include the dehydrogenases which convert single bonds to double bonds and the
oxidases which user oxygen as the oxidant. Others include peroxidases which use H2O2
as the oxidant, the hydrolases which introduce hydroxyl group and the oxygenases
which introduce molecular oxygen in place of a double bond in a substrate
b) Transferases- Enzymes in this class transfer one carbon group (methyl aldehyde or
Ketonic groups, or phosphoryl/ or amino group and so on from one substrate to another
eg., transaminases, transaldolases
c) Hydrolases- It catalyze the hydrolytic (water adding) cleavage of C-O, C-N, C-C and
other single bonds. The class includes peptidases, esterases, glycosidaes, phosphatases
d) Lyases- These enzymes cleave bonds without the addition of water, but by elimination
reactions to form double bonds or rings. It also catalyzes the reverse reaction. Usually
C-C, C==O , C=N bonds are acted upon eg., decarboxylases, aldolases, dehydralases
e) Isomerases- Racemases, epimerases cis- trans isomerases, intramolecular oxido
reductases , mutases which alter the structure, but not the atomic composition of
substrates
f) Ligases- enzyme in this class, also known as synthetases, couple the hydrolysis of a
pyrophosphate in ATP or other triphosphate to a second reaction in which two
molecules are joined eg., RNA ligase will form a new phosphodiester bonds
2) Discuss the biochemical action of vitamins as coenzyme
Vitamins are organic substances which cannot be synthesized by some organisms and
must therefore be supplied to them regularly out in small quantities in order to ensure a
normal metabolism. Certain vitamins, notably water soluble vitamins and particularly
the B group vitamins are coenzymes or essential constituents of coenzymes. It must be
noted that the same compounds often serve as coenzymes for all living organisms, but
vitamins only for some of them.
1) Nicotinamide Adenine dinucleotide (NAD)- It is coenzyme of various
dehydrogenases. It binds the hydrogen originating from a substrate AH2 and transforms
into NADH+ H+
2) Nicotinamide Adenine dinucleotide phosphate (NADP) – It is also coenzyme of
some dehydrogenases very similar to NAD. It differs only by an additional phosphate
residue esterified on the hydroxyl in 2' of the ribose to adenine. It is a hydrogen acceptor
3) Flavin nucleotides- Flavin mononucleotides (FMN) and Flavin adenine dinucleotide
(FAD) are also coenzymes of dehydrogenases often called flavour proteins. These two
coenzymes derive from riboflavin or vitamin B2. They are involved in the process of
cell oxidation by fixation- reversible of 2H. Succinate dehydrogenases is an eg. of FAD
enzyme
4) Ferro prophyrin- These ferro prophyrin coenzymes are associated with cytochromes
5) Lipoic acid- This coenzyme acts as hydrogen transporter in the oxidative
decarboxylation reactions, particularly in that of pyruvic acid
6) Thiamine pyrophosphate (TPP) - The pyrophosphoric ester of thiamine or vitamin
B1 is an integral part of the active site of Carboxylase. It is a transporter of aldehyde,
particularly acetaldehyde. It is a coenzyme of decarboxylases of α- keto acids
7) Coenzyme A- Coenzyme A derives from B group vitamins, the pantothenic acid.
Coenzyme A is important in the oxidation of fatty acid as well as in biosynthesis of
fatty acid
8) Tetrahydrofolic acid- It is the active form of a vitamin folic acid. It is coenzyme
transporter of C1 units which behaves as a substrate and is involved in a large number
of processes like biosynthesis of purine ribonucleotides, glycine-serine
interconversions.
9) Biotin- It is coenzyme of different carboxylation reactions. It is involved in the
carboxylation of acetyl coenzyme A into malonyl coenzyme A in the synthesis of fatty
acid.
 10) Pyridoxal phosphate- It is coenzyme derivative of pyridoxine or vitamin B6. It is an
integral part of the active site of various enzymes involved in the metabolism of amino
acids, transaminases, amino acid decarboxylases
11) Cobamide coenzymes- It is derivative of cobalamine or vitamin B12. It is involved
in various isomerisation reaction especially transfer of carboxyl group in the case of
isomerisation of methyl malonyl CoA to succinyl Coenzyme A
3) Discuss the chemical nature and properties of enzymes. State briefly how an
enzyme exerts its catalytic activity?
Chemical nature
The enzymes are essentially proteins and possess properties characteristic to these.
Enzyme is considered as a protein with catalytic properties due to its power of specific
activation. Enzymes contain C, H, N and S. It has amphoteric property. It undergoes
Denaturation and form antibodies. Chemically the enzyme may be divided into two
categories
1) Simple- protein enzymes- They contain simple proteins eg., Urease, amylase
2) Complex- protein enzymes- Thèse contain conjugale proteins. They have protein part
called Apoenzyme and non-protein part called prosthetic group associated with the
protein part. The two parts constitute what is called as holoenzyme eg. Catalase,
cytochrome the activity. The activity of an enzyme depends on the fact that non-
proteinaceous prosthetic group is intimately associated with the protainaceous
Apoenzyme
Conjugate-protein enzyme protein part + prosthetic group
Holoenzyme Apoenzyme + coenzyme
Coenzymes are thermostable, dialyzable organic compounds and account for 1%
of the entire enzyme molecule
Properties of enzyme
2) Catalytic power- Only small amount of enzyme is enough to convert large quantity of
the substrate into products. Their turn over number ie., the number of substrate
molecules converted by one molecule of the enzyme per second when its active site is
saturated with substrate
3) Specificity – Enzymes are very specific in their action. A particular enzyme usually
acts on a particular substrate to catalyze a particular type reaction
4) Reversibility- In most of the cases, the reactions catalyzed by the enzymes are
reversible depending upon the requirement of the cell. But in some cases, there are
separate enzymes for forward and backward reactions
5) Thermolabile- The enzymes are very sensitive to heat. They are inactivated at very
low temperature. At a very temperature (60-70oC) usually they are destroyed.
6) Inhibitors- Enzymes are sensitive to inhibitors, while some inhibitors may be partially
inhibit their activity; other inhibitors destroy them permanently and inhibit activity.
7) Colloidal nature- The enzymes are of colloidal dimensions and present large surfaces
for reactants in water to facilitate the enzyme reaction
 Mode of action of enzyme is explained by two theories
2) Collision theory- Some enzymes need water to break the bond, while others require
compounds of low molecular weight to make the enzyme active. The enzyme like
lipases, chymotrypsin, phosphatases generally catalyze the reaction following way

