CHAPTER 1

INTRODUCTION

It is obvious that animals provide numerous products and services. They serve as source of
quality food, as source of power, as source of savings and investments, different social and
cultural functions, to earn foreign currency, Manure, etc.

Animals however are dependent on plants for the continuation of their function because
plants by virtue of possessing chemical compounds called chlorophyll are in a position to
convert the less complex inorganic forms of nutrients like nitrates, mineral salts, H 20, CO2
into organic or highly complex type of chemical compounds. Inorganic compounds are
obtained from the soil or air for photosynthesis and absorbed by plants and by the help of
chlorophyll and radiant energy (energy from the sun), the inorganic substances will be
converted to organic (more complex) compounds. On the contrary animals are not able to
transfer less complex inorganic substances to more complex organic matter due to the lack of
chlorophyll. By virtue of this difference animal are dependent on plants for the perpetuation
of their body tissues.

Animals in general require both inorganic and organic form of nutrients to renew old tissue
and build new tissue. The animal system needs inorganic nutrients mainly in the form of
minerals. Animals need organic nutrients in the form of carbohydrates (largest quantity takes
by the animals, as most plant parts are made of carbohydrates), protein, Lipid (fat
specifically) and vitamins in the order of quantity consumed with the exception of proteins
and lipids as some feeds contain large amounts of lipids. Today we know that the body needs
over forty different nutrients in contrast to the three (carbohydrates, protein and fat) over a
century ago.

The primary source of organic material is totally plant tissues. Inorganic source of nutrients
mainly come form consumption of plant material, but it is possible to give animals with
actually not plant but in the form of pure nutrients (pure mineral) but the majority come
originally from plant tissue.
The subject matter of animal nutrition is the study of the phenomena where by one studies.

 The chemical structure (configuration) of the different nutrients.

 To understand how animal system actually functions, how the animals take the plant
material and how the various chemical reactions and physiological processes, which
transform food into body tissues and activities takes place. This involves the ingestion,
digestion and absorption of various nutrients, their transport to all body cells, and the
removal of unusable elements & waste products of metabolism.

 It is also concerned with the nature of the feed and feed nutrients, nature and requirement
of animals of different regions and different purposes (produce, reproduce, work), also
contain study of transformation of feed elements to animal products.

Nutritionally farm animals are divided into ruminants and non-ruminants, based on the
anatomical structure of the digestive system of farm animals.

Ruminants are animals having partitioned large stomach where as non-ruminants

(monogastrics) have simple stomach, not as complicated as ruminant stomach. In ruminants,
having large size and partitioned stomach create favourable environment for microbial
symbiotic activity such as favourable pH, temperature and anaerobic condition. To this effect
millions of micro-organisms thrive in the reticulo-rumen of ruminants, and these micro-
organisms have the ability to produce enzymes which can hydrolyse the fibrous (cellulose)
part of the feed enabling the animals to utilise such feeds.

The monogastric stomach on the other hand is simple and its internal environment not allow
the development of micro-organisms. So these animals are not in a position to utilise highly
fibrous feeds. Therefore, the nutrients in the two groups differ. In the case of ruminants one
can give them with fibrous feeds or cellulose rich diets and by virtue of the presence of
micro-organisms in their stomach, the inedible products will be converted to edible
(available) product in which case the ruminant can utilise and transfer it to highly valuable
and quality products such as meat and milk (hides, skin, hair, etc).

In the case of monogastrics, which lack the symbiotic effect of micro-organisms as a result of
their simple stomach, they require very low fibrous feeds as grains and there is a competition

2
for such feeds with humans (example, poultry, swine). But grains are given to ruminants in
intensive animals production systems like for fattening.

As well to digestion, the final product of digestion and absorption is different in different
farm animal (monogastrics and ruminants). After absorption the nutrient will go to different
tissues and changed to animal products, the transformation is taken place by metabolism, and
the metabolism of different nutrients will be considered.

In case of ruminants there are certain metabolic disorders called metabolic diseases and this
deviation will be considered.

Some definitions

Nutrient:- is any food or feed constituent be it organic or inorganic that has the same general
chemical composition and aid in the support of animal life.

Example; Proteins, amino acids, carbohydrate, starch

inorganic nutrients or minerals such as ca, p

Food is usually used to designate human beings while feed is what animals consume but
mostly they are used inter changeably. Feed also contains other components not really
support animal life.

Toxicity: - some nutrients (minerals, vitamins, etc.) when fed in excess of requirements will
result to reduced performance (growth) and/or sickness of animals. This condition is called
toxicity.

Deficiency: - we could have under supply of nutrients, that is less than the requirements of
the animals. In these cases it is possible that we could have deficiency of calcium,
phosphorous, other minerals, proteins, energy, vitamins. All these under supply of nutrients
will result in deficiency. This is also manifested by reduced performance and/or sickness also
death may happen in extreme cases.

The subject of nutrition embraces different scientific declines.

3
 To know the chemistry of products and biochemical changes taking place in the animal
body, one has to have knowledge of Biochemistry.
 Knowledge of anatomy of the animal enhances nutritional science.
 Physiological changes take place in the animal body and know-how of physiology is
important in the science of nutrition.
 Endocrinology study of hormonal activity in the animal system is good to know for
nutritional transformation, as different hormones has got enhancing effect for metabolic
pathways.
 Filed of biology as microbiology is important. If we take ruminant nutrition micro-
organisms play a great role in the nutrition of the animal. So rumen biology is of a special
importance for nutritional studies.
 The productivity of an animal is basically genetically determined. In suitable environment
genetic make up is important factor, therefore genetic is also part of nutritional science.
 There are also other different areas such as mathematics (statistics) which are important
in the equation of formulae and formulation of a ration. So the science of nutrition is not
isolated science but related to various sciences.

4
 CHAPTER 2
THE ANIMAL AND ITS FOOD

As we already said, the nutrients necessary to sustain animal life come directly or indirectly
form plants, due to the fact that plants do have chlorophyll to trap solar energy and convert to
chemical energy. The process of transformation of inorganic compounds to organic
compounds is called photosynthesis.

Animals consume plants and the stored chemical energy with in the plant is used by the
animal for the maintenance of life and synthesis of its own body tissues. These necessitates
tissues of both plants and animals basically to have similar types of chemical substances.

The main components of foods, plants and animals are:

Carbohydrates

Lipids
Proteins
Water Nuclei acids
Food organic
Dry matter
Organic acids

Inorganic - minerals
Vitamins

Both plant and animal tissues are made of water and dry matter (DM). DM of both is
composed of organic and inorganic entities although in living organisms, there is no sharp
distinction as many organic compounds contain inorganic entities. Inorganic portion refers to
mineral while organic has different chemical compounds as shown above. The basic chemical
substances found in both plants and animals is the same but there is minor difference between
the two mainly the amounts of different substances present.

5
The first difference of plant and animal tissues is the quality of the different materials; in
plants carbohydrate content is high but low in animals, incase of animals the protein is high.
Therefore, quantity of individual nutrients is different between the two. The reason is that the
wall of animal cells is protein and energy store is in the form of fat but for both are in the
form of carbohydrates in plants.

The other difference is interspecies difference. In plants the variability is very wide but in
animal tissues the variability between species is very small. Therefore animal tissue is
relatively constant as compared to plant tissues.

The amount of data accumulated in the composition of animal tissues is very limited because
of the fact that if one wants to take representative samples of the whole animal tissue, it is
expensive and difficult to undertake. But in plants it is easy to take the whole plant and
analyse for its components.

6
Composition of animal tissue on average (An adult mammal)
______________________________________
Component composition (%)
______________________________________
Water 60
Protein 16
Fat 20
Minerals 4
__________________________________

These figures are variable depending

1) Age and 2) nutritional state

Age is important factors influencing composition of the animal tissue. For example in the
case of cattle if we take the water content in different ages it is very variable and looks as
follows
_______________________________________________________
Stage (Age) composition of water (%)
--------------------------------------------------------
Embryonic stage (shortly 95
after conception)
At birth 75-80
5 months old 66-72
Adult (Mature animal) 40-65
Mature fat animal 40

The variation in composition for a given age is due primarily to the nutritional state as
reflected in the store of fat. Very fat animal may have as little as 40% water

As the age increases, there is a decrease in the content of water. Normally the content of
protein and carbohydrate is more or less content. The most variable components are water
and fat content. With advancing age water content decrease but contrary to this there is an
increase in the content of fat. This is compensation of the decrease in water with increase in

7
fat content of the animal. Other nutrients remain constant. Using this assumption certain
relationships has been established.

y= 355.88 + 0.355x - 202.91 logx

x = water
y = fat

This formula is used to estimate chemical component of body tissues.

Water is vital to the life of an organism and the water level in the body need to be maintained.
An animal will die more rapidly if deprived of water than if deprived of food. Water has
various functions in the body including:

 As a medium is which nutrients are transported about the body and in which waste
products are excreted.
 Many of the chemical reactions brought about by enzymes take place in the solution and
involve hydrolysis.
 Regulation of body temperature, as water has high specific heat and latent heat of
evaporation.

The animal obtains its mater from 3 sources

 Drinking water
 Water present in the food which varies form 6% in concentrates to 90% in some root
crops.
 Metabolic water, which is formed during metabolism by the oxidation of hydrogen
containing organic nutrients.
There is no evidence that under normal condition excess drinking water is harmful and
animals normally drink what they require.

Proteins

Proteins are the major N- containing compounds both in plant and animal tissues. Protein are
found in every living animals cells and quantity is dependent in the actively of the cell (i.e.
active & less active animal cells). Therefore most quantity of proteins are found in muscle

8
tissues which contain about 75-80% of the total weight of muscular tissue is protein. We also
found protein in skin, hair, feathers, wool and nail. Bones less active tissue contain small
quantity of proteins. In plants most of the protein is present as enzymes. The concentration of
protein is greater is young plants and falls as the plant mature.

Carbohydrates

In contrast to many plants the carbohydrate content of the animal body is very low which is
about 1% of the animal body. Carbohydrate in animal tissue is very dynamic and utilised
constantly. The forms of carbohydrates in animal tissues are blood sugars, glucose mainly,
muscle glycogen and liver glycogen. Plants store nutrients in the form of carbohydrates
largely such as starch and fructans. In the animal tissue though occurring as much less than
1% at any given moment, carbohydrates are constantly being formed and broken down in
metabolism and thus performs a multitude of vital functions.

Fat

Fat is the most important form of lipid present in both plants and animals. The fat content of
the animal body is variable and is related to age. Older animals contain a much greater
proportion of fat than young animals. Lipid content of plants is relatively low being about 4 -
5% dry matter (DM).

Minerals

The quality of minerals is almost constant in animal tissues. Calcium and phosphorous
comprises the largest amount although the concentration is different in different cells. The
two minerals comprise over 70% where as the other minerals comprise 30% of the total
minerals in the animal body.

Nucleic acids

Like proteins, nucleic acids are also nitrogen-containing compounds and they play basic role
in synthesis of proteins in all living organisms. They also carry the genetic information of the
living cell.

9
Organic acids

The organic acids which occur in plants and animals include citric, malice, fumaric, succinic
and pyruvic acids. Although these are normally present in small quantities, they nevertheless
play an important role as intermediates in the general metabolism of the cell. Other organic
acids occur as fermentation products in the rumen, or in silage, include acetic, propionic
butyric and lactic acids.

Vitamins

Vitamins are present in plants and animals in minute amounts, and many of them are
important as components of enzyme systems. An important difference between plants and
animals is that, whereas the former can synthesise all the vitamins they require for
metabolism, animals can not, or have very limited power of synthesis and are dependent upon
an external supply.

The chemical groups which make up the gross composition of the body are not evenly
distributed through out the various organs or tissue but are more or less localised according to
their function or to the activity that the nutrient roles.

 Water is an essential consistent of every part of the body, but its quantitative distribution
is not uniform or varies greatly with different parts. For instance blood plasma contains
>90% (90-92%) water, muscle contains 72-80%, bone 45%, enamel of the teeth 5%
water, the latter being the least in its content of water.
 Proteins are present in every cell and, as such are the principal constituents other than
water, of the organs and soft structures of the body such as the muscle, tendons and
connective tissues.
 The fat is also localised in specific tissues. It is mainly found in large quantities in the
adipose tissue, or fat depots which occur under the skin, around the intestines, around the
kidneys and other organs.
 The small amount of carbohydrates, e.g. Glucose and glycogen present in the body is
found principally in the liver, muscle and blood. Blood sugar (glucose) is readily

10
 available form of energy source for body cells (tissues), while glycogen (both muscle and
liver) are reserve forms and could easily be mobilised for use when required.
 This localisation is also true for minerals in which we find the largest quantity in bones
which is specially true due to strengthening function of minerals since bone is the
structural component of the animal body.

Therefore all nutrients are found in certain quantities in all tissues but there is localisation of
the different nutrients in various organs depending upon the function that nutrient makes.

11
 Estimation of gross body composition

The determination or estimation of body composition of the animal is difficult but essential in
nutritional research. Data on the gross composition of the body provide specific information
on the animal stage of development and state of nutrition not obtainable by merely weighing
the animal or its products. If we have different rations (A, B, C, D) and to see their effect we
have to be able to measure the body composition. Thus to estimate body tissues a method was
used previously called slaughter experiments (slaughter and chemical analysis technique).
The slaughter experiments are procedures, which involve the killing of the animals and the
analysis of certain specific tissues (e.g. bones for minerals) or of the body as a whole. This is
because in many feeding trials it is desirable to obtain more specific information regarding
the effect of a given ration than is furnished by the common measures of weight and size.

Example: In studies of protein requirement for growth or of the comparative value of

different protein sources, it is important to know the specific effect of the diets in terms of
protein tissue formed. This is because the increase in the body as a whole may be due to
water, fat and minerals as well as protein.

In slaughter experiments, to study the effect of a given diet on changes in body composition a
group of similar animals are selected and part of them are slaughtered and analysed at the
start of the experiment. The others are fed a weight and analysed diet for a given period and
then slaughtered and analysed at the middle of the experiment. The 3 rd group will be treated
the same at the end of the experiment. The difference in their composition from that of the
check animals killed at the start reveals the effect of the diet fed.

Disadvantage

 Slaughter experiment requires much more time and is laborious. In many instances the
difficulty with this method is presented in the selection of representative samples of
tissues and in their preparation for analysis.
 Likely to have a lot of errors. For each period of observation, a sufficient large number of
animals must be examined to minimise the rather large individual variability in
composition. So loss a lot of animals.

12
 Data on a gives animal can be obtained only once, and not get back the animal for future
use evenif you measure valuable performance on the animal.

Much recent study has therefore, been given to the estimation of the gross body composition
of the living animal, and very useful procedure has been developed accordingly. The methods
are based on 2 observations which are:

1. A highly predictable inverse relationships that exist between the concentration of water
and fat in the body, and
2. In the fat-free, water-free(dry) body, the proportions of protein and ash remains constant.
Therefore by using these observation estimation of body composition of the living
animal is made possible.

Procedure
To estimate body composition, the percent water is 1 st determined. This is determined by any
of the several methods (procedures) known as dilution technique. This involves the injection
of compounds known to go into solution in the body water and the quantitative
determination of the dilution of a marker used after equilibrium has been reached. Therefore,
a known concentration of the chemical will be injected into the animal body, then give time
to go in solution in water and distribute uniformly. After that allowed period of time, one can
know the quantity of water. If there is a lot of water the chemical will be very diluted and if
water content is smaller then the dilution rate is less. The compounds most commonly
employed are antipyrine and its analogs and isotopes deuterium and tritium.

After the water content has been measured, the contents of fat, protein, and ash can be
calculated. Obviously an inverse relationship for water and fat is developed and the following
equation is given for calculating fat content from the measured water (cattle).

Y= 355.88 + 0.355x - 202.91 logx

Where y= fat content (percent) and x= water content (percent). So by substituting water % for
x, we now get fat content. The protein and ash content is calculated from the finding that the
fat-free water-free body contains 80.3 percent protein and 19.7% ash.

Example, Animal weighing 500kg and having 60% of its weight water. This will result

13
Water weight of the animal = 60 x 500 = 300kg
100
Body fat weight = 20% = 20 x 500 = 100 kg
100
Water + fat = 400 kg
Water-free, fat-free animal body will be = 500- 400
= 100 kg

Protein = 80.3% x 100 = 80.3 kg

Ash = 19.7% x 100 = 19.7 kg

Now we know all excepts carbohydrates, but not a major concern due to two reasons.
1. Carbohydrates amount is very low almost insignificant which is about or less than 1%
2. The carbohydrate content of the animal body doesn’t fluctuate so it is neglected as it is
constant.

Composition of plants and their products

The feed of animals basically comes from plants. The animal feed (plants) constitutes
different nutrients. The feed of the animal has to accomplish two basic things;

a) It must supply nutrients which can be used to build new tissue and renew old tissue and to
form its products such as milk, egg, wool, etc. or need to provide building block for
production of products.
b) It must furnish energy for the processes involved.

Plants contain the same substances that are found in the animal body, but the relative amounts
present are very different. Plants also show much larger differences in composition amongst
species than do animals.

Water
In green plants the principal constituent is water as the case with animals. The water content
decrease as the plant matures.

14
Carbohydrates
The striking difference in composition of plants and animals is the fact that the DM of plant
consists principally of carbohydrates, while in animals the content is very less. Although the
animal body consists of a trace of carbohydrates, this nutrient is the principal constituent of
the food of most species of animals.

Carbohydrates consumed by animals serves as source of energy, as a reserve in the form of

fat mainly, and also glycogen into which it is readily transformed. They also serves as a basic
structural component for protein synthesis when the nitrogen come from other sources.
Therefore there is a possibility of changing carbohydrates to proteins.

When one sees the carbohydrate in plant tissues, basically they are found in two forms.
i) Structural carbohydrate- mainly cellulose, in terms of quantity cellulose comprise the
largest proportion of carbohydrates in plants.

ii) Reserve carbohydrate- starch is the basic reserve carbohydrates while glycogen is for
animals. This reserve carbohydrates is main reserve material in most plants but in some
plants reserve is kept in the form of fat or oils than carbohydrate like in oil being seeds such
as nuag, peanut. Starch is for cereals mostly.

Proteins
Proteins are also important components of plant material. Proteins are primarily a constituent
of active tissues. Therefore leaves are much richer in protein than stem or roots. With regard
to age, young plants contain more protein than old once. As plant matures, there is a
movement of protein from the vegetative parts to the seed to provide for the requirements of
growth during germination. Thus at maturity the seed contains a higher percentage of protein
than the rest of the plant.

Fat
Fat behave similar to proteins. They are higher in leaves, active tissues than the stem and
generally is highest in the seed where it serves as a condensed reserve of energy for latter
germination. So there is a graduate movement of fat from other parts of the plant to seeds. In
oil bearing seeds fat is the primary store of energy. Oil bearing seeds are also much higher is
protein than cereal seeds.

15
Mineral
The amount of mineral in plants is highly variable in different species and in different plant
parts. From the stand point of animal nutrition, we are particularly interested in the fact that
the percentage distribution of the mineral elements of plants differ markedly from that in
animals.

With the exception of legumes which are rich in Ca, other elements make up a rather small
part of the ash of plants. In plants potassium and silica are found in largest quantities as
opposed to animals where Ca & P is the dominant. Calcium is primarily associated with the
vegetative portion of the plant, and the leaf is richer than the stem. Without exception, seeds
are low in Ca compared with the other parts of the plant, though oil-bearing seeds are higher
than others. In contrast to Ca, P is richer in seeds than in the rest of the plant. Leaves are
richer than stems in P. The Ca and P contents of the vegetative parts of the plant is influenced
by soil fertility and other cultural factors.

16
 CHAPTER 3
THE FEED NUTRIENTS

3.1. CARBOHYDRATES

Carbohydrates make up 75% of the dry weight of most plants, up on which animal life
primarily depends. So carbohydrates form the largest part of the animals food supply.

The carbohydrates in plants are produced by means of photosynthesis, the most important
chemical reaction in nature. Radiant energy from the sun is captured by chlorophyll and
changed to chemical energy, which in turn support the formation of glucose from carbon
dioxide and water an endergonic reaction. There are many intermediary reactions but the
overall process may be represented as

6C02+ 6H20 + 673 Kcal C6H1206 +602

Glucose is the basic building structure for forming complex carbohydrates. In this way plants
store the energy of the sun in products that can be use by animals as a source of energy for
life processes. Thus all animal life is dependent upon the process of photosynthesis.

The name carbohydrates owe their name to the fact that they contains carbon combined with
H2 and 02 often in the same ration as in water and it means hydrated carbon meaning C atom
with H20 molecule. While a reasonable generalisation, this actually is imprecise definition;
although many carbohydrates have the same empirical formula (CH 20)n where n>3, the
definition is not strictly correct, and there are exceptions for this definition. This include:

a. It is possible that other chemical compounds which are not carbohydrates could have the
same ratio of the elements C,H,0.
b.
Example: Acetic acid is not CH20 but has a formula of C2H402
Lactic acid C3H603 (CH3.CHOH.COOH)

17
c. There is a possibility of the carbohydrate with out having the elements in the indicated
ratio

Example: Rhamnose C6H12O5

Deoxyribose C5H10O4

Therefore a more modern approach is to define carbohydrates as:

Polyhydroxy aldehydes, ketones, alcohols or acids, their simple derivatives, and any
compound that may be hydrolysed to these.

In nature carbohydrates are designed to foster plant existence, their use as an animal feed is
purely incidental. The more soluble forms serve in plants systems in energy transformation
and for tissue synthesis, the less soluble ones such as starch serve as a reserve energy, while
the relatively insoluble fraction cellulose, hemicellulose form plant structural entities.

Classification of carbohydrates

Carbohydrates are usually divided into 2 major groups according to their chemical nature.
1. Sugars 2. Non- sugar

1. Sugar

These are group of carbohydrates containing less than 10 monosaccharide residues. These are
groups of carbohydrates which are soluble in water and sweet to test. These things
differentiate sugars form non-sugars which contain >10 monosaccharides units, in their
structure; are insoluble in water and not show sweet taste.

The sugars include:-

A. Monosaccharides

These are the simplest sugar and are building block of carbohydrates. This could be divided
based on the number of carbon atoms present in the molecule as:

18
 Trioses (C3H6O3)- smallest monosaccharides which certain 3 carbon atoms
 Tetroses (C4H8O4)- contain 4 carbon atoms
 Pentoses (C5H10O5)- contain 5 carbon atoms
 Hexoses (C6H12O6)- contains 6 carbon atoms
 Heptoses (C7H14O7) - contains 7 carbon atoms

The trioses and tetroses occur as intermediates in the metabolism of other carbohydrates.
Monosaccharides may be linked together, with the elimination of one molecule of water at
each linkage, to produce di, tri-, or tetra-or polysaccharides containing two, three, four or
many monosaccharide units respectively.

B. Oligosaccharides

The name comes form Greek oligos means a few and is frequently used to include all sugars
other than the monosaccharides. Oligosaccharides contains carbohydrates containing 2-10
monosaccharide units. Oligosaccharides could be divided into different groups based on the
number of monosaccharide units as opposed to the number of carbon atom as in the case of
monosaccharides.

Disaccharides - oligosaccharides with 2 monosaccharide

units
Trisaccharides - oligosaccharides with 3 monosaccharide
units
Tetrasccharides - oligosaccharides with 4 monosaccharide
units

2. Non-sugars

These contain greater than 10 monosaccharide units. Sugars have less molecular weight than
non-sugars. The non-sugars are also called polysaccharides or glycans -(poly means many).
So they are polymers of monosaccharide units. We have two groups of polysaccharides based
on they type of monosaccharide units present in the chain.

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a. Homopolysaccharides (Homoglycans)

Homo means same, hence these are polysaccharides which contains only a single type of
monosaccharide units or these polysaccharides result to one type of monosaccharide on
hydrolysis.

Example, Glucans (glucosan) - homogolysaccharides made of many glucose units attached

together like Starch, glycogen, cellulose, dextrins.
Fructans (Fructosan)- made up of many fructose units like inulin, levan.
Arabinans (arabinose), xylans (xylose), galactans (galactose), mannans (mannose),
glucoseaminanna (glucoseamine).

b. Hetropolysaccharides (Hetroglycans)

Are polysaccharides which on hydrolysis yield mixture of monosaccharides. Therefore, these

polysaccharides are made of greater than one type of monosaccharides. Example.
Hemicellulose, pectic substances.

The molecular weight of polysaccharides varies from as little as about 8000 in some plant
fructans to an high as 100 million in the amylopectin component of starch. Hydrolysis of
these polymers to their constituent sugars can be effected by the action of either specific
enzymes or acids.

Non-sugars also contain complex carbohydrates which are ill-defined group of compounds
which contain carbohydrates in combination with non-carbohydrates molecules. They include
the glycolipids and glycoproteins.

Monosaccharides

Monosaccharides are the basic building block of carbohydrates and are divided based of the
number of c atom as trioses, tetroses, pentoses, hexoses and heptoses containing 3,4,5,6, and
7 carbon atom respectively.

20
In nature pentoses and hexoses play a significant role. The 1 st two trioses and tetroses are not
found in free form in nature but most of these are important in nutrition.

Trioses

Two trioses, glyceraldehyde (glycerose) and dihydroxyacetone are crucial intermediates in

the metabolism of glucose. They serve as intermediate products of metabolism. Normally
glucose is the most important carbohydrate digestion end product. The glucose will be taken
to different cells and metabolised (broken down) for energy production via two pathways.

1. Glycolytic pathways and tricarboxylic acid cycle

2. Pentose phosphate pathways

In these process the glucose will be broken down and the two trioses are important
intermediates of metabolism. But they are not found in free form in nature.

CH2OH CHO CHO

CO H-C-OH HO-C-H

CH2OH CH2OH CH2OH

Dihydroxy D-glyceraldehyde L-glyceraldehyde

Acetone (D-glycerose) (L-glycerose)

The two L and D forms of glycerose are used as a reference in establishing the proper
configuration of monosaccharides (the L and D form are mirror images).

21
Tetroses

The tertose erythrose is important product in pentose phosphate pathway (phosphogluconate

oxidative pathway)
H-C=O

H - C - OH

H - C - OH

CH2OH D-erythrose

Monosaccharides could be divided into aldoses or ketoses based on functional group it

contains. If the formula contains an aldehyde group (CHO) sugar contain this in their active
group are classified as aldoses. If it contains a ketone (CO) instead of an aldehyde group,
sugars are called ketoses.

E.g. CHO CHO CH2OH CH2OH

HCOH HOCH C=O C=O

HOCH HCOH HOCH HCOH

1
HCOH HOCH HCOH HOCH

HCOH HOCH HCOH HOCH

CH2OH CH2OH CH2OH

CH2OH
D-glucose L-glucose D-fructose L-fructose Aldose
Ketose

Aldoses or ketoses may take two forms based on the rotation of H and OH on the penultimate
carbon atom, almost last-c atom one before the last carbon atom as D and L. D when the OH

22
is on the right and L where it in one the left. The two are sterioisomeric forms, or are mirror
image isomers containing enantiomeric pair.

Pentoses
Pentoses and hexoses are most important once. Pentoses are sugars with 5 carbon atoms
having the general formula C5H10O5.

Linear structural formulas

H-C=O H-C=O H-C= O

H-C-OH CH2 H-C-OH

H-C-OH H-C-OH HO-C-H

H-C-OH H-C-OH H-C-OH

CH2OH CH2OH CH2OH

D-Ribose 2-Deoxy-D-ribose D- xylose

(RNA) (DNA) (Hemicellulose )

CH20H H-C= O CH20H

C =O H0 C-H C=0

H0-C-H H0-C- H H-C-OH

H-C-OH H0-C-H H-C-OH

CH20H CH20H CH20H

D- xylulose L- Arabinese D- Ribulose

(phosphogluconate (Gum) (Pentose
pathway) phosphate pathway)

23
D-ribose: This is not found in free form in nature. It is found in every living animal cell
also plants as constitute of ribonucleic acid (RNA). It is also component of several enzymes
and coenzymes. It occurs in a number of compounds which play a crucial role in metabolism
such as ATP, ADP, riboflavin, vitamins & coenzymes components and RNA. The sugar also
participate in phosphogluconate pathways.

2-Deoxy-D-Ribose: This is reduced form of D-ribose and is found in DNA.

D-xylose: This occurs in pentosans in the form of polymers called xylans and is
important in nutrition. It is the repeating unit of hemicellulose and could be produced when
herbage is hydrolysed with H2SO4. Small amount of D-xylose are present free in plumes,
cherries and grapes. Hydrolysis of hay, straw, oat hull, many woods and specially corncobs
will result in d-xylose.

L- Arabinose: Occurs in pentosans as arabans and this is also important constituent of

hemicellulose and can be produced by hydrolysis of herbage. Arabinose is also found in
gums such as gum Arabic & other gums. Arabinose is found in silage as a result of
hydrolysis.

D- xylulose: Not found free in nature but important as being intermediate product in
glucose degradation in pentose phosphate pathways.

D- Ribulose: Found as intermediate of pentose phosphate metabolic pathways.

Free pentoses constitute a very small part of the animal diet, but nonetheless can be used to
some degree in the phosphogluconate pathway. In the polymerised form, pentoses are found
in hemicellulose, and hence constituents a significant part of the energy supply for animals if
fermented by gastrointestinal micro-organisms. Arabans and xylana make up a significant
part of hemicellulose.

Hexoses

Hexoses are sugars containing 6 carbon atoms and are important in nutrition. The most
important hexose sugars are

24
H-C=O H-C=O H-C=O CH2OH

HCOH HOCH HCOH C=O

HOCH HOCH HOCH HOCH

HCOH HCOH HOCH HCOH

HCOH HCOH
HCOH HCOH
CH2OH CH2OH
CH2OH CH2OH
D-glucose D-mannose D-galactose D-fructose

Fructose is similar to glucose but functional group is ketone. While the difference between
glucose and mannose and galactose is in the position of OH and H at the 2 nd and 4th carbon
atom respectively. Glucose and fructose are the most important naturally occurring hexose
sugars, while mannose and galactose occurs in plants in a polymerised form as mannans and
galactans.

Glucose

Glucose occur in nature as D-form or as D-glucose. D-glucose, grape sugar or dextrose exists
in the free state as well as in combined from. The sugar occurs free in plants, fruits, honey
(40% sugar of honey) blood, lymph and in cerebrospinal fluid.

It is the basic molecule for the synthesis of starch and cellulose also for many
oligosaccharides and glucosides. In the pure state glucose in a white crystalline solid and is
soluble in water like all sugars.

D- Glucose is very important hexose sugar in nutrition as compared to others. This is due to:

25
 It is the major end product of digestion of carbohydrates in non ruminants and is the
primary form to be utilised for energy in which these nutrients circulate in the blood of
mammals.

 In ruminants although and product of digestion is other substrates, these products will be
converted to glucose somewhere (liver mainly) and glucose is available in the blood for
various purposes. It is the major source of carbohydrates transported in the blood.

 In terms of distribution in many natural products they are largely distributed.

Under physiological condition sugars exist mainly in a ring or cycle form. In the case of D-
glucose it exists in the form of pyranose ring similar to pyran is depicted in the Hawarth
perspective below as a regular hexagon.

C5 O O

C4 C1 or more simply

C3 C2

D-Glucose contains a like C atom attached to C atom 5.