EH + Rx ER + Hx
Enzyme Substrate Intermediates
ER + H2O ROH + EH
On summing up Rx + H2O ROH + Hx
Other enzymes like hexokinases, Co A Transferases catalysed the reaction in the
following manner:
E + AB E-A + B
E-A + C E + AC
The enzyme (E) first combines with A part of the compound (AB) and conserves the
bond energy. It reacts with (C) compound to form (AC). Water molecules here do not
react with ( E-A) complex and the energy of the bond is conserved to be used for the synt
Enzyme-substrate complex theory- It was proposed by Michalis and Menton
Enzyme + Substrate Enzyme – substrate complex
Enzyme- substrate complex Enzyme + product
The substrate combines with the enzyme and leaves the enzyme surface in the form of
reaction products. Enzyme substrate complex is formed as intermediates which are
decomposed rapidly into the enzyme and the product molecules of a new compound
(AC).
4 Describe in detail the various factors which affect the enzyme activity
The rate of an enzyme- catalysed reaction is influenced by the following environmental
factors
1) Enzyme concentration- Enzyme molecules are larger than the substrate molecules.
They possess many active sites in which the substrate molecules get attached at the time
of reaction. The reaction proceeds until all the active sites of the enzyme molecules are
filed by the substrate molecules.
2) Substrate concentration- If the enzyme concentration is fixed and the substrate
concentration is relatively higher, the velocity of the reaction is increased to its
maximum. If the substrate concentration is relatively low at a particular enzyme
concentration, the reaction proceeds, but at slower rate because the active sites of only
few enzyme molecules become saturated with the substrate molecules. An increase in the
substrate increase the rate of reaction and if the substrate concentration is increased
beyond a limit, when all the active sites of the enzyme molecules have become saturated,
the reaction will become constant without accelerating the velocity.
3) Temperature.-The rates of enzyme catalysed reaction are increased as the
temperature is raised. The enzyme catalysed reaction show the increase in velocity
between 25-35oC. At 0oC, the enzyme become inactivated, but not destroyed. At 60 to
 70oC, the enzymes are inactivated and destroyed. It is due to coagulation and
Denaturation.
4) Hydrogen concentration- Hydrogen ion concentration of an enzyme solution has a
marked effect on its activity. Every enzyme act at a particular pH. The pH at which the
rate of reaction is maximum is called as optimum pH range. If the pH value is increased
or decreased at either side of the optimum pH range, the rate of reaction usually
decreases. At extreme pH the enzymes are denatured and inactivated. The hydrogen ion
concentration also alters the ionization, solubility of the substrates, inhibitors, activators
and absorbed ions
5) Effect of ions- The cations like Mg2+, Ca2+, Mn2+, Zn2+,Na+ or K= play
important role in the activity of certain enzymes. These enzymes on the absence of a
particular cation remain inactive.
6) Accumulation of products- The accumulation of products of enzyme catalyzed
reaction may increase the rate of reverse reaction. The enzymes become inactive due to
accumulation of these products on the surface of the enzyme molecules itself. They may
also change the pH of the enzyme solution.
5) Write an account on the occurrence and nomenclature of enzymes
Every cell synthesizes its own enzymes with the help of genes. The synthesized enzymes
are then distributed to the different parts of the cell and ultimately to the different parts
of the plant or animal body. The enzymes that are produced within the cell for metabolic
activities are known as endoenzymes and those which act away from the site of synthesis
are called exoenzymess
Since the enzymes are specific for a particular reaction, they are named according to the
substrate on which they act or on the nature of reaction they catalysed. The most common
methods for naming them is suffix ase at the end of the name of the substrate attached.
Thus peptide is attacked by peptidases, lipid by lipase, and urea by urease
The international commission established a numerical system of classification
1) Each enzyme has a systematic code number ( EC) of four digits
2) The first digit of the four figures indicate the main class
3) The second digit indicates the subclass
4) The third digit indicates the subdivision of sub class
5) The fourth digit designates the aerial number of the specific enzyme in the fourth
sub –class
6) In the system of nomenclature, enzyme commission recommends both systematic
and trivial names for enzymes for eg, EC.1, 1, 1, 1 stands for the enzyme alcohol
dehydrogenase EC stands for the enzyme commission
1. Stands for oxido reductases
1.1. Stands for enzyme which utilizes substrate as CHOH (alcohol group)
1.1.1. Stands for the enzymes which utilizes NAD as an acceptor
6). Give a brief note on the practical application of enzymes
1) Wine manufacturing- Papain is used in brewing industry as a stabilizer for chill proof
beer
 2) Cheese making- An enzyme lipase is added to cheese for imparting flavour to it.
3) Candy making- Invertase helps preventing granulation of sugars in soft cantered
candies
4) Bread whitening- Lipoxygenase is used for whitening of bread
5) Clarifying fruit juice- Pectic enzymes is used for clarifying the fruit juice
6) Destaining and desizing fabrics- Alcalase is used for removing stains due to glue,
gelatin or starch.
7) Wound healing- Proteolytic enzymes are used to alleviate skin diseases, bed sores
8) Analysing biochemical- Uricase and urease are employed in the determination of
uric acid and urea respectively
9) Diagnosing hypertension- Radio immunoassay procedure is used for diagnosing
cases of hypertension by employing a proteolytic enzymes secreted by the kidneys.
10) Syrup manufacturing- Immobilized glucose isomerase is being used in the
production of high fructose core syrup
7) Write a detailed account on enzyme inhibition
There are certain products which inhibit the enzyme activity. These are known as enzyme
inhibitors. During the reaction, the active sites of the enzymes are filled up with theses
inhibitors instead of substrate molecules. Thus the activity of the enzymes is lost. There
are two types of enzyme inhibition 1) irreversible 2) reversible. Irreversible inhibition
results from the formation of a stable enzyme inhibitor (EI) complex which results in
complete inhibition of the enzyme. Reversible inhibition is of three types a) Competitive
inhibition b) Non- competitive c) Uncompetitive
A) Competitive inhibition- this type of inhibition depends on the fact the inhibitor
competes with the true substrate for the active site of the enzyme. The inhibition is
retrieved by increasing the concentration of the substrate eg. The inhibition of succinic
dehydrogenase by malonic acid since molecular structure of succinic acid is very similar
to malonic acid. Because of this similarity in structure, the enzyme can react with both
to form complex. However, only the enzyme- succinic acid complex decomposes to yield
a reaction product
E + Iki KI EI
Where E is the enzyme, I is inhibitor (malonic acid0, Ki inhibitor association constant
and EI enzyme inhibitor complex.
B) Non- competitive inhibition- In non- competitive inhibition, the inhibitor reacts
with the enzyme to reduce catalytic activity without preventing the formation of enzyme
– substrate complex. The affinity of the enzyme for substrate is not reduced, but
maximum velocity of the reaction is reduced eg. Fluoride ion inhibits enolase and
thiocyanate ion inhibit fumarase. Inhibition cannot overcome by increasing substrate
concentration,
C) Uncompetitive inhibition- The inhibitor is thought to combine with forms of the
enzyme, but they do not combine actually with the substrate. These forms of the enzyme
are known as substrate non- combining forms and cannot then be converted back to the
 substrate combining forms of the enzyme. This type of inhibition is not relieved by
increasing the concentration of the substrate.
D) Allosteric inhibition- The inhibitor is structurally quite different from the substrate,
is bound at asite other than the active site of the enzyme. This binding of the inhibitor
alters the conformation of the enzyme protein and thereby prevents it from binding to the
substrate. Since the inhibitors bind at a site other than the active site of the enzyme, they
are called allosteric effectors and phenomenon is called as allosteric effect.
8) Explain the mechanism and co enzymatic action with suitable examples
Mechanism of enzyme action
The mechanism of enzyme action is explained by collision theory and enzyme substrate
complex theory
1) Collision theory- Some enzymes need water to break the bond, while others require
compounds of low molecular weight to make the enzyme active. The enzyme like lipases,
chymotrypsin, phosphatases generally catalyze the reaction following way
EH + Rx ER + Hx
Enzyme Substrate Intermediates
ER + H2O ROH + EH
On summing up Rx + H2O ROH + Hx
Other enzymes like hexokinases, CoA Transferases catalysed the reaction in the
following manner:
E + AB E-A + B
E-A + C E + AC
The enzyme (E) first combines with A part of the compound (AB) and conserves the
bond energy. It reacts with (C) compound to form (AC). Water molecules here do not
react with ( E-A) complex and the energy of the bond is conserved to be used for the
synthesis of a new compound ( AC).
2) Enzyme-substrate complex theory- It was proposed by Michaelis and Menton
Enzyme + Substrate Enzyme – substrate complex
Enzyme- substrate complex Enzyme + product
The substrate combines with the enzyme and leaves the enzyme surface in the form of
reaction products. Enzyme substrate complex is formed as intermediates which are
decomposed rapidly into the enzyme and the product molecules.
Mechanism of Co enzyme action
The coenzyme is as essential a reactant as the substrate that is activated by the enzyme.
The following equation represents the reaction of the coenzyme with the substrate
Substrate (A) + Co enzyme Enzyme A Substrate (A) derivatives+ Co enzyme derivatives
The coenzyme is regenerated and again becomes available as an essential component for
the above reaction
Substrate ( B) + co enzyme derivative Enzyme B Substrate ( B) derivative + coenzyme
The function of coenzyme in the enzymatic reactions is thus to assist in their cleavage of
the substrate by acting as an acceptor for one of the cleavage products.
 The function of coenzyme in the enzymatic reactions is thus to assist in their cleavage of
the substrate by acting as an acceptor for one of the cleavage products.

Substrate + Apoenzyme + coenzyme

○-∆
∆

Fig1. Function of coenzymes

For eg. Dehydrogenases utilize NAD+ or NADP. Their functions is to transfer the
hydrogen nuclei with two electrons from the substrate, thus oxidizing it
Substrate + NAD+ + Enzyme oxidized substrate + NADH + H+
VITAMINS
Fill up the Blanks
1. The fat soluble vitamins are A , D, ___ and ____
2. The water soluble vitamin ae ____ and ______
3. Vitamin A is also called as________
4. Thiamine is also called as ________
5. Vitamin B2 is called as _______
6. Niacin is also called by _______
7. Ascorbic acid is referred as ________
8. Vitamin D is also called as ________
9. Vitamins often act as ________
10. A steroid vitamin is _______
11. Ascorbic acid act as a ______ agent
12. The first person to discover vitamins was ________
13. The cobalt containing vitamin is _______
14. Vitamin C is considered as __________ in water
15. The vitamin that act as coenzyme is ______
16. The most important function of vitamins is to serve as ________
17. Among the vitamins, ________ show greater deficiency in body
18. Several vitamins have strong ________ potential
19. Vitamins which are not stored in body are called_____
20. Vitamin which doesn't act as a coenzyme is_______

ANSWER
Sl.No Answer Sl.No Answer
1 E and K 11 Reducing
2 B and C 12 Funk
3 Retinol 13 Vitamin B12
4 Vitamin B1 14 Soluble
5 Riboflavin 15 Vitamin B complex
6 Vitamin B3 16 coenzyme
7 Vitamin C 17 Water soluble
8 Calciferol 18 Antioxidant
9 Co enzyme 19 Water soluble
10 D 20 Vitamin C

Essay type
1) General characteristics of vitamins
a. Vitamins occur in plants, animals as well as microorganisms, i.e. it has widespread
occurrence.
b. The plants and many microbes can synthesize all the vitamins, whereas only a few
vitamins are synthesized in animals.
c. Human body can synthesize some vitamins. For eg. Vitamin A from precursor
carotene and Vitamin D from ultraviolet irradiation of 7-dehydrocholesterol. Some
members of Vitamin B- complex are synthesized by micro-organisms present in the
intestinal tract. Vitamin C is also synthesized in some animals such as rat.
d. All the cells of the body store vitamins to some extent.
e. Vitamins are partly destroyed and partly excreted.
f. Vitamins are non-antigenic.
g. Most of the vitamins are coenzymes, however few are haematopoietic.
h. Vitamins carry out functions in very low concentration; hence total daily requirement
is very small.
i. Vitamins are effective when taken orally.
 j. A lack of one or more vitamins (avitaminosis) leads to characteristic deficiency
symptoms in humans as well as in animals.
2). Function of vitamins
A vitamin is an organic compound and an essential nutrient that an organism requires in
limited amounts. Vitamins have diverse biochemical functions.
1. Hormone-like functions as regulators of mineral metabolism ( Vitamin D)
2. Regulators of cell and tissue growth and differentiation ( Vitamin A)
3. As antioxidants (e.g., vitamin E and sometimes vitamin C)
4. Enzyme cofactors (tightly bound to enzyme as a part of prosthetic group, coenzymes
(vitamins, the B complex). In this role, vitamins may be tightly bound to enzymes as
part of prosthetic groups: For example, biotin is part of enzymes involved in making
fatty acids