CH20H

C O
H  H
 H 
C C
 OH H 
HO   OH
C C
 
H OH
 -D- glucose

26
 CH20H

C O
H  OH
 H 
C C
 OH H 
HO   H
C C
 
H OH

- D- glucose

Note that two forms of this sugar occurs  &  depending upon the configuration of the c
atom 1. A pair of stereoisomers related to each other as are  & -D-Glucose are called
anomers and carbon 1 is called anomeric carbon atom. This doubles the no of stereoisomers
in any group.
The  form is a precursor of starch and glycogen where as the  is for cellulose. So the
orientation is determinant weather the carbohydrate is digestible or indigestible by
mammalian enzymes.
D-fructose (fruit sugar or Laevulose)
This is am important ketohexase is nature and is the sweetest carbohydrate in nature. This
occurs free in green leaves, fruits and honey. It also occurs in the disaccharide sucrose and in
fructans. Green leafy crops usually contain appreciable amounts of this sugar both free and in
polymerised form. The free sugar is a white crystalline solid and has a sweeter taste than
sucrose. The exceptional sweet taste of honey its due to this sugar.
Table. Relative sweetness of some sugars.
Sugar Sweetness
_______________________
Sucrose 1.0
D-fructose 1.35
D- glucose 0.74
Xylose 0.67
Maltose 0.45
Galactose 0.32
Lactose 0.16

27
Fructose also normally exists as a ring like glucose which may be 6 membered but is more
commonly a 5- membered or furanose ring similar to furan. The anomeric atom is carbon
atom 2 in this case.
H

C O
H  CH2OH
 H 
C C
 H OH 
HO   OH
C C
 
OH H
-D- Fructose (pyranose form)

6CH2OH O OH
 
5C 2C
 H OH 
H   1CH2OH
4C 3C
 
OH H

- D- fructose
(furanose form)

Galactose (D- galactose)

This does not found free in nature except as a breakdown product during fermentation. It is
present as a component of milk sugar, lactose. Certain compounds of galactose, the
galactosides occur in the brain and nervous tissues. While we often think it as a sugar

28
synthesised by animals, it is found in greens and a wide range of gums, anthocyanin
pigments, mucilage and as a component of galactolipids found in plant leaves.

Mannose (D- mannose)

This does not exist free in nature but exist, in polymerised form as mannans (group of
polysaccharides wildly distributed in plants). Mannans are found widely distributed in yeast,
moulds and bacteria. Mannose also serves as component of glycolproteins. It is also found in
blood serum globulins and certain egg proteins.

Heptoses

D-sedoheptulose is an important example of a monosaccharide containing seven carbon

atoms.
CH2OH

C=O

HO C H

H C OH

H C OH

H C OH

CH2OH
D- sedoheptulose

This heptose sugar occurs as phosphate, as an intermediate in the pentose phosphate

metabolic pathway.

29
Properties of monsachrides

Because of the presence of an active aldehyde or ketone groups, they act as reducing
substances. This property is demonstrated by their ability to reduce certain metal ions notably
copper or silver in alkaline solution. The aldehyde or ketone group may also be reduced
chemically or enzymatically to yield the corresponding sugar alcohols.

Oligosacchrides

Disaccharides

Disaccharides are carbohydrates formed as a result of combination of two monosaccharide

units. Their general formula, C12H22O11 indicates that one molecule of water has been eliminated
as two monosaccharides combine. They are soluble in water, though to varying degrees and
yields two monosaccharides on hydrolyses

C12H22O11 + H2O 2C6H12O6

The possibility of disaccharide formation is enormous theoretically from limited

monosaccharides, but only some disaccharide is important in nutrition. The most nutritionally
important disaccharides in nutrition are sucrose, maltose, lactose, and cellobiose, which on
hydrolysis yield two molecules of hexoses.

A. Sucrose

Sucrose is a disaccharide formed by a reaction between one glucose and one fructose units.
The forms of the two sugars are -D glucose & -D fructose. The two sugars join together
through an oxygen bridge between two respective anomeric carbon atoms (1, 2). As a
consequence sucrose has no active reducing group.

30
 CH20H
O O
H H H CH20H H
H HO
HO OH H O H OH CH20H

H OH OH H
Sucrose
(1, 2  - D- glucose  - D- fructose)
Sucrose is the most ubiquitous and abundantly occurring disaccharide in plant nature where it
is the main transport form of carbon. This disaccharide is found in high concentration in
sugar cane (20 % of the total weight of sugar cane is sucrose) and sugar beet which contains
15-20 of the total weight is sucrose. It also occurs in many fruits, roots, carrots & vegetables.
Sucrose could be hydrolysed by the enzyme sucrase (invertase) or by dilute acids to
monosaccharide units.

B. Lactose

This is important disaccharide made up of one galactose reacting with one glucose units.
CH20H CH20H
O O
HO H H H OH
O
H OH H H OH H H

H OH H OH
-D- Galactose -D-Glucose
Lactose ( (1-4) leakage) has are active reducing group)

This occurs only in milk as a product of the mammary gland so it is called milk sugar.
Lactose is an appropriate sugar for young animals. Lactose is broken down with an enzyme
lactase found in abundance in the digestive system of young animals. Immediately after birth
lactase production increases and falls animal’s increases with age. Mature animals are less
able to digest lactose as compared young animals and lactase will be replaced by other type

31
of enzymes. On hydrolysis lactose produce one molecule of glucose and one molecule of
galactose.

C. Maltose or malt sugar

Maltose consists of two molecules of -D- glucose joined together in an  -1,4 linkage (cis
position C6).

CH20H CH20H
O O
H H H H H H

HO OH H O OH H OH

H OH H OH
-D- glucose -D-glucose Maltose

This is produced during the hydrogen of starch and glycogen by dilute acids or enzymes. This
sugar is produced form starch, during the germination of barley by the action of the enzyme
amylase (diastase). The barley after controlled drying & germination is called malt used in
the manufacture of beer & Scotch whisky. Maltose is water soluble but not as sweet as
sucrose and has one active reducing group.

D. Cellobiose

This does not exist naturally as a free sugar, but is the basic repeating units of cellulose. It is
composed of two -D-glucose linked through a - (1 4) bond (C6 trans configuration).

32
 CH20H H OH
O
H H O OH H H

HO OH H H H OH OH
O
H OH CH20H

-D-glucose -D-glucose
Cellobiose

The important difference between the two disaccharide is that maltose linkage can readily be
split by mammalian enzymes but the  1,4, linkage of cellobiose can not be broken down by
mammalian enzymes rather by the enzymes of microorganisms (cellulase).This is the main
difference between ruminant and non-ruminant digestion. So the  1,4 linkage can be
utilised by both while the  1,4 linkage is utilised by ruminants by virtue of having
microorganisms that can release the enzymes capable of hydrolysing the linkage in
cellobiose.

Trisaccharides

Trisaccharides are sugars containing three monosaccharide units. This contains a number of
carbohydrates but in terms of nutritional importance one is very important and that is
raffinose. Raffinose is a trisaccharide and is the most widely distributed oligosaccharide in
nature except for sucrose.

Raffinose is found associated with disaccharide sucrose in sugar cane & sugar beet. The
largest quantity is found is a product called mollasses during the commercial preparation of
sugar (20% of mollasses weight is raffinose). Cottonseed contains about 8% raffinose.
Raffinose on hydrolysis yields D-glactose, D-glucose and D-fructose. Upon hydrolysis
fructose is removed 1st leaving a disaccharide melibiose - isomer of lactose.

C18H32O16 + 2H2 O 3C6H12O6

33
Another trisaccharide is kestose that contain fructose attached to Sucrose molecule. It is
found in vegetative parts & seeds of plants.

Tetrasaccharide and pentasaccharides

Tetrasaccharide and pentasaccharides are not that much important nutritionally.

Tetrasaccharides are sugars containing four monosaccharides. One example is stachyose
( Raffinose + D-galactose), therefore yield two galactose, one molecule of glucose and one
fructose molecule up on hydrolysis. Stachyose is as ubiquitous as raffinose in higher plants.
C24H42O21 + 3H2O 4C6H12O6

One example of pentasaccharide is verbascose (Raffinose + 2 D-galactose)

Polysaccharides

As the name indicates polysaccharides are carbohydrates which contain many

monosaccharide units as constituents. A polysaccharide by definition constitutes greater than
ten monosaccharide units. But most of the polysaccharides contain much more than this, 100
monosaccharides at least in actual. So polysaccharides as compared to others contain high
molecular weight, most of them are insoluble in water.

Polysaccharides could be hydrolysed by enzymes specific to that kind of linkage, by acids

and also alkali. During hydrolysis they broke into various intermediate products and finally
into their constituent monosaccharides. Polysaccharides are two types’ homoglycans and
heteroglycans.

Homoglycans

A. Starch
Starch is a glucan and is the most important reserve carbohydrates in plants. It is most
abundant in seeds (70%), in fruits, tubers, and roots (30%).
The starch molecules in plants could be of two forms and except in rare instances starch is
mixture of two structurally different polysaccharides, amylose and amylopectin. For most
plants about 20-30 % of the total starch moiety is amylose which is soluble is hot water and

34
has a molecular weight of 10,000 to 100,000. Amylose contain a straight chain of D- glucose
units is an - 1, 4 linkage and is linear in structure. Starch granules are insoluble in cold
water.

Amylopectin is insoluble is hot water, and is a branched polymer of D-glucose with a chain
of  - 1,4 linkage of glucose primarily connected by an  - 1,6 cross linkage. This has a
molecular weight of over 1,000,000. The branch in amylopectin has specific feature in that it
contains about 19 to 26 glucose units in a branch. Upon hydrolysis starch is changed to
dextrin then to maltose and finally to glucose.

B. Glycogen

This is basically found is animal body, in liver and muscles and resembles starch is certain
property as well as in function. This is very similar to amylopectin form of starch. But the
difference between glycogen and amylopectin is by the number of glucose units found in
branches. In glycogen it is 12 glucose units we find in a branch but 19 to 26 in amylopectin.

In terms of function, glycogen is a reserve carbohydrate in animals while starch is for plants.
Therefore has a close similarity in the role they play. Due to this similarity, glycogen is
referred as animal starch. Dextrins are intermediate products of the hydrolysis of starch and
glycogen and are soluble in water and produce gum like solution.
Starch Dextrins Maltose Glucose
Glycogen

35
C. Cellulose

Cellulose is the most abundant plant constituent forming the fundamental structure of plant
cell wall. The cellulose molecule is different from starch and glycogen because of the type of
linkage formed between glucose units as it is - glucoside linkage. Cellobiose is the repeating
unit of cellulose.

Cellulose can be hydrolysed to glucose by strong acids. It may or may not be combined with
lignin, hemicellulose. There are many different forms of cellulose, depending up on the
species of the plant. Cellulose occurs is a nearly pure form is cotton. Cellulose is found in
largest quantity than other carbohydrates.

Other homoglycans include

 Arabinans or arabans - polymers of arabinose

 Xylans - polymers of xylose
 Fructans (fructosans) - polymers of fructose. It occurs as reserve material in roots, stems,
leaves & seeds of various plants. It is soluble is cold water & is relatively low in
molecular weight. Example, levan, inulin & highly branched group containing both.
 Galactans & mananas - polymers of galactose & mannose, and occurs is cell wall of
plants.
 Glucoaminans polymers of glucoseamine. It is the most abundant polysaccharide in
nature next to cellulose. It is component of the exoskeleton of insects and crustaceans.
Example, chitin.

36
Heteroglycans

The most important heteroglycan in plants is hemicellulose. Hemicellulose is dominantly

made up of two monosaccharides glucose and xylose. It also contain mannose, arabinose,
galactose and also uronic acid. Cellulose is an alkali soluble cellwall polysaccharide that are
closely associated with cellulose. The type of linkage () in hemicellulose can not be
hydrolysed by monogastrics rather by microbes of ruminants.

Hemicellulose is not as the name implies one-half of cellulose. This is much less resistant to
chemical degradation than cellulose and is defined as carbohydrate soluble in mild alkali. It
can also be hydrolysed by a relatively mild acid treatment. It is a cell wall fraction most
closely allied with lignin.

There are also other heterogycans

 Pectic substances found in cell wall, peel of citrus fruit. Sugar beet pulp and
contains monosaccharides rhamanose, xylose, galactoseand arabinose.
 Hyaluronic acids found in skin, umbilical cord contain monosaccharides
aminosugar and glucuronic acid.
 Exudate gums found in barks, leaves and wounds and contain
monosaccharides arabinose, galactose, rhamanose and glucuronic acid.
 Chondroitin found in cartilage, tendon, bones
 Acidic mucilages found in barks, leaves, seeds and roots and contain
monosaccharides arabinose, galactose, rhamanose and glucuronic acid.
 Mucopolysaccharides found in soft tissues and is important for lubrication.

Lignin

Lignin is not a carbohydrate but give structural support to plant cell walls and as such is
discussed together with carbohydrates. This happens because of the fact that:
 Lignin is found in close association with other carbohydrates.

37
 Lignin has got series nutritional implication in the feeding of animals and utilisation of
other carbohydrates.

Strictly speaking the term lignin doesn’t refer to one well defined individual compounds. Its
specific structure is not well described and its form can vary. Lignin is a polymer of three
phenylpropane derivatives (coumaryl alcohol, coniferyl alcohol and sinapyl alcohol).

CH = CHCH2OH

R R1
OH

1. Coumaryl alcohol, where R= R1 = H

2. Coniferyl alcohol where R= H, R1 = OCH3
3. Sinapyl alcohol where R=R1= OCH3

The lignin molecule is made up of many phenylpropanoid units associated is a complex

cross linkage structure. This compound is highly resistant to chemical degradation both to
acid and alkali. Encrustation of plant fibres by lignin renders the fiber inaccessible to
enzymes that would normally digest them. Therefore the chemical linkage of lignin with
cellulose and hemicellulose as the plant matures markedly reduce the digestibility of the
latter.

Lignin is not breakable by the enzymes of mammals or enzymes of anaerobic

microorganisms, so has nutritional implication. Aerobic organism and fungi can break the
linkage resulting in the rotting of forages & wood observed in nature. So can be utilised by
animals. The association between lignin and other polysaccharides is age dependent in that it
increases with age of the plant. Comparatively speaking young plants are more digestible
than older once due to this fact.

38
Lignin is partially soluble is dilute alkali which breaks the hemicellulose - lignin bond,
improving digestibility of hemicellulose but not destroying the lignin that is dilute alkali 2-4
% Ammonium hydroxide, NaOH, KOH solution will be sprayed on straw and will break the
lignin- hemicellulose bondage to improve digestibility of straws.

39
 3.2. Proteins

Proteins are chemical compounds, which are closely related but physiologically distinct
members. Proteins are found in all living cells where they are intimately connected with all
phases of actively that constitute the life of the cell. Each species has its own specific proteins
and a single organism has many different proteins in its cells and tissues.

Plant proteins differ from each other and from animal proteins. In fact no two proteins seem
to be exactly alike in their physiological behaviour. From the standpoint of nutrition the
important distinguishing feature of the various proteins is their amino acid makeup. Proteins
are basically made of building blocks called amino acids, which is one structurally unifying
factor of proteins. Proteins are mainly found in active tissues in plants and animals like
leaves, shoots, and muscle. In common with carbohydrates proteins contain carbon, hydrogen
and oxygen but in addition they also contain nitrogen. Most proteins also contain sulfur and a
few contains phosphorous and iron. In terms of composition of these different elements, they
account the following percentages:

_____________________________________________
Element Percentage
_____________________________________________
Carbon 51.0 - 55.0
Hydrogen 6.5 - 7.3
Oxygen 21.5 - 23.5
Nitrogen 15.5 - 18.0
Sulfur 0.5 - 2.0
Phosphorous 0.0 - 1.5
Iron -
_____________________________________________

40
 Amino acids

Proteins are polymers of amino acids. Amino acids are produced as hydrolytic end products,
and where proteins are heated with strong acids, alkalis or when they are acted upon by
certain enzymes.