3) Classification of vitamins
The body needs 13 vitamins for normal health. These include vitamins A, C, D, E, K
and the B complex (thiamine, riboflavin, niacin, pantothenic acid, biotin, vitamin B 6,
B 12 and folate. Each of these vitamins provides various functions for the body. Under
normal circumstances, a person can obtain all of the vitamins he needs from eating a
well-balanced diet.
Vitamins are classified several different ways, according to how they travel through
your body and the various roles they play in keeping you healthy (Vitamins are
classified by their biological and chemical activity). Vitamins are classified primarily
as to solubility. Some are soluble in fat and some in water. Vitamins that are fat soluble
are stored in the body and can accumulate. Water soluble vitamins are flushed out by
the kidneys.
1- Fat soluble vitamins:
a) Vit. A (Retinol, Retinal, Retinoic acid)
b) Vit. D (Vit. D3: Cholecalciferol, Vit. D2: Ergocalciferol)
c) Vit. E (α-Tocopherol)
d) Vit. K (Vit. K1: Phylloquinones, Vit. K2: Menaquinones)
2-Water soluble vitamins:
(A) Vit. B group
B1 (Thiamin)
B2 (Riboflavin)
B3 (Niacin)
B5 (Pantothenic acid)
B6 (Pyridoxine)
B9 (Folic acid)
B12 (Cyanocobalamin)
B) Vit. C : (l-Ascorbic acid)
(C) Vit. H: (Biotin)
Definition
1. Vitamins: Any of a group of organic compounds which are essential for normal growth
and nutrition and are required in small quantities in the diet because they cannot be
synthesized by the body.
2. Water soluble vitamins: A vitamin that can dissolve in water. Water-soluble vitamins
are carried to the body's tissues but are not stored in the body. Water-soluble vitamins are
found in fruit, vegetables and grains.
3. Fat soluble vitamins: A vitamin that can dissolve in fats and oils. Fat-soluble vitamins
are absorbed along with fats in the diet and can be stored in the body’s fatty tissue. They
come from plant and animal foods or dietary supplements Vitamins A, D, E, and K are
fat-soluble.
 PLANT HORMONES
Plant‘s growth and development are under the control of two sets of internal factors. Nutritional
factors such as supply of carbohydrates, protein, fats and others constitute the raw materials
required for growth. Proper utilization of these raw materials is under the control of certain
chemical messengers which can be classified into hormones and vitamins

The term hormone is derived from a greek root “hormao” which means “to stimulate”( Beylis
and Starling, 1902). Thimann (1948) suggested using the term “phytohormone” for hormones
of plant
A hormone is a naturally produced chemical synthesized in one part of the plant and then travels
to another part where it effects growth and development. Hormone- gr. to excite. Organic
substances produced in small amounts that regulate and coordinate metabolism, growth, and
morphogenesis

Plant Growth regulators

Plant growth regulators (PGR) refers to natural or synthetic substances influence the growth
and development
IAA ( Auxin) – both natural and synthetic
IBA (Auxin) – Always synthetic
All plant hormones are plant growth regulators, but all plant growth regulators are not plant
hormones
Six Major Classes of Plant Hormones
Auxins
Leaf primordia, young leaves, developing seeds.
Polarly (unidirectionally) and nonpolarly.
Cytokinins
Root tips.
From roots to shoots via xylem.
Ethylene
Most tissues in response to stress.
Diffusion from site of synthesis.
Abscisic acid
Mature leaves and roots, seeds.
From leaves in phloem and from the roots in the xylem.
Gibberellins
Young tissues of the shoot and developing seeds.
Xylem and phloem.
Brassinosteroids
Young tissues and throughout the plant.
They act locally.
Classification of PGR
a) On the basis nature of function
Growth promoting hormones / growth regulators: Increase the growth of the plants
Eg Auxin, Gibberellin and cytokinins
b) Growth inhibiting hormones/ growth retardant
Inhibit the growth of the plant
Eg, ABA, ethylene
Auxin
Derived from the greek word “ auxein” means “to grow/increase”. Auxins may be defined as
growth promoting substances which promote growth along the vertical axis when applied in
low concentration to the shoot of the plant
The idea of existence of auxin was proposed by Charles Darwin (1880) in his book “The power
of movements in plants”. Coleoptiles of canary grass to unilateral light and observed it to bend
towards light. He covered the coleoptiles tip with tin foil or cut it off and observed that
coleoptiles did not bend towards unilateral light. Concluded some stimulus is transmitted from
upper to the lower part which induced bending of the coleoptiles
Auxin – promotes plant growth causes elongation of developing cells. Increases the
concentration of hydrogen ion in primary walls, in turns, loosens cellulose fibers which
increase cell wall plasticity. In response, turgor pressure causes the cell expand, thus generating
growth. It is produced at the tips of shoot and roots. Active phototropism and geotropism.
Active in leaves, fruits and germinating seeds

Cytokinins
Group of hormones that stimulate cytokinesis (cell division).
Produce mainly in the roots and transported throughout the
plant. Stimulates the growth of lateral buds, thus weakening
apical dominance.

Cytokinins Promote Cell Division

Gibberellins (gibberelic acid- GA)
Promotes cell growth; Synthesized in young leaves, roots, and seeds. Involved in the promotion
of fruit development and seed germination. High concentrations of GA causes rapid elongation
of stems called bolting.
It was discovered by Japanese plant pathologist Kurosawa in the year 1928. Rice plants was
infected by fungus Gibberella Fujikurai showed excessive cell elongation. The symptom is
called Bakane disease. Chemical was extracted and purified and named as Gibberellic acid.
Now there are 80 type of gibberelic acid. The most common is GA3 .

Ethylene
Gas- C2H4
Promotes the ripening of fruit. Involved in stimulating the production of flowers. In
combination with auxin, ethylene inhibits the elongation of roots, stems, and leaves, and
influences leaf abscission, the aging and dropping of leaves.
Abscisic acid (ABA)
Discovery: F.T. Addicott and his associates discovered abscisic acid in the early 1960s in the
process of studying abscission in cotton. Bud Dormancy -- This is influenced by cytokinins
and auxin-induced synthesis of ethylene.
Abscisic Acid (ABA) Prevents Seed Germination
Seed Dormancy -- Abscisic acid delays seed germination in many plants. Has some effect on
induction and maintenance of dormancy in general. Induces seeds to synthesize storage
proteins. Inhibits the effect of gibberellins on stimulating de novo synthesis of a-amylase
Abscisic Acid Plays a Role as a Root-to-Shoot Signal
Biomass production by plants is regulated by water availability. A limited water supply in the
soil is sensed by roots and communicated to the shoot to allow timely adjustment of the plant’s
transpiration. Abscisic acid plays a pivotal role in adjustment of plants to abiotic stress
conditions abscisic acid (ABA) is the long‐distance signal that communicates water stress from
the root to the shoot.
Abscisic Acid is Responsible for Stomatal Closure

Closure of Stomata --
Large amounts of abscisic acid in the leaves causes the stomata to close which helps the plant
conserve water during droughts. Reactions can be instigated within minutes of spraying.
commercially it is used in fields when droughts threaten.
Fill up the blanks
1) The term auxin was coined by ______
2) The precursor of indole acetic acid (natural auxin) is _______
3) _______ is the gaseous hormone
4) The rooting hormone is ______
5) The auxin which is used as weedicide is _______
6) _________ is synthetic auxin
7) Nodule formation is induced by _____
8) Bud initiation in shoots in promoted by_______
9) Bolting of some rosette plants is promoted by______
10) Regulators of plants growth are produced in ___________
11) Synthetic hormones used for ripening is _____
12) Combination of hormones which cause apical dominance and bolting in plants is
______ and _______
13) Maximum seed germination occurs when seeds are treated with ______
14) _________ is growth inhibiting hormones
15) Auxin promotes growth in plants by________
16) Plants synthesize auxin from the amino acid_______
17) This plant hormone promotes stem elongation and enzyme production in developing
seeds is ____
18) _______ is produced by aging fruit
19) The hormone promotes lateral bud dormancy is _______
20) Plant hormone inhibits the effects of other hormones is ____
21) Plant hormone causing, abscission of leaves, senescence, bud dormancy and inhibition
of cell division is _______
22) A dwarf plant can be induced to reach normal height by the application of: _______
23) Removal of the tip of a plant stimulates lateral growth AND the plant gets bushier,
because the tip of a stem produces _______
24) Auxins are produced at or near the tips of roots and stems in areas called______
25) Any substance produced in one part of the plant that affects another part is a ________
26) A ripe Avocado will cause other avocados to ripen through the release of ______
27) Seedless fruits can be produced by the application of auxin or:_______
28) Extraordinary growth in the height of a plant would be caused by: _____
29) Substances that stimulate cell division and cause dormant seeds to sprout are:_____
30) Ethylene differ from other plant hormones as it is ____
31) A high concentration of auxins can inhibit plant growth. Many of these compounds
could be used as ______
32) Plant hormone which saves the crops from falling is _____
33) Plant hormone which helps in formation of proteins and RNA is ____
34) The dormancy of the plant is broken by application of ________
35) Hormone which help in the cell division and development in the presence of auxin is
____
36) The hormone which increases the cambium activity in the wooden plants is _____
37) Apical dominance is affected by the hormone _________
38) Delay in senescence is caused by the spray of ________
39) Abscission is prevented by ______
40) High concentration of ethylene is present in ________
41) The precursor of ethylene is _______
42) All the climatic fruits except_____ respond to ethylene application
43) _______ hormone promotes release of ethylene
44) ABA act as antagonistic to _______
45) Hormones promote stem elongation and stimulate enzyme production in germinating
seeds is ________
46) Plant hormones stimulate cell division in the presence of auxin, promote chloroplast
development and bud formation, and delay leaf aging is ___
47) The site of gibberellic acid production in the plant is __________
48) At the cellular level, hormone important in triggering cell division is _______
49) _____ can be sprayed on peach trees in the spring to cause fruit or flowering thinning.
50) Sprouting of potatoes is inhibited by__________
51) _________ is referred to as stress hormone
52) Gibberellin is named after the fungus _______
ANSWER
Sl.No Answer Sl.No Answer
1 F W Went 27 Gibberellins
2 Tryptophan 28 Auxin
3 Ethylene 29 Cytokinins
4 NAA 30 Gas
5 2,4 D 31 Herbicides
6 NAA, 2,4 D and 2,4,5 T 32 Auxin
7 IAA 33 Cytokinins
8 Auxin 34 Gibberellins
9 Gibberellins 35 Cytokinins
10 Phytohormones 36 Gibberellins
11 Ethephon 37 IAA
12 Auxin , Gibberellins 38 Abscisic Acid
13 Gibberellins 39 Ethylene
14 Abscisic acid and Ethylene 40 Ripening fruits
15 Stem elongation 41 Methionine
16 Tryptophan 42 Grapes
17 Gibberellins 43 Abscisic Acid
18 Ethylene 44 Gibberellic acid
19 Abscisic Acid: 45 Gibberellins
20 Abscisic Acid: 46 Cytokinins
 21 Abscisic Acid: 47 Leaf
22 Auxin 48 Cytokinins
23 Auxin 49 Abscisic Acid:
24 Apical meristems 50 2,4 D
25 Hormone 51 Abscisic Acid:
26 Ethylene 52 Gibberella fujikoroi

Essay type
1, Plant hormone or plant growth regulator
Thimann (1948) designated the plant hormones by the term ‘phytohormones’ in order to
distinguish them from animal hormones. Johannes van Overbeek (1950) defined plant
hormones as “organic compounds which regulate plant physiological process regardless
of whether these compounds are naturally occurring and/or synthetic ; stimulating and/or
inhibitory ; local activators or substances which act at a distance from the place where
they are formed.” Plant hormones, also known as phytohormones are chemicals that
regulate plant growth. In plants, these are produced by cells in one area of the plant, such
as leaves, stems or roots and then transported to a different area of the plant in order for
them to have a response. Plant hormones shape the plant, affecting seed growth, time of
flowering, the sex of flowers, senescence of leaves, and fruits. They affect which tissues
grow upward and which grow downward, leaf formation and stem growth, fruit
development and ripening, plant longevity, and even plant death. Hormones are vital to
plant growth, and, lacking them, plants would be mostly a mass of undifferentiated cells.
So they are also known as growth factors or growth hormones. Plants lack glands that
produce and secrete hormones. Instead, each cell is capable of producing hormones.
Hormones are transported within the plant using localised movement and cytoplasmic
streaming within cells and slow diffusion. Phloem and Xylem are vascular tissues that
also help in the transportation of hormones from one part of the plant to another. Plant
hormones can be classified into five major categories, some of which are made up of
many different chemicals that can vary in structure from one plant to the next. The
classifications is based on chemical structural similarities and their effects on plant
physiology. Each class has positive as well as inhibitory function and work in tandem
with each other, interplaying to affect growth regulation. Abscisic acid, Auxins,
Cytokinins, Ethylene and Gibberellins
2. Role of Auxin in plants
Kögl and Haagen-Smit (1931) introduced the term ‘auxin’ (auxeinG = to grow or to
increase) for designating those plant hormones which are especially concerned with cell
enlargement or the growth of the shoots. An auxin may, thus, be defined as “an organic
substance which promotes growth (i.e., irreversible increase in growth) along the
longitudinal axis when applied in low concentrations to shoots of the plants freed as far
as practicable from their own inherit growth promoting substances. Auxin is a plant
phytohormone involved in practically every dimension of plant development, including
 responses to light and gravity, organ patterning, vascular development and regulating
intrinsic growth and environmental responses in both shoot and root architecture. The
auxin in plant shoots cause them to grow away from gravity or upwards, while the auxins
in roots cause them to grow towards gravity or downwards. There are four auxins that
exist in nature and are synthesized by plants. Since their discovery, more auxins have
been derived from existing ones and others have been synthesized in the laboratory. The
most prevalent of the natural auxins is indole-3-acetic acid (IAA), which is produced by
algae, plants, bacteria, and fungi. IAA thickens the cambium layer of plants by actually
enlarging xylem cells. Another agriculturally significant auxin is indole-3-butyric acid
(IBA), a synthetic form of which is used in a variety of products available to boost
propagation rates. If you have used a rooting hormone products on your cuttings to make
clones, it is highly likely you were using IBA to initiate adventitious root production.
Functions
1) Eradication of weeds: Auxins are being used as weedicides mainly due to their
selective herbicidal nature ,toxic residues of auxins disappear from soil very
soon.2,4-D is used to destroy broad leaved divots(mostly weeds).However auxins
like 2,4-D and 2,4,5-T are nontoxic to narrow leaved plants i.e monocots.
2) Root initiation: Application of auxins activates root initials. Rapid adventitious root
formation is absolutely essential in cuttings for their successful development into new
plants in vegetative propagation. Auxins like IAA, IBA, NAA,2,4-D when applied in
low concentration from 10–1000ppm on cuttings initiate adventitious root formation.
3) Flower initiation: Auxins normally inhibit flowering. However in litchi and
pineapple (Annanus sativus) auxins like 2, 4 -D and NAA have been found to
promote flowering.
4) Production of parthenocarpic fruits: The conversion of ovary into fruit had been
believed mainly due to the activity of auxins.
5) Apical dominance and dormancy: Auxins recommended for increasing the
dormancy period in potato tubers is methyl ester of naphthalene acetic acid.
6) Enzymatic activity: the auxins stimulate the activity of enzymes (conjugated with
aspartic acid).They show inhibitory effect on isoenzymes like peroxidase in tobacco.
7) To prevent premature fruit drop: Auxins have been successfully employed for
checking premature fall of fruits because their application prevent the formation of
abscission layer
3) Role of gibberellin on plants
The gibberellins are weakly acidic phytohormones which help in longitudinal growth of
stem. .In 1926, a plant pathologist Kurosawa, discovered the causative agent of the
disease (bakanae disease) as a fungus Gibberella fujikoroi. Yamuta and Sumuki (1938)
demonstrated that some substance secreted by this fungus was responsible for the
elongation and they later isolated this substance and named it gibberellin A3 or
gibberellic acid (GA). There are more than 70 gibberellins isolated. They are GA1, GA2,
GA3 and so on. The GA3 Gibberellic acid is the most widely studied plant growth
Gibberellins are chemically different from auxins, in that they contain gibbane ring
system with specific biological properties
Gibberellins are the plant growth regulators involved in regulating the growth and
influencing different developmental processes which include stem elongation,
germination, flowering, enzyme induction, etc.