There are a number of amino acids identified the highest figure mentioned in books is 200
amino acids. Out of these only 20 amino acids are commonly found as components of
proteins and hence nutritionally important.

Amino acid are characterised by having a basic nitrogenous group, generally an amino group
(-NH2), and an acidic carboxyl group (-COOH). Most amino acids occurring naturally in
proteins are of the  type, having the amino group attached to the carbon atom adjacent to the
carboxyl group and can be represented with the general formula.

COOH

H2NCH

R
L- amino acid

The difference in different amino acids, is in the side chain R. In nature the amino acids
usually assume the L- configuration and hence this form is important. There is a possibility of
manufacturing amino acids is the laboratory both the L and D form. When we supply both
forms to animals only the L form is utilised for protein synthesis as this is similar to the one
in nature.

The exception to the general formula of amino acids are the amino acids proline and
hydroxyproline which have an imino (NH) instead of an amino group (NH2).

41
Amino acids by virtue of having an amino and carboxyl group, they show different
characteristics in different medium solutions. They assume acidic or basic proteins depending
on the pH medium. In acidic pH shown basic characteristics (amino acid is a cation) and is
basic medium show acidic characterise (amino acid is an anion), and at a pH it is electrically
neutral amino acid is dipolar. Such characteristic is called amphoterism. Because of this
amphoteric nature amino acids act as buffers, resisting changes in pH.

To study the different amino acids that constitute the different proteins classification is
developed where by amino acids are divided into 3 groups depending on their chemical
structure or a series of organic compounds in which they belong.

I. Aliphatic amino acids - this contain straight chain amino acid.

II. Aromatic amino acids - these are amino acids
containing benzene ring somewhere in their structure. Example, phenylalanine,
tyrosine, diiodotyrosine, thyroxine.

III. Heterocyclic amino acids - are amino acids not fit

in any one above. Example, Histidine, proline, hydroxyproline, tryptophan.

Aliphatic amino acids are the amino acids which contain most of the nutritionally important
amino acids. These group can be subdivided into:

A. Neutral amino acids - are amino acids which contain equal no of the amino and
carboxylic group. Since this group contain one NH2 & one COOH, they are called
monoamino-monocarboxylic acids. This comprises the largest number of amino acids.
Example, glycine, alanine, serine, valine, leucine. isoleucine and threonine.

B. Acidic amino acids (monoamino-dicarboxylic acids)- These are amino acids that contain
more number of carboxylic than amino group and hence the acidic properly is more.
Example, Aspartic acid, glutamic acid.

C. Basic amino acids (Diamino-monocarboxylic acids) - These amino acids has more amino
than carboxylic group and hence dominant basic character. Example, Arginine. Lusine.
Citrulline.

42
D. Thio amino acids - these are sulfur containing amino acids like cysteine, cystine,
methionine.

Plants and many microorganisms are able to synthesise proteins from simple nitrogenous
compounds such as nitrates, so can synthesise all the 20 amino acids. Animals can not
synthesise the amino group. So in order to build up proteins a dietary source of amino acids is
essential. Certain amino acids could be synthesised in the animal body from others while a
number of them can not be synthesised in the animal body and these are referred to as
indispensable or essential amino acids, so must be included in the diet. The others which are
not obligatory and can be synthesised with in the body are called dispensable or non-essential
amino acids.

From works done on rats, monogastric animals require the following ten essential amino
acids.
Phenylalanine Valine Threonine
Tryptophan Isoleucine Methionine
Histidine Arginine Leucine Lycine

The chicks require in their diet the ten amino acids plus glycine as the 11 th essential amino
acid. To easily remember, one may use the abbreviation PVT TIM HALL + G (for poultry),
where each letter represents the 1st letter of the respective essential amino acid.

Dispensable amino acids include:

Cysteine Tyrosine Glutamic acid Alanine Aspartic acid

Serine Proline Cystine Citrulline Hydroxyproline
Glycine (for non poultry)

In the case of ruminants, all the indispensable amino acids can be synthesised by the rumen
microbes, which theoretically make these class of animal independent of a dietary source for
essential amino acids. The exception is for high producing animals exception where
supplementation of good protein feeds may be essential to meet the demand for their high
production of animal products. In non ruminants the dispensable amino acids could be

43
synthesised by a process called transamination that is by the utilisation of amino acid and
ketoacid, we form new amino acids.

COOH COOH COOH COOH

C=O + CH-NH2 Transaminases CH-NH2 + C=O

R1 R2 R1 R2
Ketoacid Amino acid 1 Amino acid 2 Ketoacid
From the amino acid amino group will be transferred to the ketoacid structure and keto
position goes to the amino acid structure. As a result other amino acids & a new ketoacid is
formed.

Proteins

Proteins are made up of building blocks called amino acids, which contain amino and
carboxylic groups except for some which contain imino group (NH) so called imino acids
like proline & hydroxyproline. Proteins are built from amino acids by means of a linkage
between -carboxylic of one amino acid and -amino group of another amino acid.

R H H R1 O
    
H2N- C - C- OH + H- N - C - C - OH
 
H H

R O R1 O
   
H2N- C - C - HN – C – C – OH + H20
 
H H

44
This type of linkage is called peptide linkage. One hydrogen from amino group and OH from
carboxyl group of the other amino acid will be removed as H 2O molecule to form peptide
linkage. Similarly other amino acids could be added to this basic chain to synthesise the
protein required. During formation first dipeptide is formed, then tripeptide, tetrapeptide, etc.
with the elimination of one H2O molecule at each linkage to produce polypeptides.

The structure of protein can be considered under four heading for convenience:

 Primary structure refers to the sequence of amino acids along the polypeptide chain of
proteins.
 Secondary structure of proteins refers to conformation of the chain of amino acids
resulting from the formation for hydrogen bonds between imino (NH) and carbonyl (CO)
groups of adjacent amino acids. This exist is form of - helix.
 Tertiary structure – describes how the chain of the secondary structure further interact
through R group of the amino acid residues. This causes foldings & bendings of
polypeptide chain, which gives each protein its characteristic biological activity.
 Quaternary structure - protein posses of quaternary structure if they contain more than
one polypeptide chain.

200-1000 amino acids are required to make many proteins. Compounds which involve up to
100 amino acids in the chain are called polypeptides. If it contains more than 100 amino acids
it is called proteins.

Proteins are what they are by virtue of the kind and sequence of amino acids in its
polypeptide chain. Each protein is precisely built to serve its specific function in the body and
has a structure which is determined genetically, it is not a random process. Protein found is
blood is specific to blood, finger nail to finger nail, etc. Each protein has specific
physiological, chemical & biological character determined genetically. This is due to
differences in the sequence and kind of amino acids involved. For example, in blood protein
if glycine is found at the 20th position, it is always found there, if it is changed that will result
to totally different protein. Therefore not only kind but the position of amino acids in a
protein molecule is also predetermined genetically.

45
In synthesising a specific protein, all the necessary amino acids must be found in place, in the
required quantity and right time. If there is a miss in a single amino acid or come late that
protein could not be synthesised.

Properties of proteins

Proteins is a collective term encompassing so many compounds. But there are general
properties common to most or all proteins. These include:

1. In the formation of peptide chain whatever the length is there must be one NH2 and one
COOH group at end positions. Since they have these two ends in their structure, proteins
show the property of amphoterism, perform as basic in the acidic medium and viseversa.
All proteins show this properly and hence serve as buffers.

2. Proteins are insoluble in fat solvents (organic solvents) such as ether and petroleum ether.
With respect to their solubility in water the widely differ ranging from keratin which is
insoluble (found in horns, nails, hooves of animals) to the soluble albumin (blood, egg,
milk). Other proteins fall in between the two. Proteins is solution has colloidal properties.

3. Many proteins (weather with other nutrients or alone) can be precipitated from solution
by neutral salts such as ammonium sulphate or sodium chloride. This process is called
salting out. This mechanism is not clearly understood, and is specific to proteins not to
other nutrients.

4. All proteins can be denatured. (change from their natural sate). Denaturation is change or
any non proteolytic modification of the unique structure of a native protein, giving rise to
definite changes in chemical, physical or biological properties. Products of protein
hydrolysis are not included under this definition.

Many proteins are heat coagulable. Heating can therefore denature proteins. Apart from heat
there are many other agents which can bring about the denaturation of proteins; which
include strong acid, alkali, alcohol. Acetone, urea, etc. result in denaturation. In this case
biological activity, like enzyme function is destroyed. Digestive action on some kinds of
protein is improved if the protein is cooked before eating.

46
The effect of heat on protein is of special interest in nutrition as this results in new linkages
within and between peptide chains. Some of this new linkages resist hydrolysis by proteases
produced is the digestive tract and impede the access to adjacent peptide bonds. Susceptibility
of proteins to heat damage is increased in the presence of various carbohydrates, owing to the
occurrence of maillard-type reactions which initially involve a condensation between the
carboxyl group of a reducing sugar with the free amino group of an amino acid or protein .
Lysine is particularly susceptible. With increasing severely of heat treatment further
reactions, involving protein side –chain can occur resulting in the browning of foods. The
dark colouring of overheated hays and silages is symptomatic of these types of reactions.

Denaturation has practical implication in that during the process of digestion in monogastrics
& ruminants true stomach (abomasum), HCl is produced and have effect in denaturing
protein. This have a positive effect in the digestion of proteins as denatured proteins are
comparatively more susceptible to enzyme action than the natural proteins in the stomach &
small intestines.

In the stomach of monogastrics & abomasum of ruminants along with HCl, protein digesting
enzymes pepsin is produced. But pepsin (almost all enzymes) are proteins. So the enzyme
could be denatured by the HCl present, which will make the enzyme ineffective. But there is
a certain mechanism to avoid this phenomenon in that the pepsin is not produced in the final
form but rather in an inactive form called pepsinogen. So the HCl will act on the inactive
form of enzyme and denaturing the pepsinogen. This result in the activation of enzyme
pepsinogen & formation of pepsin. Therefore, protein digesting enzymes not produced in the
final form but in inactive form to make free form denaturation.

HCl + Pepsinogen Pepsin

47
 Classification of protein

Proteins may be classified into two main groups

1. Simple protein - are proteins that yield only amino acids upon hydrolysis. This are
subdivided into two groups according to their shape solubility and chemical
composition)
A. Fibrous proteins - this include elastins, collagens and keratins
B. Globular proteins - this include albumins and globulins

2. Conjugate proteins - are proteins that yield other compounds in addition to amino acids.

Fibrous proteins

These are long chain polypeptides and are found in the animal tissue in the form of collagen,
elastin and keratin. These groups are insoluble & very resistant types of proteins to enzymes
and in most cases have structural role in animal cells & tissues.

Collagen:- are very touch proteins well distributed in muscular tissues and specially
connective tissues like tendon, ligament. This is the most abundant single protein in
mammals (30%). The quantity of this protein is dependent on age, the proportion is lower in
young animal and increases with age.

In case of fibrous proteins is addition to the peptide bond, there is also a formation of H
boding which make these proteins touch compared to the other two protein groups. These
protein collages is rich in amino acid hydroxylproline and is considered as poor quality
protein. This protein makes meat of older animals less tender (touch). It is insoluble and
indigestible, but upon heating or treating with acid, it becomes a soluble, easily digested
mixture of polypeptides called gelatin.

48
Elastin: This is found in smaller quantities compared to collagen. This protein is found in
elastic tissue such as tendons and arteries (wall of lung). This protein can stretch in two
direction and is very poorly digested. The polypeptide chain of elastin is rich is alanine and
glycine & flexible. It contain cross links involving lysine side chain which prevent the protein
from extending excessively under tension and allow it to return to its normal length when
tension is removed.

Keratins: is the toughest fibrous protein which is found in hair, nails, wool, horn, hooves,
feathers, skin, and beaks. The protein is high in cysteine and has many disulfide linkages (-S-
S-) which make hair quite malleable and permit it to stretch when moist heat is applied and
then contract when cooled and dried.

Globular Protein

Are so called because their polypeptide chains are folded into compact structures. Most of the
members of globular proteins are soluble in water. These proteins include the enzyme,
hormones and oxygen carrying proteins (blood proteins), antigens. They are soluble of also in
acids, bases or alcohol.

Albumins: are water soluble and heat coagulable. They include a significant part of serum
proteins and egg proteins. They also occurs is milk and many plants.

Globulins: are insoluble in water or sparingly soluble. These are present in eggs, milk, and
blood are main reserve proteins in seeds. Immuno globulin & hemoglobin in blood,,
lactoglobulins of milk, myoglobins in muscles.

Some proteins fall between fibrous & globular proteins like myosin of muscle and fibrinogen
of blood.

Conjugated proteins (complex or compound protein)

These groups of proteins are proteins which contain other non protein moiety or radical called
prosthetic groups. So yields non- protein grouped on hydrolysis. Conjugated protein =
Protein + prosthetic group. The prosthetic group varies and may be phosphoric acid resulting

49
to a conjugated protein called phosphoprotins, a carbohydrate or carbohydrate derivative
glycoproteins, a lipid yielding lipoproteins, a pigment chromoproteins, or a nucleic acid
called nucleoproteins.
 The phosphoproteins include large number of compounds like casein which is found in
milk, phosvitin in egg yolk.
 Glycoproteins are complex proteins with one or more heteroglycans as prosthetic group.
Glycoproteins are compounds of mucous secretions which act as lubricant in many parts
of the body. Example, ovalbumin.
 Lipoproteins are proteins conjugated with lipid, like lecithin, cholesterol). These are the
main components of cell membranes and play a basic role in lipid transport. These are
divided into 3 based on density as chilomicrons, low density lipoproteins (LDL), high
density lipoproteins (HDL).
 Chromoproteins contain pigment as the prosthetic group. Example, haemoglobin which
consists of the protein globin, combined with an iron contains compound haem or
haemalin. Other example is haemocyanin, cytochrome (prosthetic group haem) &
flavoprotein (prosthetic group flavins).
 Nucleoproteins are compounds of prosthetic groups nucleic acids, mainly found in germ
portion of plants useful for propagation.

50
 Non protein nitrogenous compounds

In plants and animals there exists a number of nitrogenous compounds which by definition
are not proteins, that is not contain amino acids joined by a peptide bond. They are all classed
as non protein nitrogen (NPN) compounds. These NPN compounds include amino acids
found freely, which make the main part of NPN in plants, amines, amides, purines,
pyrimidines, nitrates, alkaloids, many members of the vitamin B complex containing
nitrogen, urea, uric acid, biuret (2xurea) & ammoniated products.

In plant tissues NPN content is comparatively speaking higher at young stage of the plant and
actively growing portion like the shoot has got more NPN. Silage crops contain a let of NPN
due to the immaturity of the crop at harvest & to the fermentation processes during ensiling
which hydrolyses protein to amino acids. For example, fresh corn forage contains 10-20 %
NPN, while in corn silage NPN accounts for up to 50% of the total N.

Some specific NPN compounds having nutritional significance

1. Amine

Amines are basic compounds present in small amounts in most plant and animal tissues.
Many occur as decomposition products in decaying organic matter and have toxic properties.
Many microorganisms are capable of producing amines by decarboxylation of amino acids.
These may be produced in rumen under certain conditions and may give rise to symptoms. In
the reticulorumen certain microbial enzymes may removed the COOH of amino acids leaving
amino acid with amino group which is amine. So for every amino acid amine can be
produced.

One concern is with the amine histamine formed from amino acid histamine and in case of
anaphylactic shock (hypersensitivity mainly due to contraction of smooth muscle & increased
capillary permeability caused by release in the tissues & circulation of histamine) is found in
blood in relatively large amounts.

51
Betaine, is an amine which is converted to trimethylamine in the animal body giving rise to
fishy taint to milk by cows that has been excessively fed sugar beet byproducts. Betaine is
formed by the oxidation of choline.