Functions of Gibberellins
Stem elongation:
Gibberellins cause stem elongation and leaf expansion. It is believed that certain types of
dwarfness are due to gibberellin deficiency. But it has no effect on roots.
Bolting
Gibberellin induces stem elongation in rosette plants. Cabbage is a rosette plant with
profuse leaf growth and retarded intermodal length. Just prior to flowering, internodes
elongate enormously. This is called bolting. Bolting can be induced artificially by the
application of gibberellins under normal conditions.
Seed Germination
Some seeds that are sensitive to light such as tobacco and lettuce exhibit poor germination
in the absence of sunlight. Germination begins rapidly if the seeds are exposed to the
sunlight. If the seeds are treated with gibberellic acid, the light requirement can be
overcome
Breaking of seed dormancy
Gibberellins break dormancy of buds and tubers. But in root tubers it inhibits the
development of the root tuber.
Parthenocarpy
Gibberellins cause parthenocarpic in apple and pear.
Increasing Fruit Size
Gibberellins along with auxin, control the growth and development of fruits.
Flowering and sex expression
Gibberellins control flowering in long day plants. Gibberellins promote the production
of male flowers, either in place of female flowers in monoecious plants or in genetically
female plants such as cucurbits.
 Fruit growth and parthenocarpy
Increased yield (larger size) and better shape of grapes is obtained by treating the fruit
bunches with GA. It induces parthenocarpy in apples, pears, tomatoes and cucumbers.
Delayed ripening
Gibberellins delay fruit maturity and senescence in lemons, oranges and cherries. This
helps in storing the fruits.
Flowering
Gibberellins help in the flowering of many long day plants
4. Role of Cytokinins in plants
Cytokinins are a group of hormones that promote cell division in plant roots and shoots
and the growth of buds. These hormones have been found in all complex plants as well
as mosses, fungi, and bacteria. There are about 200 different natural and synthetic
cytokinins known to botanists today. Most cytokinins are produced in the meristem of
the roots. Meristem is the name for a region of tissue within the plant that actively
promotes cell division. In other words, the meristem is any place that's still growing (like
the tip of the roots or the top of the stem). Once the cytokinins has been produced in the
roots, it travels up the xylem, or vascular tissue, to other parts of the plant where
continued growth takes place (such as young leaves, developing fruits, and seeds).
Cytokinins increase cell division by stimulating the production of proteins needed for
mitosis. Cytokinins help in cytokinesis
Functions of Cytokinins:
1. Cell Division:
Cytokinins are essential for cytokinesis though chromosome dou- bling can occur in
their absence. In the presence of auxin, cytokinins bring about division even in
permanent cells.
2. Cell Elongation:
Like auxin and gibberellins, cytokinins also cause cell elongation.
3. Morphogenesis:
Both auxin and cytokinins are essential for morphogenesis or dif- ferentiation of
tissues and organs. Buds develop when cytokinins are in excess while roots are formed
when their ratios are reversed
4. Differentiation:
Cytokinins induce formation of new leaves, chloroplasts in leaves, lateral shoot
formation and adventitious shoot formation. They also bring about lignification and
differentiation of inter-fascicular cambium
5. Senescence (Richmond-Lang Effect):
Cytokinins delay the senescence of leaves and other organs by mobilisation of
nutrients
6. Apical Dominance:
Presence of cytokinins in an area causes preferential movement of nutrients towards
it. When applied to lateral buds, they help in their growth despite the presence of apical
bud. They thus act antagonistically to auxin which promotes apical dominance.
 7. Seed Dormancy:
Like gibberellins, they overcome seed dormancy of various types, including red light
requirement of Lettuce and Tobacco seeds.
8. Resistance:
Cytokinins increase resistance to high or low temperature and disease.
9. Phloem Transport:
They help in phloem transport.
10. Accumulation of Salts:
Cytokinins induce accumulation of salts inside the cells.
11. Flowering:
Cytokinins can replace photoperiodic requirement of flowering in certain cases.
12. Sex Expression:
Like auxins and ethylene, cytokinins promote femaleness in flowers.
13. Parthenocarpy:
Crane (1965) has reported induction of parthenocarpy through cytokinins treatment
5. Role of Abscisic acid (ABA) in plants
Abscisic acid (ABA) is often referred to as a inhibitory rather than stimulatory hormone.
It is involved in the closure of stomata, bud and seed dormancy and is known to inhibit
other hormonal actions. F.T. Addicott and his associates discovered abscisic acid in the
early 1960s in the process of studying abscission in cotton. Abscisic acid owes its names
to its role in the abscission of plant leaves. Plants also have hormones that stimulate
processes that are necessary for them to live. Abscisic acid is a plant hormone involved
in many developmental plant processes, such as dormancy and environmental stress
response. Abscisic acid is produced in the roots of the plant as well as the terminal buds
at the top of the plant. It is also called as stress hormone because the production of
hormone is stimulated by drought, water logging and other adverse environmental
conditions. Abscisic acid is known as dormin as it induces dormancy in buds,
underground stems and seeds. Abscisic acid is a mildly acidic dextrorotatory cis
sesquiterpenes growth hormone.
Functions of Abscisic Acid:
1. Bud Dormancy
Abscisic acid induces dormancy of buds towards the approach of winter.
2. Seed Dormancy
It is mainly caused by abscisic acid. Dormancy allows seeds to tolerate desiccation
and extremes of temperature better. The buds as well as seeds sprout only when
abscisic acid is overcome by gibberellins. Because of its action in inducing dormancy,
abscisic acid or ABA is also named as dormin.
3. Stoppage of Cambium Activity
Formation of abscisic acid stops mitosis in vascu- lar cambium towards the approach
of winter.
4. Abscission
Abscisic acid promotes abscission of flowers and fruits.
 5. Leaf Senescence
Its excessive presence stops protein and RNA synthesis in the leaves and hence
stimulates their senescence (leaf fall is actually promoted by ethylene)
6. Transpiration
During desiccation and other stresses, abscisic acid is rapidly synthesised. The
inhibitor causes closure of stomata and hence prevents transpiration.
7. Resistance
Abscisic acid increases resistance of plants to cold and other types of stresses. It is,
therefore, also known as stress hormone.
8. Starch Hydrolysis
Abscisic acid inhibits gibberellin mediated amylase formation during germination of
cereal grains.
9. Flowering:
In small quantities, Abscisic acid is known to promote flowering in some short day
plants, e.g., Strawberry, Black Currant.
10. Parthenocarpy:
ABA has been found to induce parthenocarpic development in Rose.
11. Rooting:
Rooting of stem cuttings is promoted in some cases by abscisic acid, e.g., Bean, Ivy,
Poinsettia (= Euphorbia pulcherrima)
12. Membrane Potential:
ABA induces a positive surface potential on cell membrane.
13. Controlled Growth:
It is antagonist to gibberellins and counteracts the effect of other growth promoting
hormones (auxins and cytokinins) and therefore, keeps their activity under check. By
controlling growth, ABA plays an important role in seed development and seed
maturation. Normally it inhibits seed germination, growth of excised embryos, growth
of Duckweed and other plants.
6. Role of ethylene in plants
Ethylene (ripening hormone), unlike the rest of the plant hormone compounds is a
gaseous hormone. Ethylene is produced in all higher plants and is produced from
methionine in essentially all tissues. Production of ethylene varies with the type of tissue,
the plant species, and also the stage of development. The mechanism by which ethylene
is produced from methionine is a 3 step process. Plants synthesize ethylene in response
to stress to drought stress, heat stress, biotic stress, wounding and flooding
In 1901, Dimitry Neljubov observed that dark grown pea seedlings in the laboratory
exhibited symptoms that were later termed the triple response. The first indication that
ethylene is a natural product of plant tissues was published by H. H. Cousins in 1910. In
1934, R. Gane and others identified ethylene chemically as a natural product of plant
metabolism, and because of its dramatic effects on plant it was classified as a hormone.
Ethylene can easily be synthesized in all plant organs such as roots, stems, leaves, tubers,
fruits and seeds. It is highest in senescing tissues and ripening fruits. Within the plant
organs, ethylene formation is mainly located in peripheral tissues. Ethylene is
biologically active at low concentration (less than 1 ppm). Ethylene can easily pass
through plasma membrane into the cell, easily diffuse within the plant, and flushed out
of plant tissues through intercellular spaces
Ethylene is regarded as a multifunctional phytohormone that regulates both growth, and
senescence. It promotes or inhibits growth and senescence processes depending on its
concentration, timing of application, and the plant species. Often considered an 'aging'
hormone due to its role in accelerating such developmental processes as ripening,
senescence, and abscission, Ethylene will cause a wide range of effects in plants,
depending on the age of the plant and how sensitive the plant is to ethylene.
Functions of Ethylene:
1) Growth:
Ethylene inhibits longitudinal growth but stimulates transverse or horizontal growth
and swelling of axis
2) Senescence:
It hastens the senescence of leaves and flowers
3) Abscission:
Abscission of various parts (leaves, flowers, fruits) is stimulated by ethylene which
induces the formation of hydrolases.
4) Apical Dominance:
Ethylene promotes apical dominance and prolongs dormancy of lateral buds
5) Breaking of Dormancy:
It breaks the dormancy of buds, seeds and storage organs.
6) Root Initiation:
In low concentration ethylene helps in root initiation, growth of lateral roots and root
hairs. This increases the absorption surface of the plant roots.
7) Fruit Ripening:
It aids in ripening of climacteric fruits and dehiscence of dry fruits. Climacteric fruits
are fleshy fruits which show a sudden sharp rise of respiration rate at the time of
ripening (respiratory climacteric). They are usually transported in green or unripe
stage. Ethylene is used to induce artificial ripening of these fruits, e.g., Apple,
Mango, Banana, etc.
 8) Flowering:
It stimulates flowering in Pineapple and related plants as well as mango though in
other cases the gaseous hormone causes fading of flowers. This helps in
synchronizing fruit set.
9) Sex Expression:
Like auxins and cytokinins, ethylene has a feminizing effect on sex expression. The
genetically male plants of Cannabis can be induced to produce female flowers in the
presence of ethylene. The number of female flowers and hence fruit is enhanced in
monoecious plants like Cucumber.
10) Epinasty (bending of stems)
Definitions
1. Plant Hormones: Plant hormones (also known as phytohormones) are chemicals that
regulate plant growth. (or) Any of various hormones produced by plants that control or
regulate germination, growth, metabolism, or other physiological activities
2. Auxin: A plant hormone which causes the elongation of cells in shoots and is involved
in regulating plant growth.
3. Gibberellins: Any of a group of plant hormones that stimulate stem elongation,
germination, and flowering.
4. Cytokinins: any of a class of plant hormones, produced by the roots and traveling
upward through the xylem, that promote tissue growth and budding and, on application,
retard plant senescence. Abscisic acid: Abscisic acid is a plant hormone involved in
many developmental plant processes, such as dormancy and environmental stress
response.
5. Ethylene: Ethylene is a regulator of seed germination, seedling growth, leaf and petal
abscission, organ senescence, stress responses, and pathogen responses.
6. Growth retardants: Natural growth inhibitors are regulating substances which retard
such processes as root and stem elongation, seed germination, and bud opening.
 SECONDARY METABOLITES
Metabolites

Organic compounds produced by the plants which have no direct role in the growth and
development are called as secondary metabolites.
These secondary compounds produced by plants are grouped into five major groups.
1. Phenolics
2. Terpenoids
3. Alkaloids
4. Special nitrogen metabolites
5. Cuticular compounds
Phenolics