2. Urea and uric acid

Urea is an amide, organic compounds containing CONH 2 radical. There are also other amides
also closed as amino acids like Aspargine, glutamine. The chemical composition of urea and
uric acid is not similar but both are major end products of nitrogen metabolism of animals.
Urea is main end product of nitrogen metabolism in mammals, although it also occurs in
many plants (wheat, soybean, potato, cabbage).
NH2
O= C
NH2
Urea
While uric acid is end product of nitrogen metabolism is birds thus corresponds, it its
function to urea in mammals. In man and other primates uric acid is the end product of purine
metabolism and is found in the urine. In subprimate mammals the uric acid is oxidised to
allantoin before being excreted.

O H
N O H
N N
O H2N C

O
N N N N
H H H H H
Uric acid Allantoin

In poultry uric acid is exerted in poultry excreta. In the excreta we find black (Grey)
and white portion. The white portion is almost 100% uric acid which contain large
quantities of nitrogen and ruminants can utilise this nitrogen for synthesising the

52
 necessary amino acid which goes for protein synthesis. Because of this poultry
excreta have been used to feed ruminant to meet their need of nitrogen.

3. Nitrates

Nitrates are salts or esters of nitric acid (HNO 3). Nitrates may be present in plant material
especially it is high at young stage. While nitrate itself may not be toxic to the animals, it is
reduced readily under favourable conditions, as in the rumen which contains much free
floating hydrogen to nitrite which is toxic. This produce a condition called nitrate nitrite
toxicity or prussic acid toxicity or oat hay poisoning which is attributed to relatively large
amount of nitrate present in green oats.

4. Alkaloids

These are organic substances having alkaline properties and containing nitrogen. These
compounds occur only in certain plants mainly found in accumulator plants. These are of
particular interest since many of them have poisonous properties. Example, solanine unripe
potato and potato sprouts have green patches all over potato tuber. This alkaloid if fed to pig,
they are very sensitive to this alkaloid and death may happen. There are others from other
plants.

5. Nucleic acids

Nucleic acids are high molecular weight compounds which on hydrolysis yields a mixture of
basic nitrogenous compounds (purine and pyrimidines), a pentose (ribose or deoxyribose) and
phosphoric acid. They play a fundamental role in living organisms as a store of genetic
information (DNA, RNA), energy metabolism (ATP, ADP, AMP), cell metabolism (NAD,
NADH, FAD). They are NPN compounds and can serve as source of nitrogen for ruminants
specially.

53
 Protein deficiencies and/or inadequacies

1. Protein deficiency

Since protein exists in almost everywhere in the animal body, it may be difficult to see a
specific deficiency signs. A shortage of protein obviously results to depression of metabolic
activities, food intake, decrease in production, growth is impaired, reproduction and lactation
will be reduced, and in extreme cases like in nitrogen-free diets death will result. In human
disease of protein malnutrition of young is kwashiorkor as marasmus for a calorie deficiency.

2. Amino acid deficiency

In this case the total quantity of protein could be enough but may not contain the essential
amino acids in the quantity required. Therefore, a deficiency of any one of the essential
amino acids is in effect a protein deficiency. If there is a lack of amino acid in time, there is
inability to utilise all the other amino acids for protein synthesis. These unused amino acids
will be deaminated for energy production and urea excretion increases. A unique feature of
an amino acid deficient diet is the prompt reduction in feed intake.

3. Amino acid antagonism

This is a condition where two or more amino acids being antagonist to each other. So one
amino acid will affect the requirement of the other by interfering with its metabolism.
Example, lysine - arginin antagonism, these amino acids have similar structure. In this case
dietary lysine increases the requirement for arginin. Lysine acts by competing with arginine
for reabsorption in the renal tubules increasing arginin excretion and by increasing renal
arginase activity and thus splitting arginine into urea and ornithine. High lysine also
suppresses feed intake.

In poultry a valine - leucine - isoleucine antagonism also exists. Corn for example is high in
leucine and could cause an imbalance. Although in practical feeding these things may be
infrequent, they should be considered while preparing rations for animals.

54
4. Amino acid imbalance

An amino acid imbalance results from the addition to a low-protein diet of one or more amino
acids, other than the growth limiting one, in amount that are not individually toxic and yet
cause depressions in food intake and growth that are readily prevented by a supplement of the
growth limiting amino acids. Rats prefer a protein-free diet to an imbalanced one and, when
corrected leave the protein-free diet. Feed intake is depressed via the same mechanism
describe for an amino acid deficiency but involves also the medial any amygdala of the brain.
The imbalance diet also intefers with protein synthesis in the liver.

55
 3.3. Lipids

Lipids are group of substances found in plant and animal tissues, insoluble in water but
soluble in common organic solvents such as benzene, ether, chloroform, ethanol which is the
specific character of lipids. These are basically made up of the elements carbon, hydrogen
and oxygen, but quantity of oxygen found in basic lipid structures is lower than that found in
carbohydrates. The term lipid includes a number of different chemical compounds, and they
are classified into subgroups as depicted in the table.

Lipids can be divided into two basic groups

1. Glycerol based lipids: are lipids having glycerol unit in their structure while
CH2OH

HCOH Glycerol (trihydroxy alcohol having three OH)

CH2OH

2. Non glycerol based lipids: are lipids that do not contain glycerol in their structure.

Glycerol based lipids are divided further into:

a. Simple lipids: these have one group of compounds that is fat & oils.
b. Compounds lipids: these are of two types
i. Glycolipids: are lipids that contain sugar attached to the lipid molecule. It can be
glucolipids that contain glucose attached to the lipid or galactolipids that contain
galactose attached to lipid molecule.
ii. Phospholipids: are lipids containing phosphoric acid or phosphorous attached and
are of two types, lecithins and cephalins

Lipids play different roles in the animal body. They act as electron carriers, substrate
carriers in enzymatic reaction, as components of biological membranes & stores of
energy. In plants lipid are two types structural (components of membranes and protective
surface layers such as waxes) and storage like in fruits, and seeds. In animals lipids are

56
 the major forms of energy storage mainly as fat which may constitute up to 97 % of the
adipose tissue of obese animals. Structural lipids of animal mainly phospholipids
constitute between 0.5 and 1% of the muscle and adipose tissue.

Fats

Fats and oils are constituents of both plants and animal and are important sources of stored
energy. Both have the same general structure and chemical properties but they have different
physical properties. Fats are those that are solid at ordinary room temperature (20 oC) while
oils are liquids at this temperature. The term fat is frequently used in a general term to include
both groups.
Fats are glycerol based compounds and are basically made of glycerol unit and fatty acids.
There could be one glycerol unit to which one to three fatty acids attach to the 3 position of a
glycerol unit. Fats function as source of energy, thermal insulator and as source of heat.
1 CH2OH

2 CHOH + 3 R- COOH CH2 .O.CO.R

CH. O. CO. R + 3H2O

3 CH2 OH
C2H .O. Co. R
Glycerol + Fatty acid Triacylglycerol (Triglyceride)

Therefore, fats are esters of fatty acids with the trihydric alcohol glycerol called glycerides or
acylglycerols. When all the three alcohol groups are esterified with fatty acids, the compound
is a triacylglycerol or triglyceride. Di and monoacylglyerols also occur naturally but in much
smaller amounts than the triacyl form.

Triacylglycerides differ in type according to the nature and position of the fatty acid residues.
Those with 3 residues of the same fatty acid are termed as simple triacylglycerols & when
more that one fatty acid is involved in the esterification then a mixed triacylglycerol results.

57
 Fatty acids

Fatty acids are classed into two groups, which are saturated fatty acids and unsaturated fatty
acids. The difference between the two is that the saturated group contain no double bonds in
their structure, while the unsaturated fatty acids contain as least one double bond in their
structure.
For some common fatty acids see the attached table. The common names are given while
names in parentheses represent the modern chemical nomenclature the suffix anoic refers to
the saturated fatty acids, and enoic shows that the fatty acid is unsaturated. The suffix
monoenoic refers to the presence of one double bond, dienoic, trienoic, tetraenoic four,
polyenoic refers to the presence of two, three, four and many double in the fatty acid
molecule.

These double bonds are reflected in the formulas for the fatty acids in that they have smaller
number of hydrogen atoms relative to the carbon atom present. They posess different physical
properties form the saturated once, they have lower melting points and chemically more
reactive or susceptible to oxidation. The term polyunsaturated fatty acid is frequently applied
to those having more than one double bond and they have specially significance in nutrition.

The melting point of a fatty acid increase with chain length but adding a double bond lowers
it for a given chain length, two double bonds low it even more. Thus the melting point of
C18:1 is greater than C18:2. Therefore the physical property of fatty acids depends on the
number of carbon atoms and the degree of unsaturation or number of double bonds present.
From the fatty acids listed in that table the first five are volatile fatty acids since they can be
distilled with steam.

The carbon atom of fatty acids are numbered from carboxyl group and the position of each
double bond  is shown by the number of the carbon atom at its carboxyl end that is a 7
fatty acid would have a double bond between carbons atom 7 and 8.

When we consider naturally occurring fatty acids in plant and animal tissues, they have
certain general characteristics in that they contain an even number of carbon atoms, most of
the naturally occurring fatty acids are unbranched or are straight chained; they also have one
carboxylic end or contain a single carboxyl group. Microbial lipids or lipids synthesised by

58
micro-organism however are often branched, have chains of an old number of carbon atoms
& it is possible to observe greater than one carboxyl group in the structure. These things have
significance in ruminant feeding in that all fatty acids in monogastric animals are natural fatty
acids whereas fat depots in the tissue of ruminants, it is possible to find fatty acids of
microbial origin. Hence the fats of ruminant body and milk characteristically contain these
aberrant forms.

In many nutrition books linoleic, linolenic and arachidonic acids are classed as essential fatty
acids (EFA), because the lack of these fatty acids in the diet of animal specially at young
stage (calves, lamb, kids, pigs, chicks, mice, guinea pigs) result to the development of
deficiency symptoms. The deficiency symptoms observed in rats include, scaly appearance of
the skin, necrosis of the tail, failure of growth, decline in reproduction, lactation, overall
production has been observed. So animals need to have the supply of the EFA. In case of
chicks, those kept on low fat diets have shown poor growth rates, poor feathering, oedema
and high mortality in the 1st few weeks of life.

These EFAs like other polyunsaturated acids they form part of the various membranes and
play a part in lipid transport and certain lipoprotein enzymes. In addition they are the source
materials for the synthesis of prostaglandins and thromboxanes, hormone-like substance that
regulates many cell functions including blood clothing, blood pressure and the immune
response. The need for the dietary source of the acid arises from the inability of animal to
introduce double bonds because of the absence of relevant desaturases from animal tissues.

Recent experiments recognise that the most important EFA is linoleic and if animals supplied
enough quantities of this acid the other two EFA could be synthesised from this acid. The
oilseeds are generally rich sources of linoleic acid, linseed is particularly good source of
linoleic acid. Considerable quantities of oilseeds in the diet of monogastrics (pigs & poultry)
exist, so animals will receive an adequate supply of EFA.

In ruminants considerable hydrogenation of unsaturated fatty acids takes place in the rumen
thereby reducing the available EFA. Despite this the possibility of ruminants suffering from
EFA deficiencies is remote, since they are able to conserve their dietary supply efficiency.

59
Over supply of polyunsaturated fatty acids may have a nutritional disadvantage, as these
unsaturated fatty acids increase the requirement for vitamin E, which appears to serve
primarily as an antioxidant, which will result to the shortage of vitamin E and its deficiency
condition such as muscular dystrophy & encephalomalacea. This does not occur for
hydrogenated oils. Vitamin E functions as a chain breaking antioxidant thereby neutralising
free radicals and preventing peroxidation of lipids can destroy the structural integrity of the
cells and cause metabolic derangements. The double bond which is the reactive site may react
with other elements like oxygen or be broken down, and vitamin E prevents this oxidation of
double bond which will increase requirement for the vitamin and cause its deficiency
symptoms as muscular dystrophy.

As mentioned somewhere in this chapter, fats are defined as esters formed by the union of
trihydroxy alcohol glycerol unit to which three moles of fatty acids are linked. If for example,
three moles of stearic acid is attached to a glycerol unit the fat is termed as tristearine. The
linkage is formed by the removal of one water molecule at each linkage. This type of fats
(like tristearine) where only one type of fatty acid is bonded to the glycerol unit is called
simple triglyceride.

There is also a possibility that three different fatty acids can attach to the glycerol unit. For
example, if palmitate, oleic acid and stearic acid are attached to the first, second and third
carbon atoms of a glycerol unit, the fat is termed as palmitooleostearine, which is a mixed
triglyceride.

1. C - Palmitic acid
2. C - Oleic acid
3. C - Stearic acid
Palmitooleostearine

The assembling of fatty acids by plants or animal cell is not a random process rather it is
genetically determined. The position of specific fatty acids to the glycerol is also not
completely random, but determined genetically. Example, in specific fats lard (hard pig fat)
all of its palmitic acid is found in the 2 nd position, while in plant oils all of the saturated acids
are esterified to the 1st and 3rd position. The 2nd position is being esterified by unsaturated
fatty acids.

60
In animals there is a very small opportunity to modify this genetically determined situation by
the kind of diet supplied to animals. For example, if pigs are supplied with a diet not
containing palmitic acid, there is a possibly to accumulate other fats in their tissue.

Specific features of fats

Let us see some specific feature of fats under three specific titles.

1. Melting point
2. Process of rancidity
3. Hydrogenation

1. Melting point

Melting point (solidifying point) gives a useful measure of the hardness of the fat. These
hardness of fat depend on two things or indirectly reflects two things.

A. Carbon chain length: that is if fatty acid contain longer chain length, it will have higher
molecular weight and melting point and vise versa.
B. Degree of unsaturation: fats containing large quantities of unsaturated fatty acids will
have low melting point and vise versa.

Therefore the above two factors (A and B) are indicators or measures of hardness of fat.
There are however, specific measures of the above two.

To measure the degree of unsaturation a specific measure used called iodine number. This is
the number of grams of iodine absorbed by 100 gram of fat.

Example: if we have oil from two sources soybean and coconut, and if 130 molecules of
iodine is consumed per 100 g of soybean and only 8 is consumed by coconut, this will
indicate that soybean contains more double bonds or is high in unsaturated fatty acids. This is
because for every double bond there is a consumption of one molecule of iodine to make it
saturated. Hence the higher the iodine number the higher the content of unsaturated fatty
acids.

61
 I I

CH2 – CH = CH – CH2 - + I2 CH2 – CH – CH - CH2 –

The double bond point is a very reactive site which can react with halagens, O 2, H2, F2, I, etc.
Therefore in determining iodine number, for every double bond there is a consumption of 2
atoms of iodine for 2 = 4 for 5 = 10 iodine atoms. The higher the degree of unsaturation the
more iodine consumed per 100 gram of fat.

To estimate the chain length of fatty acids in fats a method used is saponification number.
When a fat is boiled with alkali it splits into glycerol and alkali salt of fatty acids called soap
and the process is called saponification.

Base + fatty acid Soap + glycerol

Saponification number is the number of milligrams of alkali (KOH) required to saponify 1

gram of fat. Naturally fatty acids contain only one COOH group. Therefore for every fatty
acid there is a consumption of one KOH. Therefore, the larger the saponification number the
smaller the average chain length. Example, if we have fat from two sources A and B one
gram each, as COOH
A) COOH B) COOH
COOH COOH
COOH COOH
COOH
COOH

COOH

If we add KOH to both only 5 units are consumed in the case of fat A whereas about 11 KOH
is consumed in fat B since has more COOH that is 5 for A and 11 for B which is important to
determine saponification number. The higher the saponification number, the higher the
number of short chained fatty acids and vise versa.

62
2. Rancidity

The process of rancidity is the type of chemical and/or physical change due to keeping of fats
for longer time. Fats are susceptible to two kinds of rancidity, hydrolytic and oxidative
rancidity.

Hydrolytic rancidity: is the result of hydrolysis or hydrolytic splitting of the fatty acids from
the glycerol, which is the opposite of triglyceride synthesis. This is produced by action of
enzyme lipase, which occurs in moulds & bacteria and in some fresh foods. This enzymes
specifically breaks the bondage on C1 and C3 of fatty acids attached to the glycerol unit, C2
however is more difficult to break. Under normal condition the products of lipolysis are
usually mixtures of mono and diglycerides with free fatty acids. Most of these acids are
odourless and tasteless, but some of the lower once, as butyric & caproic acids have powerful
taste and smell which may make the product unacceptably by consumers. This process
(hydrolytic rancidity) happens in lipid degradation in animals in the small intestine.
Therefore, nutritional speaking there is no loss of nutritional value of fats as a result of
hydrolytic rancidity.

Oxidative rancidity: this occurs in fats having substantial levels of polyunsaturated fatty
acids, when a result of oxidative process taking place in fatty acid chain.
-CH2 –CH = CH - CH2 –CH -

O2

CH2 – CH = CH - CHOOH - CH2- (hydroperoxide)

The double bond is a reactive site but oxygen occurs on the adjacent carbon atom of the
double bond not on the double bonds. The type of compounds that will be formed as a result
of oxidative process is called hydroperoxides, which are not stable and can break down to
aldehydes & ketones which do not have nutritional value. Therefore, oxidative rancidity will
create abnormal flavour and odour and seriously alter the nutritive value of feeds. This
process of oxidation could be prevented in feeds by the addition of certain products called
antioxidants like hydroquinone or ethoxyquine (synthetic antioxidants widely used). Vitamin
E serves as natural antioxidant in feeds containing a lot of unsaturated fats. This may create

63
vitamin E deficiency so must be included in the diet in sufficient amounts when fed along
with such kind of fats. Vitamin A or carotene is also useful as antioxidant to some extent.

3. Hydrogenation

This is the process where by hydrogen is added to the double bonds of the unsaturated fatty
acids converting them to their saturated analogs.
CH3

(CH2)7 CH3

CH H (CH2)16
+
CH H COOH

(CH2)7

COOH
Oleic acid Stearic acid

Hydrogenation has practical advantage since it improves the keeping quality by removing the
double bond. So this is used in the preparation of vegetable oils for food.

Dietary fat of ruminants undergo substantial hydrogenation in the rumen where by the
stomach of ruminants has a lot of free floating H 2 which will hydrogenate the double bond of
unsaturated fats. So the type of fat deposited in ruminants is always hard fat due to
hydrogenation. The lower the double bonds the harder the fat. In swine if you feed oil rich in
unsaturated fatty acids, will end up in the formation of soft fat since no hydrogenation
process in monogastrics. In ruminants however if you feed saturated or unsaturated fatty
acids you end up on saturated fatty acids so find hard fat in ruminants despite the content of
the fat in the feed.

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Compound lipids

i. Phospholipids (phosphatids)

This group of lipids contains carbon, hydrogen and oxygen common to all lipids also contain
phosphorous and most of them contain nitrogen. The role of phospholipids is primarily as
constituents of lipoprotein complexes of biological membranes. Cell membrane is made up of
lipoproteins. The lipid portion is phospholipids. Therefore, phospholipids are kind of lipids
involved in lipoprotein complex. In terms of distribution in animal tissue they are widely
distributed and found in every cell, but more abundant in the heart, kidneys and nervous
tissues. Myelin sheath of the nervous axon contains up to 55% phospholipids.

The most common occurring phospholipids or phosphoglyceride in higher plants and animals
are the lecithins and cephalins. In terms of structure they are the same, the difference is on the
nitrogen base attached to the 3 rd carbon of glycerol unit. If the nitrogen base is choline the
phospholipids is lecithin, if it is ethanolamine, it is cephalin. The two consists of glycerol in
which 1st & 2nd carbon are esterified with long chain fatty acids, often a saturated form at 1 st
carbon and unsaturated form at 2nd carbon, and the 3rd carbon is esterified to a phosphoric acid
and in turn to a nitrogen base of choline or ethanolamine.

Lecithin
CH2.O.CO . R1

CH. O. CO. R2

CH2 .O. PO3 . CH2.CH2. N+ (CH3)3
--------------------------------
Choline

NH2.CH2. CH2OH
Ethanolamine

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ii. Glycolipids

In these lipids two of the glycerol carbons are esterified by fatty acids while the other is
linked to a sugar residue. The fatty acid largely joined to the 2 nd & 3rd carbon atom positions
whereas the carbohydrate to the 1st position. There are two types of glycolipids, glucolipids
and galactolipids. In terms of importance and pressure is plants and animal tissues glucolipid
is insignificant as compared to galactolipid. Galactolipid is the predominant lipid found in
plant leaves as triglycerides in seeds. Out of the total lipids of grasses & legumes about 60%
is galactolipid. So for grazing animals consuming forage alone, they represent a major source
of lipid.

In galactolipids there may be one or more galactose attached to the 1 st position of glycerol
units. Monogalactosyl glyceride is when only one galactose unit is attached to the 1 st position,
and digalactosyl glyceride, those are having two galactose unit attached at C1 of the glycerol
unit. The galactolipids of grasses are mainly the monogalactosyl type but smaller quantities
of the digalactosyl type also exist. Rumen microbes but not monogastrics are able to break
the galactolipids to give galactose, two fatty acids and glycerol. Galactosyl glycerides are
preliminarily hydrolysed by the microbial galactosidases.

CH20H
O
HO H O CH2

H OH H CH.O.CO.R

H OH CH2.O.CO.R
Galactolipid

Glycolipids in animal tissues present mainly in the brain, and nerve fibers.

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 2. Non glycerol based lipids
i. Waxes

Waxes are lipids resulting from the combination of fatty acids & high molecular weight of
monohydroxy or dihydroxy alcohols. These do not contain glycerol in their structure but
esterification of fatty acids (common to all lipids) take place with high molecular weight
alcohols.

C-------------------------------OH

C-------------------------------OH
High molecular weight, dihydroxy alcohol (meaning it has long CH2 or carbon chain)

Wakes are usually solids at ordinary temperature. Waxes are component parts of plants and
animals where they serve a protective function. In plants we found waxes in leaves which
reduce water transpiration, especially in desert plants. In animal tissues waxes are found in
feather, hair, wool of farm animals serving as protective material against penetrating water.
They also occur as secretions and excretions in animals and insects like bee wax.

Waxes have a high melting point and unlike fats, waxes are not readily hydrolysed and are
unlikely to have any nutritive value. They are removed in the ether extract and often inflate
the nutritive significant of the assay.
From feather one could prepares a product called feather meal by chopping and pressing and
used as protein supplement to ruminants but waxes are not available to ruminants because of
strong bondage between fatty acids and monohydroxy or dihydroxy alcohols

ii. Steroids

These are very large numbers of chemical compounds have a basic ring structure
phenanthrene nucleus linked to a cyclopentane ring. Slight modification at any point of the
ring will result in the variation between the different steroids.

The steroids include:

 Sterols: include cholesterol and ergosterol

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 Bile acids
 Steroid hormones: include adrenal and sex hormones

Sterol: Cholesterol is one of the most important sterol and it is zoosterol or animal sterol.
This is a structural component of cells and occurs in smaller amount in all animal cells
(mainly found in brain). This can be synthesised in the body (liver) from acetate. So it is not
dietary essential.

One nutritionally important compounds is 7- dehydrocholesterol, which is derived from

cholesterol found widely spread under the skin of farm animals which is important precursor
of cholecalciferol (vitamin D3), which is produced when the sterol is exposed to UV light.

Cholesterol is a key constituent of membranes in higher animals. Cholesterol is the precursor

of other steroids such as sex hormones and bile acids and it is believed that its major function
is as source material for such synthesis.

Since cholestrol is very insoluble, prolonged high levels of cholestrol in the blood result in its
deposition on the wall of blood vessel which will bring in to heart attack (atherosclerosis).

Ergosterol is the principal plant sterol which is found widely distributed in yeast, brown
algae, bacteria and higher plants. This is important in animal nutrition as it is a precursor of
ergocalciferol (vitamin D2), into which it is converted by ultraviolet irradiation. Therefore,
there are two vitamin D sources, vitamin D3 (animal origin) and vitamin D2 (plant origin).
The two vitamins are different in terms of effectiveness.

Bile acids:- are major components of bile. These are produced in the liver from cholesterol
(constitute major end product of cholesterol metabolism) and stored in gall bladder or
released to the intestine continuously is animal having no fall bladder like rats & horses.

Bile acids have two specific functions

 Emulsification of fats, that is physical breakdown of fat molecules into smaller fat
molecules rendering them more susceptible to lipolysis and increasing the efficiency of
their absorption form the small intestine.

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 Activation of lipase, and by so doing play role in the chemical breakdown of fats. Lipase
is fat digesting enzyme found in inactive form immediately after production, which must
be activated which is done by bile acids.

Steroid hormones: Sex hormones are the once produced in sex organs such as oestrogen
(females sex hormone), androgen (male sex hormone) and progesterone. Adrenal hormones
are hormones produced in the adrenal cortex such as cortisol, aldosterol, corticosterol having
an important role in glucose & fat metabolism or energy metabolism.

iii. Terpenes

These lipids are not that much important. They contain certain common building blocks
called isoprene units linked together to form chains or cyclic structures.

CH3

CH2 = C- CH = CH2
Isoprene

It can give nutritional compounds such as carotenoids (vitamin A). It also contain xanthopyll
not a nutrient but give a yellow colour to poultry skin and egg yolk.

69
 3.4. Vitamins

Vitamins are nutrients, which have a physiological and nutritional significance. But these
group of nutrients (most of them) are unrelated chemically and is a group name. One specific
character common to all vitamins is that, they are required in minute quantities for normal
growth & maintenance of animal life. This fact is also shared with trace minerals but minerals
are inorganic while vitamins are organic substances.

There are at least 15 vitamins which has been classified as essential food factors and their
chemical structure and function known. There are also other chemical compounds similar to
vitamins but require further evidence to be classed as new vitamins. These include lipoic
acid, coenzyme Q (ubiquinons), vitamin B13, vitamin Bt , vitamin B17, rutin, inositol, and
others. These additional compounds have been suspected to have vitamin function or play
role as vitamin.

In addition to vitamins, there are other chemical compounds that could have a certain role in
bringing growth rate, better animal performance. These compounds are found in certain
specific types of food like in whey, fish, and by-products of alcohol fermentation. These
feeds improve productivity and growth of animals. But scientists were not able to know the
specific ingredient responsible for bringing this condition. Therefore, they call such products
as UGF (unidentified growth factors).

The identification of vitamins attribute to certain type of the experiments called purified diet
experiments. In this case animals will be supplied by diets containing mixtures of nutrients
proteins, fats, carbohydrates inorganic salts and the animal not perform optimally or show
deficiency conditions. So scientists concluded that there should be additional nutrient to
sustain animal life. The scientist Funk carried out such kind of experiments with other
scientists and coined a name to these essential nutrients as vital amines since he thought these
accessory food factors contain amino-nitrogen. It is now known that only a few of these
substances contain amino-nitrogen and the name has been shortened or changed to vitamins.

70
Vitamins are required in smaller quantity for animal metabolism. Its quantity is expressed in
mg/kg, g/kg, PPM. There is also another way of measurement called international units
(i.u.) but is abandoned as it is confusing or not standardised.

Vitamin A 1 i.u. = 0.3 g of crystalline retinal

Vitamin B1 1 i.u. = 3g thiamine
Vitamin C 1 i.u = 50 g of ascorbic acid
Vitamin D 1 i.u.= 0.025 g of crystalline vitamin D3
Vitamin E 1 i.u = 1mg of - tocopherol acetate

So international unit is not a standard unit to measure quantity of vitamin as it has individual
definitions for each vitamin. So other units mg, g, ppm are used in new books.

Table. Vitamins important in Animal Nutrition

Vitamins Chemical name
Fat soluble vitamins
A Retinol
D2 Ergocalciferol
D3 Cholecalciferol
E Tocopherol
K Phylloquinone
Water soluble vitamins
B complex
B1 Thiamin
B2 Riboflavin
Nicotinamide
B6 Pyridoxine
Panthothenic acid
Biotin
Folacin
Choline
B12 Cyanocobalamin
C Ascorbic acid

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Vitamins play a role in the metabolism process is as catalysts. The catalysts play a role in
chemical reaction but it does not changes its nature in the reaction. They do not involve as a
source of energy or as building materials for synthesis of proteins, amino acids, fats, etc.
They only serve as catalysts and at the end of the reaction remain unchanged. That is why
vitamins are required in minute quantities.

Deficiency

Normally one could observe two forms of vitamin deficiency, in the feeding of animals:

1. Avitaminosis: this is a situation where there is a deficiency of one vitamin. The symptom
observed in avitaminosis is specific to that vitamin. It could be avitaminosis A, K, C, etc.
Example, avitaminosis a results to night blindness.

2. Hypovitaminosis: hypo means low, and this is a condition of multiple vitamin deficiency
whereby more than one vitamin is deficient in the diet of the animal. Hypovitaminosis is
not specific to one vitamin but a number of vitamins may be deficient at the same time.
This type of symptoms is not specific but a general type like skin lessons attributed to
deficiency of viatmin C, E. we could also have a decreased in disease resistant as a result
of many vitamin deficiency.
Hypervitaminosis: refers to oversupply of vitamins. The most frequently observed are the 1 st
two avitaminosis & hypovitaminosis, hypervitaminosis is a rare and mostly occurs in
intensive type of production. In this case we supply additional nutrients as synthetic vitamins
which may results to the over supply of vitamins, and to its associated risks.

In intensive system of production, when we prepare rations we add small quantities of

vitamins and while mixing, the feed should be thoroughly mixed if not it may be concentrated
at one point and when consumed by the animals the high dosage may result to
hypervitaminosis. The hypervitaminosis is specific to certain vitamins A, D, K which will
result in decreased production or illness. Other vitamins not a series problem for
hypervitaminosis.

There are different situations that will result the deficiency condition of vitamin. These
include:

72
1. Under supply of vitamin/vitamins: when these is under supply, obviously avitaminosis or
hypovitaminosis will occur.

2. Antivitamins (vitamin antagonists): despite enough quantities of vitamin supplied to

animals, there could be vitamin antagonists which could be natural or synthetic products
which will ultimately result to deficiency condition. These products could be added for
better results such as to improve the colour, odour, etc of feeds but may form complexes
with specific vitamins thereby creating vitamin deficiency. Example, avidin that is found
in raw egg white, when consumed in large quantities by animals form complex with
biotin resulting to biotin deficiency. Raw fish when consumed contain specific bacteria
that produce thiaminase which break thiamine (vitamin B1) thereby creating deficiency of
thiamin.

3. Level of nutrient intake: almost all vitamins are involved in the metabolism of different
nutrients. Therefore, the quantity of the specific vitamin in dependent upon the rate of
metabolism in which it is involved. Example, vitamin B 6 is involved in the metabolism of
proteins; if supply a lot of protein, the animal will need more vitamin B 6 otherwise
deficiency of vitamin B6 will be produced. Thiamin (Vitamin B 1) is involved in
carbohydrate metabolism. So there is a need to increases it with the level carbohydrate
supplied. Increase in unsaturated fatty acid intake require more vitamin E supply. If not
there will be a deficiency condition. Therefore, the level of nutrient intake will have effect
on the requirement of vitamins.

4. Disease condition, parasitic invasion, bodily stress increases the animal requirement for
vitamins.

When animals are diseased, the animal will react to the situation by producing antibodies. So
there will be an increase in the metabolism rate which in turn increase the amount of vitamin
required. In the case of parasitic invasion, there will be production of antibodies which
increase vitamin requirement, absorption of vitamin takes place in the intestinal lumen and
parasitic invasion will result to the irritation of the intestine thereby decreasing rate of
absorption and increasing vitamin requirement and parasites themselves also will compete
with the host for vitamin thereby increasing the vitamin requirement.