Phenolics are a group of compounds characterized by at least one aromatic ring bearing one or
more hydroxyl groups. Phenolic compounds from plants are one of largest group of secondary
plants constituents synthesized by fruits, vegetables, teas, cocoa and other plants that possess
certain health benefits. They are characterized by the antioxidant, anti-inflammatory, anti-
carcinogenic and other biological properties, and may protect from oxidative stress and some
diseases.. Phenolics range from simple, low molecular-weight, single aromatic-ringed
compounds to large and complex tannins and derived polyphenols. They can be classified based
on the number and arrangement of their carbon atoms and are commonly found conjugated to
sugars and organic acids. Phenolics can be classified into two groups: the flavonoids and the
non-flavonoids. Flavonoids are polyphenolic compounds comprising fifteen carbons, with two
aromatic rings connected by a three-carbon bridge. They are the most numerous of the
phenolics and are found throughout the plant kingdom. They are present in high concentrations
in the epidermis of leaves and the skin of fruits and have important and varied roles as
secondary metabolites. Plants produce a large variety of secondary compounds containing a
phenol group. Most of the thousands of phenolics known to date are of plant origin. These
phenolic compounds are synthesized via two different routes: the shikimate pathway and the
acetate-malonate pathway, and thus represent a heterogeneous group. The shikimate pathway
participates in the synthesis of most plant phenolics, whereas the malonate pathway is of less
significance in higher plants, although it is an important source of phenolic products in fungi
and bacteria.
The shikimate pathway is defined as seven metabolic steps beginning with the condensation of
phosphoenolpyruvate (PEP) and Erythrose 4-phosphate (Ery4P) and ending with the synthesis
of chorismate. It is the common route leading to the production of three aromatic amino acids:
phenylalanine (Phe), tyrosine (Tyr) and tryptophan (Trp).Shikimic acid is a tri-hydroxy
cyclohexene carboxylic acid important in biosynthesis of so many compounds that
the shikimate pathway is named after it. Shikimic acid, more commonly known as its anionic
form shikimate, is an important biochemical intermediate in plants and microorganisms
The key starting materials are phosphoenolpyruvate (PEP) and Erythrose 4P derived from
glycolysis and pentose phosphate pathways, respectively. These two compounds condense to
produce a six carbon cyclic compound with one carbon (COOH) side chain namely shikimate.
Then shikimate is phosphorylated and condensed with another molecule of PEP to produce a
cyclic compound containing a three carbon and one carbon side chains. This is finally
converted to aromatic amino acids phenylalanine and tyrosine. These amino acids are
deaminated followed by hydroxylation at different carbon atoms in the aromatic ring to form
cinnamic acid derivatives. These cinnamic acid derivatives are utilised for the synthesis of
different phenolic compounds.
Functions of phenolics
Phenolics are of great importance as cell wall components. Cell wall structures such as lignins,
cutins and suberins, which provide mechanical support and function as barriers against
microbial attack. The flavonoids and anthocyanins contribute to flower and fruit colours.
Attracting insects and animals to the plant for pollination and seed dispersal Phenolics also
play a defensive role in plants by protecting against predators. Tannins and phenolic resins at
the plant surface are effective feeding deterrents. Phenolic compounds also produce
allelopathic effect. Phenolics also function as signal molecules in the interaction between
nitrogen fixing bacteria and leguminous plants. Phenolic compounds function as effective
antioxidants. Polyphenolics are important in foodstuffs, wines and herbal teas because of their
astringent taste . Polyphenolics were used as tanning agents in leather industries. Anthocyanins
have considerable potential in the food industry as safe and effective food additives
What Are Alkaloids?
These are commonly applied to basic nitrogenous compounds of plant origin that are
physiologically active
Characteristics
They are bitter in taste. Derived from amino acids. The amino acids that are most often serve
as alkaloidal precursors are: phenylalanine, tyrosine, tryptophan, histidine, anthranilic acid,
lysine and ornithine. Alkaloids form double salts with compounds of mercury, gold, platinum
and other heavy metals. These salts are obtained as precipitate which are microcrystals.
Insoluble or sparingly soluble in water, but the salts formed on reaction with acids are usually
freely soluble. Most are crystalline solids although a few are amorphous. Alkaloids constitute
a very large group of secondary metabolites, with more than 12,000 substances isolated. A
huge variety of structural formulas, coming from different biosynthetic pathways. Alkaloids
are produced by a large variety of organisms, such as bacteria, fungi, animals but mostly by
plants as secondary metabolites. Most of them are toxic to other organisms and can be extracted
by acid-base. The term alkaloid was coined in 1819 by the pharmacist W. Meisner and meant
simply, alkali like.
Sources and Occurrence of Alkaloids
Alkaloids can occur in plant kingdoms; among the angiosperms,
• Leguminosae, • Papaveraceae, • Ranunculaceae, • Rubiaceae, • Solanaceae,
• Berberidaceae are outstanding alkaloid-yielding plants
Types of Alkaloids
True Alkoloids
True alkoloids derived from amino acids. Heterocyclic ring with nitrogen. Highly reactive
substances in low doses also. Bitter taste with white appearance. Form water soluble salts
examples: cocaine, morphine, nicotine, dopamine etc
Proto-Alkaloid
General Characteristics Features:
• Have no nitrogen as part of heterocyclic ring
• Derived from amino acids like Phenylalanine, Tyrosine
• Physiologically active compounds
• Examples: Adrenaline, Ephedrine, Colchicines, Mescaline
Pseudo Alkaloids
Alkaloid-like compounds that do not originate from amino acids. This group includes terpene-
like and steroid-like alkaloids, as well as purine-like alkaloids such as caffeine, theobromine,
theacrine and theophylline. These do not show many of the typical characters of alkaloids but
give the standard qualitative tests for alkaloid.
Functions
 They may act as protective against insects and herbivores due to their bitterness and
toxicity.
 They are, in certain cases, the final products of detoxification (waste products).
 Source of nitrogen in case of nitrogen deficiency
 They, sometimes, act as growth regulators in certain metabolic systems.
 They may be utilized as a source of energy in case of deficiency in carbon dioxide
assimilation
 Muscle relaxant, Pain killers, tranquilizers, Mind altering drugs, Chemotherapy
TERPENOIDS
Terpenoids are hydrocarbons of plant origin of the general formula (C5H8)n as well as their
oxygenated, hydrogenated and dehydrogenated derivatives.
Terpenes - class of >20,000 compounds containing carbon atoms in multiples of five
Terpenoids - oxygen-containing terpenes (alcohols, ketones, aldehydes)
The name "terpene" is derived from the word "turpentine"
Terpenes and terpenoids are the primary constituents of the essential oils of many types of
plants and flowers.
The chemist Leopold Ruziicka ( born 1887) showed that many compounds found in nature
were formed from multiples of five carbons arranged in the same pattern as an isoprene
molecule (obtained by pyrolysis of natural rubber).

He called these compounds “terpenes”.

ISOPRENE C5 is the basic unit of the terpenoids
Production in Plants: * Flowers * Leaves * Fruit

Physical properties Chemical properties

Biological Role (volatile and non-volatile)

 Flavour, fragrance, scent
 Antibiotics
 Hormones
 Membrane lipids
 Insect attractants
 Insect antifeedants

Isolation of terpenoids
 Menthol, camphor, eugenol
Pheromones, Lemon grass, citral

Vitamin A

Carotenoids
Rubber

Functions
a. Plants employ Terpenoid metabolites for a variety of basic functions in growth and
development, majority of terpenoids for more specialized chemical interactions and
protection in the abiotic and biotic environment.
b. Traditionally, plant-based terpenoids have been used by humans in the food,
pharmaceutical, and chemical industries, and more recently have been exploited in the
development of biofuel products.
c. Plants have direct and indirect defence responses when they are attacked by herbivores or
infected by fungal and bacterial pathogens. Direct defences include physical structures,
such as trichomes and thorns, and the accumulation of chemical or biochemical
compounds that have antibiotic activities or toxicities
d. Phytoalexins are low-molecular-weight compounds that are produced as part of the plant
defence system. In many plant species diterpenes and sesquiterpenes act as phytoalexins.

Fill up the blanks

1. Molecules found in all plant cells and are necessary for the life of the plant is ____
2. Created through the mevalonic acid pathway; they are composed of isoprene units is ____
3. Created through the shikimic acid pathway; it contains a hydroxyl group attached to an
aromatic ring ___
4. They are modifications of amino acids; they are nitrogenous compounds that are bases is
___
5. Monoterpenoids consists of ________ carbon
6. Number of isoprene units in carotenoids is _______
7. Chlorophyll is an example of ______________
8. The best example of Monoterpenoids is_______
9. Terpenoids made out of _________
10. The molecular formula for isoprene is ______
11. Essential oils are types of __________
12. Members of secondary metabolites include ____, _____ and ¬¬¬¬¬¬¬¬¬¬
13. Terpenes are derived biosynthetically from units of ________, which has the molecular
formula
14. Organic compounds produced by the plants which have no direct role in the growth and
Development are called as __________
15 Compounds characterized by at least one aromatic ring bearing one or more hydroxyl
Groups is known as _____
16 Phenolic compounds are biosynthesised through ____ pathway
17 The ______ and ______ contribute to flower and fruit colours
18 Phenolic compoundso produce _____ effect on succeeding crop
19 Element from the periodic table is found in all Alkaloids is ______
20 ______ number of alkaloids known to exists
21 Compounds that contain a fully unsaturated six carbon ring linked to an oxygen are called
____.
22 Alkaloids are naturally occurring compounds which contain .............in their molecules.
23 Derivatives of five carbon isoprene units is _____
24 The secondary metabolites are the end product of _________
25 The role of secondary metabolites is mainly ___
26 Group of compounds characterized by at least one aromatic ring bearing one or more
hydroxyl groups is _________
27 Phenolics can be classified into two groups: the ____ and the _____
28 Flavonoids are present in _______ and _______ of plants
29 _____ coined the term terpenes
30 All terpenoids are classified based on number of _________
31 _______ are formed by monoterpenes (C10), with two isoprene units
32 The amino acids that are most often serve as alkaloidal precursors are ________,
_________, ______, ____________, ________ and ________
33 All names of alkaloids should end in ____
34 The key starting materials are ______ for Shikimate pathway
35 True alkaloids derived from ____
36 Phenolics are uncommon in ______
37 In plants, phenols are present largely in ______
38 The member of the non-flavonoids is _______
39 _____ consist of 10-C atoms or two isoprene residues
40 Both mono and sesquiterpenoids have common source is _______
41 ____ are low-molecular-weight compounds that are produced as part of the plant defence
system

ANSWER
Sl.No Answer Sl.No Answer
1 Primary metabolite 22 N atoms
2 Terpenoids 23 Terpenoids
3 Phenolics 24 Primary metabolism
4 Alkaloids 25 Defence
5 Ten 26 Phenolics
6 8 27 Flavonoids, non-flavonoids
7 Diterpenoid 28 Fruits and flower
8 Menthol 29 Leopold Ruziicka
9 isoprene 30 Five carbon
10 C5H8 31 Menthol/ linalool/ geraniol /
caryophyllene
11 Terpenes 32 Phenylalanine / tyrosine /
tryptophan / histidine /
anthranilic acid / lysine and
ornithine
12 Phenolics, alkaloid, terpenoids 33 “-ine”
13 C5H8 34 phosphoenolpyruvate (PEP)
and Erythrose 4P
14 Secondary metabolites 35 Amino acids
15 Phenolics 36 bacteria, fungi, and algae
16 Shikimate 37 Vascular plants
17 Flavonoids and anthocyanin 38 Gallic acid
18 Allelopathic 39 Monoterpenes
19 N 40 Essential oils
20 10000 41 Phytoalexins
21 Phenolics

Short notes
1) Secondary metabolites
A substance essential to the metabolism of a particular organism or to a particular
metabolic process is called metabolites. A plant cell produces two types of metabolites:
primary metabolites involved directly in growth and metabolism (carbohydrates, lipids and
proteins), and secondary metabolites considered as end products of primary metabolism
 and not involved in metabolic activity (alkaloids, phenolics, sterols ,steroids, essential oils,
lignin’s and tannins etc).They acts as defence chemicals. Their absence does not cause bad
effects in the plants. Organic compounds produced by the plants which have no direct role
in the growth and development are called as secondary metabolites. There are about
100,000 secondary compounds that are produced by the plants and the structures of more
than 15000 alkaloids, 30000 terpenes, several thousand phenyl propanoids, 1000
flavoniods, 500 quinones, 700 polyacetylenes and 800 non-protein amino acids have
already been characterised. Secondary metabolites are frequently produced at highest
levels during a transition from active growth to stationary phase. Secondary metabolites
are biosynthetically derived from primary metabolites. They are more limited in
distribution being found usually in specific families. Chemical warfare to protect plants
from the attacks by predators, pathogens, or competitors. Attract pollinators or seed
dispersal agents. Important for abiotic stresses, Medicine and Industrial additives. The four
major classes of secondary metabolites are alkaloids, glycosides, phenolics, Terpenoid
2) Phenolics
Phenolics are a group of compounds characterized by at least one aromatic ring bearing
one or more hydroxyl groups. Phenolic compounds from plants are one of largest group of
secondary plants constituents synthesized by fruits, vegetables, teas, cocoa and other plants
that possess certain health benefits. They are characterized by the antioxidant, anti-
inflammatory, anti-carcinogenic and other biological properties, and may protect from
oxidative stress and some diseases. Phenolics range from simple, low molecular-weight,
single aromatic-ringed compounds to large and complex tannins and derived polyphenols.
They can be classified based on the number and arrangement of their carbon atoms and are
commonly found conjugated to sugars and organic acids. Phenolics can be classified into
two groups: the flavonoids and the non-flavonoids. These phenolic compounds are
biosynthesised through shikimate pathway. Flavonoids are polyphenolic compounds
comprising fifteen carbons, with two aromatic rings connected by a three-carbon bridge.
They are the most numerous of the phenolics and are found throughout the plant kingdom.
They are present in high concentrations in the epidermis of leaves and the skin of fruits
and have important and varied roles as secondary metabolites
3. Terpenoids
The chemist Leopold Ruziicka showed that many compounds found in nature were formed
from multiples of five carbons arranged in the same pattern as an isoprene molecule
(obtained by pyrolysis of natural rubber). He called these compounds
“terpenes”.Terpenoids are the largest and most diverse family of natural products, ranging
in structure from linear to polycyclic molecules and in size from the five-carbon
hemiterpenes to natural rubber, comprising thousands of isoprene units. All terpenoids are
synthesized through the condensation of isoprene units (C5) and are classified by the
number of five-carbon units present in the core structure. They are polymeric isoprene
derivatives and synthesized from acetate via the mevalonic acid pathway. During their
formation, the isoprene units are linked in head and tail fashion. The number of units
incorporated into a particular terpene serves as a basis for their classification. Many flavour
 and aromatic molecules, such as menthol, linalool, geraniol and caryophyllene are formed
by monoterpenes (C10), with two isoprene units, and sesquiterpenes (C15), with three
isoprene units. Other bioactive compounds, such as diterpenes (C20), triterpenes (C30)
and tetraterpenes (C40) show very special properties
4. Classification of Terpenes
1 Hemiterpenes consist of a single isoprene unit.
2. Monoterpenes consist of two isoprene units and have the molecular formula
C10H16. Examples of monoterpenes are: geraniol, limonene and terpineol.
3. Sesquiterpenes consist of three isoprene units and have the molecular formula
C15H24. Examples of sesquiterpenes are: humulene, farnesenes, farnesol.
4. Diterpenes are composed of four isoprene units and have the molecular formula
C20H32. They derive from geranylgeranyl pyrophosphate. Examples of diterpenes
are cafestol, kahweol, cembrene and taxadiene (precursor of taxol)
5. Triterpenes consist of six isoprene units and have the molecular formula C30H48.
6. Tetraterpenes contain eight isoprene units and have the molecular formula
C40H64 Biologically important tetraterpenes include the acyclic lycopene, the
Monocyclic gamma-carotene, and the bicyclic alpha- and beta-carotenes.
5. Alkaloids
Alkaloids are defined as basic compounds synthesized by living organisms containing
one or more heterocyclic nitrogen atoms, derived from amino acids (with some
exceptions) and pharmacologically active. The class name is directly related to the fact
that nearly all alkaloids are basic (alkaline) compounds. Alkaloids constitute a very large
group of secondary metabolites, with more than 12,000 substances isolated. A huge
variety of structural formulas, coming from different biosynthetic pathways. Alkaloids
are produced by a large variety of organisms, such as bacteria, fungi, animals but mostly
by plants as secondary metabolites. Most of them are toxic to other organisms and can
be extracted by acid-base. There are many different ways of classifying alkaloids; here
we use a system based mainly on either the type of ring structure or the botanical taxa in
which the alkaloids are found. By this method, there are some sixteen major groups of
alkaloids. They are bitter in taste. Derived from amino acids. The amino acids that are
most often serve as alkaloidal precursors are: phenylalanine, tyrosine, tryptophan,
histidine, anthranilic acid, lysine and ornithine. Alkaloids can occur in plant kingdoms;
among the angiosperms, Leguminosae, Papaveraceae, Ranunculaceae, Rubiaceae,
Solanaceae, Berberidaceae are outstanding alkaloid-yielding plants. All names of
alkaloids should end in “-ine” A prefix or suffix is added to the name of a principal
alkaloid from the same source. (Quinine, quinidine, hydroquinine)
6 Shikimate pathway
Shikimate pathway is an important pathway in plants through which many secondary
plant products are synthesised. The key starting materials are phosphoenolpyruvate
(PEP) and Erythrose 4P derived from glycolysis and pentose phosphate pathways,
respectively. These two compounds condense to produce a six carbon cyclic compound
with one carbon (COOH) side chain namely shikimate. Then shikimate is phosphorylated
 and condensed with another molecule of PEP to produce a cyclic compound containing
a three carbon and one carbon side chains. This is finally converted to aromatic amino
acids phenylalanine and tyrosine. These amino acids are deaminated followed by
hydroxylation at different carbon atoms in the aromatic ring to form cinnamic acid
derivatives. These cinnamic acid derivatives are utilised for the synthesis of different
phenolic compounds.
Essay types
1. Functions of phenolics
1. Phenolics are of great importance as cell wall components. They form part of cell wall
structures such as lignins, cutins and suberins, which provide mechanical support and
function as barriers against microbial attack
2. The flavonoids and anthocyanins contribute to flower and fruit colours. This is important
for attracting insects and animals to the plant for pollination and seed dispersal.
3. Phenolics also play a defensive role in plants by protecting against predators.
4. Simple phenolic acids, polyphenolics like tannins and phenolic resins at the plant surface
are effective feeding deterrents
5. Phenolics are accumulated as post-inflectional low molecular compounds called
phytoalexins as a result of microbial attack.
6. Among the phenolic phytoalexins, hydroxycoumarins and hydroxycinnamate conjugates
contribute to disease resistance mechanism in plants.
7. Phenolic compounds also produce allelopathic effect. A well-known compound from
Juglans species is juglone which is highly toxic for a wide range of plants. It occurs in
the plant as a non-toxic glucoside and is made active by deglucosylation and oxidation
after leaching from the leaves into the soil.
8. Phenolics also function as signal molecules in the interaction between nitrogen fixing
bacteria and leguminous plants
9. These plants exude flavonoids which act selectively in Rhizobia as inducers of nodulation
gene transcription.
10 Salicylic acid is strongly implicated as a signal molecule which induces active defence
responses in several plant species against many types of pathogens.
11 Recently, it has been shown that phenolic compounds function as effective antioxidants.
12 Polyphenolics are important in foodstuffs, wines and herbal teas because of their
astringent taste.
13 Plants rich in polyphenolics were used as tanning agents in leather industries.
14 Phenolic pigments (anthocyanins, flavones etc) of fruits are most widespread food
colours occurring in fruit juices, wines and jams.
15 Anthocyanins have considerable potential in the food industry as safe and effective food
additives.
2. Explain the occurrence, classification and function of alkaloids
Alkaloids are commonly applied to basic nitrogenous compounds of plant origin that are
physiologically active. The names of these molecules tend to end in the suffixes –ine or
–in. Many are derived from amino acids, but others result from modification of various
 classes of molecules including polyphenols, terpenes, or steroids. Alkaloids are produced
by a large variety of organisms, such as bacteria, fungi, animals but mostly by plants as