73
Bodily stress such as cold and hot conditions will accelerate animal metabolic condition and
so to the vitamin requirements.

74
 Vitamins

Many different compounds are classed as vitamins. Vitamins are grouped into two depending
upon their solubility.

1. Fat soluble: are vitamins, which are soluble in fat and oil solvents, including A,D,E, and
K.
2. Water soluble: are vitamins, which are soluble in water and include vitamin C, vitamin B
complex groups.

The two groups show some specific differences, whereby fat soluble vitamins can be stored
in the fat of animal tissues such as around intestine, liver, kidney, under skin (fat storage
areas), the water soluble vitamins can not be stored by animals. This has nutritional
implication in that since animals do not store water soluble vitamins, they have to be supplied
in the diet regularly or daily, but not for fat soluble vitamins since the animal can mobilise the
stored vitamins.

The length of time for deficiency symptom to occur is longer for fat soluble vitamins since
can be mobilised from storage but in the case of water soluble vitamins the deficiency
symptoms develop quickly. The other thing is if we want to cure deficiency symptoms, water
soluble vitamins deficiency symptoms could be cured very quickly, whereas the deficiency
symptoms for fat soluble vitamins may take longer time and in some instances may not be
cured at all.

The fat soluble vitamins are primarily exerted in the faeces, via the bile, whereas water
soluble vitamins are excreted in the urine. Water soluble vitamins are relatively non-toxic but
excess of fat soluble vitamins can cause serious problems. The sign of deficiency of fat
soluble vitamins is specific but sign of water soluble vitamins deficiency is much less specific
as dermatitis, rough hair coat, poor growth, etc.

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 Vitamin A (C20 H29OH)

This vitamin gets its name as it was the 1 st vitamin to be discovered as useful component of
the animal diet. The vitamin is a pale yellow crystalline solid, insoluble in water but in fat
and various fat solvents. All animals require a dietary source of vitamin A. The vitamin does
not occur as such in plant products but rather as its precursor of this vitamin or as provitamin
A carotene mainly as -carotene. The body can transform carotene into the active vitamin.

A lot of carotene is found in green forages but upon curing some is lost partly due to
enzymatic (destruction require oxygen) and partly due to photochemical as carotene is
sensitive to light and heat. Liver, milk, egg yolk, butter fat and oil from fish are also rich
sources of vitamin A. The vitamin is also manufactured synthetically and can be obtained in a
pure form.

Retinol is the alcohol, retinal the aldehyde and retionic acid is the acid form of vitamin A.
vitamin A is fat soluble vitamin so is found in association with fats. The vitamin is usually
stored as the retinyl ester, usually palmitate. In the animal body it is mostly attached with
palmitic acid.

Conversion of the carotene into vitamin A, can occur in the liver but usually takes place in
the intestinal mucosa. One molecule of -carotene yields two vitamin A theoretical.

Function and deficiency symptoms of vitamin A.

Obviously the under supply of nutrients will result to impairment of the functions the
nutrient serve thereby resulting to the deficiency condition. The following deficiency
condition may happen as a result of vitamin A under supply.

1. The vitamin is vital in the synthesis of a product called rhodopsin which gives the animal
the ability to see in the dim light. When vitamin A is deficient rhodopsin formation is
impaired resulting to reduced ability to see in dim light commonly called night blindness
(nyctalopia).

76
2. Vitamin A is involved in animal reproduction both in male and female animals, and in
breeding animals its deficiency may lead to infertility. In pregnant animals the vitamin is
important for maintenance of placenta especially during the last 1/3 rd period of pregnancy.
So its deficiency may result to abortion. It may also result to a production of dead, weak
or blind calves. In male animals the vitamin play role in spermatogenesis, so lack of
vitamin will result for sperm production not to take place in required quantities and rate.
3. Vitamin A is important in the synthesis of Muccopolysaccharides. These are compounds
synthesised in animal cells in areas where there are a lot of mucous membranes, such as
internal structure of respiratory, alimentary, reproductive and genitourinary tracts. When
there is a deficiency of vitamin A, the production of mucopolysaccharides decrease and
the normal epithelium (mucous membranes) become replaced by stratified, keratinized
epithelium that is the layer would accumulate a lot of keratin, epithelium because harder,
and lubrication absent.

This keratinization lowers the resistance of the epithelial tissues to the entrance of infective
organisms. Thus respiratory troubles, such as colds and sinus infections may occur.
Keratinizaiton of gastrointestinal tract result to disturbances such as diarrhoea. The
genitourinary tract when keratinized result to the problem in urination as it interfere with the
normal secretion and execration of the urine, and there is a gradual accumulation of minerals
in the kidney and urinary bladder as there may no enough flushing out and form crystals. This
condition of accumulation of crystals in kidney and urinary bladder is called kidney stones or
bladder stones. Vitamin A is called antiinfection vitamin as has important role in combating
infection.

4. Vitamin A is concerned in the normal development of bones through a control excised

over the activity of the osteoclasts and osteablast (bone forming cells). So incoordination
of gates may be due to poor development of bones as a result of vitamin A deficiency.

In practical severe deficiency symptoms are unlikely to occur in adult animals except after
prolonged periods of deprivation as it is fat soluble vitamin and also grazing animal can get
enough vitamin A from grazing pasture. Cereal rations are poor is vitamin A.

Vitamin D

77
A number of different forms of vitamin D, are known although not all of them are naturally
occurring compounds. But the two most important forms are vitamin D 2 and vitamin D3
(ergocalciferol and cholecalciferol). Vitamin D 2 and D3 are formed by UV irradiation of
sterols ergosterol (plant origin) and 7-dehydrocholesterol (animal sterol). The provitamins as
such have no vitamin value and must be converted into calciferol before they are of any use
to the animal. For this conversion it is necessary to impart a definite quantity of energy to the
sterol molecule, and this can be brought about by UV light of sunlight, by artificially
produced radiant energy or by certain kinds of physical treatment. Under natural conditions
activation is brought by irradiation from the sun.

The chemical transformation occurs in the skin and skin secretions, which are known to
contain the precursor. Absorption of the vitamin can take place from the skin, since
deficiency can be treated successfully by rubbing cod liver oil into the skin.

Both D3 and D2 have the same feeding value for higher farm animals but D 3 is much more
effective for poultry than D2.
D vitamins are more stable to oxidation than A, D3 being more stable than D2.

Sources
The D vitamins are limited in distribution. They occur is dry forages and dry vegetable
opposite to vitamin A which occur in greens. Fish, egg yolk contain this vitamin, milk
however is a poor source although summer milk tend to be richer than winter milk.

Physiological function and symptoms of deficiency

1. This vitamin is involved in bone formation but the role is different from vitamin A.
vitamin A stimulates the laying down of the organic portion of bones. But to give strength
for bones mineraliztion is necessary and this aspect of bone formation or hardening of
bones is aided by vitamin D. This vitamin is actually involved in indirect manner in the
mineralization process whereby it is important in the synthesis of calcium - binding
protein, which is necessary for efficient calcium absorption from the intestine lumen and
being transported and deposited in the bone.

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2. Vitamin D also plays role in phosphorous absorption and also reabsorption of
phosphorous and calcium from the kidney and bone thereby reducing the amount excreted
in urine.
3. Vitamin D also serves a role in egg production, and hatchability specially egg shell
production as egg shell of poultry will contain a lot of calcium to harden it.

In relation to the functions mentioned, deficiency conditions will occur when there is less
vitamin D in the diet. A deficiency of vitamin D in young animals results to rickets, lack of
mineraliztion of new bones formed which will result to bones become flexible, weak and
easily breakable. Growth rate is generally adversely affected. The term rickets in confined to
younger animals is older animals vitamin D deficiency causes osteomalacia, in which there is
reabsorption of bone already laid down, the bones are already formed but since there is
constant mobilisation of mineral from bones they tend to be demineralized resulting in bones
become weak and brittle. Rickets and osteomalacia are not specific diseases necessarily
caused by vitamin D deficiency, but can be caused by lack of calcium or phosphorous or an
imbalance between the two elements.

In poultry deficiency of vitamin D result to reduced egg production and egg shell quality
deteriorates. This will result to laying of thin shelled eggs & easily broken, in extreme cases
shell less eggs may be produced. Bone and beak become soft and rubbery, legs become weak
& growth retarded.

Practically, the deficiency of vitamin D is rare practice as it is fat storable and for adult
ruminants it is not a problem since get it from grazing. But in poultry specially laying poultry
require higher level of vitamin D for eggshell formations so must be supplemented in layer
poultry.

Vitamin E (Tocopherols)

Vitamin E is a group name which includes a number of closely related active compounds.
Eight naturally occurring forms of the vitamin 4 saturated & 4 unsaturated are known. It
includes the alpha, beta, Gamma, zeka, zeta, eta, epsilon. But the - form is the most

79
biologically active or effective and most abundant. So vitamin E in many books is written as
- tocopherol.

Source
Vitamin E is widely distributed in feeds green fodders are good source of - tocopherol,
young grass being a better source than mature herbage. Cereal grains are good source of the
vitamin. Animal products are relatively poor in the vitamin but level depends on content of
vitamin E in the diet. Synthetic vitamin E is available. Vitamin E unlike vitamin A is not
stored in the animal body in large amounts for any length of time and consequently a regular
dietary source is important.

Function and deficiency symptoms

1. This specific vitamin is a natural antioxidant. So it functions in preventing peroxidation of

fats and thereby maintains the integrity of cell membrane as this can destroy structural
integrity of the cells and cause metabolic derangement. This change can account for many
of the observable symptoms of vitamin E deficiency. Vitamin E protects the vital
phospholipids from peroxidative damage in preventing formation of peroxides.

2. A less defined role of vitamin E is it plays a role in the development and function of the
immune system.

3. Vitamin E also functions in energy metabolism (phosphorylation), ADP, ATP, in

metabolism of nucleic acids, thio amino acids and vitamin c synthesis.

The deficiency signs of vitamin E may differ greatly amongst species and even within the
same species. Most important manifestation of vitamin E deficiency is muscle degeneration
(myopathy) or nutritional myopathy or muscular dystrophy also called white muscle disease
or stiff lamb disease which frequently occurs in young animal’s calves, pig, lambs, chicks. It
is associated with low vitamin E & high polyunsaturated fatty acids intake. Myopathy
primarily affects skeletal muscle which causes weak leg muscle which result in causes
difficulty in standing and after standing trembling & staggering gate. Eventually the animals
are unable to rise & weakness of the neck muscle prevents them form raising their head

80
called white muscle disease. The heart muscle is also affected & death may happen. In lambs
such condition is called stiff lamb disease.

Vitamin E deficiency in chicks may lead to a number of diseases like myopathy, nutritional
encephalomalacia (crazy chick disease) which is a condition where the chick is unable to
walk or stand and is accompanied by haemorrhages and necrosis of brain cells. Exudative
diathesis is another one and is a vascular disease of chicks characterised by a generalised
oedema of the subcutaneous fatty tissues associated with an abnormal permeability of the
capillary wall.

Testicular degeneration in pig, rooster, fish; fetal death in hen, cow, ewe; liver
necrosis in pigs, beef calves; hoemolysis of RBC in chick, man are also other deficiency
signs of Vitamin E under supply.

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 Vitamin K

This vitamin was discovered as a result of studies by chicks, which was discovered to be an
essential factor in the prevention of haemorrhage symptoms produced in chicks. The
discovery was made by a group of Danish scientists who gave the name Koagulation factor to
the vitamin which became shortened as K factor and eventually to vitamin K.

Although the vitamin is needed in physiological function in all species, a dietary need may be
unimportant in species other than birds because of synthesis in the digestive tract. In
ruminants it is synthesised by microbes in the rumen and monogastrics in large intestine
(cecum) by microbes available there. This synthesised amount is enough to meet the
requirement of animals. Therefore, there is no need for giving any special consideration to the
vitamin K content of the ration of farm animals except for poultry.

In certain conditions in chicks the deficiency of the vitamin is exaggerated by the fact that
there are parasites called coccidia which destroy the microbes that synthesise the vitamin.

A number of compounds are known to have vitamin K activity. The two most naturally
occurring compounds are
 Vitamin K1 (phylloquinone): found in green plants
 Vitamin K2 (menaquinone): is a product of bacterial growth or synthesised by
microorganism.

All forms of vitamin k are converted in the liver into menaquinone which suggest that this is
metabolically active form of the vitamin. Vitamin k is relatively stable at ordinary
temperatures but is rapidly destroyed on exposure to sun light.

Vitamin K plays a role in blood clotting and the role played is by assisting in the synthesis of
a protein called prothrombin in the liver, which is the inactive precursor of thrombin an
enzyme that converts the fibrinogen into fibrin, the insoluble fibrous protein that holds blood
clots together. Prothrombin normally must bind to calcium ion before it can be activated. If

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the supply of vitamin K is inadequate, the prothrombin molecule is deficient in -
carboxyglutamic acid a specific amino acid responsible for calcium binding.

In chicks if the deficiency of this vitamin is mild, symptom observed is anaemia & increased
in clotting time of blood and if deficiency is severe the chicks will bleed to death. But in farm
animals’ deficiency symptoms is uncommon.

Source
All green leafy materials, fresh or dry are rich sources of the vitamin. Liver, egg and fish
meal are good animal sources.

Water soluble vitamins

These include two basis vitamins, vitamin C and vitamin B complex groups.

Vitamin C (ascorbic acid)

Vitamin c is chemically known as L-ascorbic acid. The vitamin can be synthesised by all
farm animals but not in humans, guinea pigs, in certain birds and fish, due to the lack of an
enzyme called L-gulonolactone oxidaze. Other species synthesise the vitamin from glucose,
and therefore not dietary essential for these farm animals.

The vitamin is necessary for the maintenance of a normal collagen metabolism, play
important role is various oxidative- reduction mechanisms in living cells. It also serves as
antioxidant.

Deficiency of the vitamin in man is scurvy. This is characterised by such signs as swollen,
bleeding and ulcerated gums, loosening of teeth, weak bones, and fragility of the capillaries
which result to haemorrhage or oedema throughout the body. Emaciation and diarrhoea is
also observed. This reflects is basic role as tissue catalyst.

Since farm animals can synthesise this enzyme deficiency symptoms will not arise. But for
poultry dietary supplement may be essential under certain condition such as during climatic
stress as tissue synthesis may not be enough.

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Source
Well known sources of the vitamin are citrus fruits and green leafy vegetables (tomato,
potato). Milk is good source but much of vitamin may be lost during pasteurisation.
Vitamin B complex

Vitamins under this group have the property of being soluble in water and most of them are
components of coenzymes. Therefore daily supplementation of these vitamins is necessary
especially for monogastrics animals but in ruminants the microorganisms can synthesise all
of B group vitamins and their requirement be mate. In pig and poultry also part of their
requirement is mate but not enough so dietary sources to fill the gap is essential.

1. Vitamin B1 (Thiamin)

Higher plants synthesise this vitamin and so do many lower forms of organisms. All animals,
however, must have a dietary source unless it is synthesised by microbes in gut for them,
alike in ruminants.

The vitamin functions in all cells as coenzyme cocarboxylase thiamine diphosphate (TDP),
which is essential in the metabolism of carbohydrates, that is in oxidative decarboxylation of
pyruvate to Acetyl Coenzyme A in glycolytic pathway (essential process to provide energy
from carbohydrates for body processes); oxidative decarboxylation of - ketoglutarate to
succiny coenzyme A in citric acid cycle and pentose phosphate pathway; and synthesis of
valine in bacteria, yeast and plants.

When thiamin is deficient animals accumulate pyruvic acid and most of pyruvic acid is
converted to stable form lactic acid which will be accumulated in muscular tissue which
results to muscular weakness or muscular degeneration, or paralysis. In chicks accumulation
of lactic acid around neck muscle results to degeneration of the neck muscle and starring
upwards called star gazing.