secondary metabolites. Most of them are toxic to other organisms and can be extracted
by acid-base. The class name is directly related to the fact that nearly all alkaloids are
basic (alkaline) compounds. Alkaloids constitute a very large group of secondary
metabolites, with more than 12,000 substances isolated. Dicots are richer in alkaloids
than Monocots. Families rich in Alkaloids: Apocynaceae, Rubiaceae, Solanaceae and
Papaveracea. Families free from Alkaloids: Rosaceae, Labiatae
There are many different ways of classifying alkaloids; here we use a system based
mainly on either the type of ring structure or the botanical taxa in which the alkaloids are
found.
a) True Alkaloids
True alkaloids derived from amino acids. Heterocyclic ring with nitrogen. Highly
reactive substances in low doses also .Bitter taste with white appearance. Form water
soluble salts Examples: cocaine, morphine, nicotine, dopamine
b) Proto-Alkaloids
Which contain nitrogen and also originate from amino acids. Examples include
mescaline, adrenaline and ephedrine
c) Pseudo alkaloids
Alkaloid-like compounds that do not originate from amino acids. This group includes
terpene-like and steroid-like alkaloids, as well as purine-like alkaloids such as
caffeine, theobromine, theacrine and theophylline.
Functions
1) They may act as protective against insects and herbivores due to their bitterness and
toxicity.
2) They are, in certain cases, the final products of detoxification (waste products).
3) Source of nitrogen in case of nitrogen deficiency
4) They, sometimes, act as growth regulators in certain metabolic systems.
5) They may be utilized as a source of energy in case of deficiency in carbon dioxide
assimilation
6) Muscle relaxant, Pain killers, tranquilizers, Mind altering drugs, Chemotherapy
2. Explain the occurrence, classification and function of phenols
Compounds that contain a fully unsaturated six carbon ring linked to an oxygen are called
phenolics These are secondary natural metabolites produced in plants biogenetically from
either the shikimate/phenylpropanoid pathway which directly provide phenylpropanoid
and which fulfil a very broad physiological role in plants. Plant phenolics are a chemically
heterogeneous group of nearly 10,000 individual compounds: Some are soluble only in
organic solvents, some are water-soluble carboxylic acids and glycosides, and others are
large, insoluble polymers. Plant phenolics are synthesized by several different routes and
thus constitute a heterogeneous group from a metabolic point of view. Two basic pathways
are involved: the shikimic acid pathway and the malonic acid pathway. The shikimic acid
pathway participates in the biosynthesis of most plant phenolics. The malonic acid
pathway, although an important source of phenolic secondary products in fungi and
bacteria, is of less significance in higher plants.
Phenolic compounds are the most widely distributed secondary metabolites, ubiquitously
present in the plant kingdom, even if the type of compound present varies according to the
phylum under consideration. Phenolics are uncommon in bacteria, fungi, and algae.
Bryophytes are regular producers of polyphenols including flavonoids, but it is in the
vascular plants that the full range of polyphenols is found. It is estimated that about 2% of
all carbon photosynthesized by plants is converted into flavonoids or closely related
compounds
Phenolics can be mainly classified into 2 groups: a) The flavonoids b) the non-flavonoids
The Flavonoids
Largest group of phenols: 4500, -Flavonoids are polyphenolic compounds comprising
fifteen carbons, with two aromatic rings connected by a three-carbon bridge. They are the
most numerous of the phenolics and are found throughout the plant kingdom. They are
present in high concentrations in the epidermis of leaves and the skin of fruits and have
important and varied roles as secondary metabolites
Major role in plants: color, pathogens, light stress
Very often in epidermis of leaves and fruit skin and Potential health promoting compounds
– antioxidants
They can be divided into anthocyanins, flavones and flavonols.
The non-flavonoids
The main non-flavonoids of dietary significance are the C6–C1 phenolic acids, most
notably gallic acid, which is the precursor of hydrolysable tannins, the C6–C3
hydroxycinammates and their conjugated derivatives, and the polyphenolic C6–C2–C6
stilbenes
Functions
The highly ordered interactions between plants and their biotic and abiotic environments
have been a major driving force behind the emergence of specific natural products. In this
connection, the accumulation of phenolics in plant tissues is considered a common
adaptive response of plants to adverse environmental conditions, therefore increasing
evolutionary fitness.
a) Plant phenolics are considered to have a key role as defence compounds when
environmental stresses, such as high light, low temperatures, pathogen infection,
herbivores, and nutrient deficiency, can lead to increased production of free radicals
and other oxidative species in plants. A growing body of evidence suggests that plants
respond to these biotic and abiotic stress factors by increasing their capacity to
scavenge reactive oxygen species.
b) Plant growth depends on the supply of recycled nutrients; external nutrient inputs.
Polyphenols, phenolic compounds can directly affect the composition and activity of
decomposer communities, thus influencing the rates of decomposition and nutrient
cycling.
 c) Different types of soluble polyphenols, such as ferulic acid, gallic acid, or flavonoids,
have been found to either stimulate or inhibit spore germination and hyphal growth of
saprotrophic fungi.
d) Plant mycorrhizal infection, nutrient uptake, and plant growth can be impaired by
specific phenolics released by competitors in a process referred to as allopathy.
Flavonoids present in the root exudates of a variety of leguminous plants activate the
rhizobium genes responsible for the nodulation process and might be responsible for
vesicular–arbuscular mycorrhiza colonization.
e) Nodule formation is initiated by the host plant roots exuding phenolic flavonoid
compounds into the rhizosphere.
f) Anthocyanins represent a class of flavonoids providing the red and blue/purple colors
familiar in many flowers and fruits. These compounds are synthesized as visual cues,
to attract pollinators and other animals for seed dispersal, as well as molecular cues
protecting plants from various stress conditions, and are stored in the acidic vacuole
of specialized cells.
g) Plants produce a broad range of phenolic metabolites that serve a dual function of both
repelling and attracting different organisms in the plant’s surroundings. The role of
plant phenolics in chemo ecology, especially on the feeding behaviour of herbivores,
has been recognized
3. Explain the occurrence, classification and function of terpenoids
Terpenoids, also known as isoprenoids, are the most numerous and structurally diverse
natural products found in many plants Terpenoids are the largest and most diverse family
of natural products, ranging in structure from linear to polycyclic molecules and in size
from the five-carbon hemiterpenes to natural rubber, comprising thousands of isoprene
units. Terpenes are hydrocarbons resulting from the condensation of several 5-carbon
isoprene units. Plant terpenoids are used extensively for their aromatic qualities and play
a role in traditional herbal remedies. Terpenoids contribute to the scent of eucalyptus, the
flavors of cinnamon, cloves, and ginger, the yellow color in sunflowers, and the red color
in tomatoes. Well-known terpenoids include citral, menthol, camphor, salvinorin A in the
plant Salvia divinorum, the cannabinoids found in cannabis, ginkgolide and bilobalide
found in Ginkgo biloba, and the curcuminoids found in turmeric and mustard seed.
Classification
Most natural Terpenoid hydrocarbon have the general formula (C5H8)n. Terpenes are
classified into many categories based on the no. of carbon atoms and iso- prene residues
present in their structure
i) Monoterpenes. They consist of 10-C atoms or two isoprene residues.
ii) Sesquiterpenes. These contain 15-C atoms or three isoprene residues.
iii) Diterpenes. These contain 20-C atoms or four isoprene residues.
iv) Triterpenes. These consist of 30-C atoms or six isoprene units.
v) Tetraterpenes. These consist of 40-C atoms or eight isoprene residues.
vi) Polyterpenes. These consist of large number of isoprene residues.
Both mono and sesquiterpenoids have common source i.e essential oils
General properties of Terpenoids
1. Most of the terpenoids are colourless, fragrant liquids which are lighter than water and
volatile with steam. A few of them are solids e.g. camphor. All are soluble in organic
solvent and usually insoluble in water. Most of them are optically active.
2. They are open chain or cyclic unsaturated compounds having one or more double bonds.
Consequently they undergo addition reaction with hydrogen, halogen, acids, etc. A
number of addition products have antiseptic properties.
3. They undergo polymerization and dehydrogenation
4. They are easily oxidized nearly by all the oxidizing agents. On thermal decomposition,
most of the terpenoids yields isoprene as one of the product
Functions
a) Plants employ Terpenoid metabolites for a variety of basic functions in growth and
development majority of terpenoids for more specialized chemical interactions and
protection in the abiotic and biotic environment.
b) Traditionally, plant-based terpenoids have been used by humans in the food,
pharmaceutical, and chemical industries, and more recently have been exploited in the
development of biofuel products.
c) Plants have direct and indirect defence responses when they are attacked by herbivores
or infected by fungal and bacterial pathogens. Direct defences include physical
structures, such as trichomes and thorns, and the accumulation of chemical or
biochemical compounds that have antibiotic activities or toxicities
d) Phytoalexins are low-molecular-weight compounds that are produced as part of the plant
defence system. In many plant species diterpenes and sesquiterpenes act as phytoalexins.
Definition
1. Secondary metabolites: Organic compounds produced by the plants which have no
direct role in the growth and development are called as secondary metabolites
2. Phenolics: Phenolics are a group of compounds characterized by at least one aromatic
ring bearing one or more hydroxyl groups
3. Alkaloids: Alkaloids are basic N containing heterocyclic compounds derived from
higher plants often having marked physiological activity.
4. Terpenoid : Any of a large class of organic compounds including terpenes, diterpenes,
and sesquiterpenes. They have unsaturated molecules composed of linked isoprene
units, generally having the formula (C5H8)