Nerve cells are particularly dependent on the utilisation of carbohydrates. For this reason the
deficiency of thiamin has particular effects on nervous tissues. Thaimin deficiency may result

84
to a reduced fat synthesis as acetyl CoA is important for lipogenesis. Other symptoms of
thiamin deficiency include reduced appetite, emaciation, vomiting. In man a classic disease
beriberi represent last stage of deficiency of thiamin resulting to a peripheral neuritis, which
perhaps may be caused by accumulation of carbohydrate intermediates or may be due to lack
of permeability of membranes and that thiamin is localised in the membranous structure in
the nerve and plays a role is the sodium transport system.

A deficiency symptom for this vitamin is rare in practice, as thiamine is widely distributed in
feeds.

Source
Thiamine is wildly distributed in foods. The vitamin is abundant in brewers’ yeast, germ of
cereal grains & aleuronic layer. Other sources include beans, peas, and leafy crops, and
animal products like egg yolk, liver, kidney, and pork muscles. The synthetic vitamin is
obtainable, usually marketed as the hydrochloride.

2. Riboflavin (vitamin B2)

This vitamin functions as two coenzymes, as flavin mononucleotide (FMN) and flavin
adenine dinucleotide (FAD). Riboflavin is an important constituent of the flavoproteins; the
prosthetic group of flavoproteins contains riboflavin in the form of the phosphate FMN and
FAD. There are several flavoproteins in the body of the animal which all are involved in
chemical reactions involving the transport of hydrogen, which is important in carbohydrate
and amino acid metabolism in citric acid cycle. It is apparent that riboflavin plays many
essential roles in the release of food energy and the assimilation of nutrients.

It is hard to relate the deficiency symptoms to the specific biochemical roles of the vitamin
which have been established. Chicks’ deficient in riboflavin shows a peculiar type of leg
paralysis called curled toe paralysis, a specific symptom caused by peripheral nerve
degeneration in which the chicks walk on their hocks with their toes curled inwards. Other
deficiency symptoms that may be encountered include; diarrhoea, low egg production and
poor hatchability, poor appetite, retardation of growth, vomiting, skin eruption, eye
abnormalities, crooked and stiff legs, thickened skin, etc. It also affects reproductive systems
of sows.

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In ruminants microbial synthesis is the gut is adequate to meet body needs after the rumen
has developed. But for new-born calves and lambs riboflavin is a metabolic essential.

Source
The vitamin can be synthesised by all green plants, yeast, fungi & most bacteria but not by
animal tissues. Thus animals depend of plants for their supply except ruminants. In plants the
vitamin is more abundant on leaves so leafy forages as alfalfa are good sources. Cereal and
their by-products are poor sources and since these generally form the major diet of poultry
and pig, deficiency conditions may occur in practice.

Because of the bacterial action, poultry droppings are frequently richer in riboflavin than the
diet. This is of great significance with floor brooding where chicks have access to droppings.
In poultry the requirement decreases with age and chicks may recover from symptoms
eventhough the diet is not altered.

Yeast us the richest natural source of riboflavin. Milk specially whey, liver, heart, kidney and
muscle meat is rich sources from animal products.

3. Niacin (nicotinamide)

Nicotinamide is the amide derivative of nicotinic acid and is the form in which it functions in
the body. The term niacin is used to include both the acid and its derivatives.

Niacin can be synthesised from amino acid tryptophan. However, the efficiency of
conversation is poor which necessitates an exogenous source of the vitamin.

The vitamin has a widespread distribution among feeds, but that present is cereals can not be
counted because of poor availability or is found in a bound form which is not readily
available to monogastrics. Rich sources include liver, yeast, groundnut, sunflower meals, and
leafy pasture plants. Dairy products, egg and fruits are poor sources, though they contain the
precursor tryptophan. Because niacin is found in a wide range of feeds and because it is
partly synthesised in the body from tryptophan, deficiency symptoms are rare. Synthesis of
vitamin in the rumen of ruminants has been demonstrated.

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In the body niacin functions as a component of two coenzymes, nicotinamide adenine
dinucleotide (NAD) and nicotinomide adenine dinucleotide phosphate (NADP). Enzymes
containing NAD and NADP are important with carbohydrate, protein & lipid metabolism in
aspects of hydrogen transfer or as hydrogen transfer agents. So the enzymes involve in
oxidation-reduction systems.

Deficiency symptoms may vary between species and most of them are not specific
symptoms. This include poor growth, dermatitis, diarrhoea, loss of weight, poor feathering,
enteritis, mouth symptoms, loss of appetite, anaemia.

4. Vitamin B6

The vitamin exists in three forms, which are interconvertible in the body tissues. The parent
substance is known as pyridoxine, the corresponding aldehyde derivative as pyridoxal and
amine derivative as pyridoxamine. The term vitamin B6 is used frequently to describe the
three forms. The amine and aldehyde derivatives are less stable than pyridoxine and are
destroyed by heat.

Of the three related compounds, the most actively functioning one is pyridoxal in the form of
a phosphate that is pyridoxal phosphate which plays a central role as coenzyme in the
reaction by which a cell transforms nutrient amino acids into mixtures of amino acids and
other nitrogenous compounds required for its own metabolism (protein and amino acid
metabolism). The vitamin is also involved in the absorption of amino acids form the intestine
not only metabolism.

Deficiency symptoms

The animal growth rate will be affected because of biochemical lesson or reduction in amino
acid metabolism. Convulsion may occur due to accumulation of glutamic acid or as a result
of reduction is activity of glutamic acid decarboxylase. Other symptoms include, reduced
appetite slow growth, animal may develop anaemia, jerk movement, reduction in hatchability
and egg production

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In practice, vitamin B6 deficiency is unlikely to occur in farm animals, because of the vitamin
being widely distributed. Common sources include yeast, liver, milk, pulses, muscle meat,
vegetables and cereal grains are rich sources.

5. Pantothenic acid

This is an amide of pantoic acid and - alanine. Pantothenic acid is a constituent of coenzyme
A (coenzyme for acetylation) which is important coenzyme of acyl transfer. This combines
with two-carbon fragments from fat, carbohydrates and certain amino acids to form acetyl
CoA, an essential step in their complete metabolism, because the coenzyme enables these
fragments to enter the citric acid cycle. It is essential in the synthesis and catabolism of fats
and the synthesis of steroids. So the vitamin plays an essential role in many cellular reactions.

Deficiency symptoms

Deficiency symptoms of this vitamin include growth and reproduction failure, skin and hair
lesions, gastrointestinal symptoms like diarrhoea, lesions of the nervous system. There are
also different symptoms in different farm animals.

Source
The vitamin is widely distributed in feeds, indeed the name is derived from the Greek
pantothen means from every where, indicating its ubiquitous distributions both in animals
and plants. Rich sources include: liver egg yolk, groundnut, peas, yeast and molasses. Cereal
grains are also good sources.

This vitamin like other B vitamins can be synthesised by the rumen microorganisms. The
deficiency of pantothenic acid is rare in practical, as it is widely distributed.

6. Folacin

Folacin is used to describe a number of compounds, which are derivatives of folic acid
(monopteroylglutamic acid). The derivative of the vitamin which functions as coenzyme is

88
tetrahydrafolic acid which is derived from folic acid after absorption into cell. In the form of
this coenzyme the vitamin serves as a carrier of various one carbon groups (e.g. formyl,
methyl) that are added or removed from such metabolites as histidine, serine, methonine, &
purines.

Source
Widely distributed in nature. Green leafy materials, cereals, oilseed meals, animal protein
meals are good sources.

Deficiency symptoms

Nutritional anaemia and poor growth, poor bone development, poor hatchability leucopenia
(reduced number of white blood cells) are some of the deficiency symptoms of this vitamin.

With the exception of young chicks, folacin deficiency is uncommon in farm animal because
of the synthesis by intestinal bacteria. Prolonged oral administration of sulpha drugs is known
to depress bacterial synthesis of the vitamin and deficiency symptoms may occur by
medication of this kind. Synthesis occurs in rumen but for new born, they require dietary
supply.

7. Biotin

Biotin serves as a prosthetic group of several enzymes, which catalyse the transfer of carbon
dioxide from one substrate to another (both for CO2 fixation and decarboxylation). It involve
in addition of CO2 to pyruvate, adenine, gaunine, decarboxycation of oxalaoaccetate,
succinate. It also participates in addition of CO 2 to acetyl CoA to form malonyl CoA so is
important in fat synthesis. It participates in carbohydrate metabolism, protein synthesis,
amino acid deamination & nucleic acid metabolism.

Deficiency symptoms

Dermatitis, loss of hair or feathers and poor growth observed in all species. Reproductive
performance decrease in pigs as a result of under supply of the vitamins.

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Source
The vitamin is widely distributed in plant and animal tissues. Liver, yeast, milk and
vegetables are rich sources. Molasses, peanut meal, safflower meal are other sources.

Because of the vitamin being synthesised by microbes in the rumen and its wider distribution
in feeds, deficiency symptoms are rare for this vitamin. The presence of avidin in row egg
whites which may induce biotin deficiency by preventing its absorption from intestine after
being combined with the vitamin. Heating will inactivate this antagonist protein.

8. Vitamin B12 (cobalamin)

This has most complex structure of all the vitamins. This vitamin functions as a coenzyme
adenyl cobamide that play a role in several metabolic reactions. The coenzyme plays a role in
propionic acid metabolism in ruminants, in transformation of methyl malony CoA to succinyl
CoA, in biosynthesis of methionine from homocysteine or in protein synthesis and purine
metabolism.

Deficiency symptoms

A deficiency of this vitamin results in impairment of propionic acid metabolism in ruminants.

Vitamin B12 deficiency can be induced with the addition of high dietary levels of proponic
acid.

In humans pernicious anaemia is a vitamin B12 deficiency state in the tissues caused by the
failure of absorption of the vitamin, usually due to the lack of intrinsic factor (glycoprotin)
which is secreted by the gastric mucosa. Lack of intrinsic factor in man is hereditary (not a
problem to ruminants).

In poultry, poor feathering, retarded growths, kidney damage, and low hatchability occurs
due to deficiency of this vitamin. In pigs poor growth, incoordination of hind legs, rough
coat, dermatitis, suboptimal growth are observed.

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Rumen and intestinal synthesis of this vitamin is there which is adequate. But if the level of
cobalt in the diet is low a deficiency of the vitamin can arise even in ruminants, since cobalt
is the active centre or the nucleus of the vitamin. If cobalt level is adequate except for young
ruminants, dietary source of the vitamin is not essential.

Source
Vitamin B12 is considered to be microbial synthesis and its presence in food is thought to be
ultimately of microbial origin. There is no convincing evidence for its production by higher
plants and animals. The main natural source of the vitamin are foods or animal origin, liver
being particularly rich source, either because of ingestion of the vitamin in animal products or
because of rumen or intestinal synthesis in the case of herbivore. The best feed source are
fermentation residues & amount needed by all species is smaller than other vitamins, so
deficiency symptoms for the vitamin are rare.

9. Cholin

Unlike other B vitamins, choline is not a metabolic catalyst but forms an essential structural
component of body tissues. It is component of lecithins which plays a role in cellular
structure and activity. It plays role in lipid metabolism in the liver by preventing
accumulation of fat in this organ by promoting its transport as lecithin or by increasing the
utilisation the fatty acids in the liver itself (lipotropic factor). This also plays role in
transmission of nerve impulses by being essential for the formation of acetyl choline. Choline
can be synthesised in the liver from methionine, so level of methionine in the diet influence
choline requirement.

Deficiency symptoms
Slow growth and fatty infiltration of the liver or fatty livers, are some important deficiency
symptoms.
Sources
- Green leafy materials, yeast, egg yolk, cereals are rich sources. Since it is widely
distributed and can be derived from methonine deficiency symptoms are not common in
spits of high requirement by farm animals for the vitamin.

3.5 Minerals

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These are inorganic nutrients necessary in serving the animal body in may different ways.
Vitamins generally play role as catalysts, minerals on the other hand has many roles in
addition to their catalytic role by activation of many enzymes. Other roles of minerals
include.

 They are building blocks of animal tissues such as constituents of bones and teeth
(structural role), and also essential for synthesis of structural proteins like the mineral
sulphur.
 Minerals are components of organic compounds like iron haemoglobin, cobalt is vitamin
B12.
 Minerals serve a variety of functions as soluble salts in blood and other body fluids
playing role in maintenance of osmotic relations and acid base equilibrium (elector
chemical function).

The interaction of minerals with each other is important factor in animal nutrition and an
imbalance of mineral elements, as distinct with a simple deficiency is important in certain
nutritional disorders of the animals.

The mineral elements in feed or animal tissue as a group could be determined by burning off
the organic matter at high temperature in furnace (500-600 oc for 8 hours) and weighing the
residue, which is called ash. Such a determination tells nothing about the specific elements
present, and ash may include carbon from organic matter as carbonate when base forming
minerals are in excess.

The determination of the individual minerals could be accomplished by an instrument called

atomic absorption spectrophotometer. The determination of individual minerals has a
limitation since not tell us the form the mineral is found which affects the availability of the
minerals for the animals.

For example, calcium found in free form is more available but be precipitated by oxalates.
Therefore, calcium-oxalate is less available form. Phosphorous found as phytic acid or
phytate also less available than other forms like calcium phosphate. So the form should be
known.

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Minerals are essential for the functions mentioned. In the body we find many minerals, some
of which are essential, but others not yet considered essential. Some of the minerals may be
there in the body simply because they were present in the ingested food. To determine for a
mineral is essential or not we undertake purified diet experiments. An essential mineral
element is restricted to minerals which have been proved to have a metabolic role in the
body. When an animal supplied with purified diets lacking the mineral we want to test if;

 Deficiency symptoms appear and

 Those symptoms can be eradicated or prevented by adding that particular mineral or
element to the experimental diet, the minerals is said to be essential.

But when we follow such procedure in determining essential mineral elements we have to
provide purified diets which are practically not easy as minerals required for normal health
and growth by animals is in minute quantities and construction of diets deficient in the
mineral in question is often difficult to achieve.

In such studies it is also necessary to monitory the environment not only water and feed
supplied. The environment should be free from contamination as the animals may obtain the
minerals from cages, troughs, attendants or dust in the atmosphere which increase the
difficulty of determining essential elements. In recent years, improved technology such as
ultraclean, more or less, trace-element-sterile isolators and highly purified amino acid diets
have resulted in the demonstration of the dietary essentiality of several minerals such as
silicon and vanadium. Further more, more precise ways and accurate methods of determining
minute quantities of trace elements has been developed. Accurate analysis is essential, as
minerals are mostly found and required in minor quantities.

Classification of essential mineral elements

Essential minerals are classified into two depending upon their concentration in the animal or
up on the quantity animals require these elements.

1. Major element: are elements required in relatively larger quantities

93
2. Minor elements (trace elements)- are elements required is relatively less quantities.

Normally trace elements are present in the animal body in a concentration not greater than
50mg/kg and are required at less than 100 mg/kg diet. While the concentration of major
elements in the animal body is greater than 50mg/kg. Normally trace and major elements are
expressed in different units (values) whereby, major elements are expressed in percentage
(%) of the feed or g/kg as it larger quantity. Whereas minor elements are expressed in PPM
(parts per million), or mg/kg, or g/kg.

Nutritionally important essential mineral elements and their approximate concentration in the
animal body is indicated in the table shown. In addition to the elements shown in the table
chromium (Cr), fluorine (F1), silicon (Si), Vanadium (V), tin (Sn), arsenic (As) and nickel
(Ni) have been added to the list of dietary essential minerals. It has been suggested that as
many as 40 or more elements may have metabolic roles in mammalian tissues. Fortunately,
any of this trace elements, especially those of more recent discovery are required in such
minute quantities or are so widely distributed in animal feeds, their deficiencies are likely to
be extremely rare under normal practical condition.

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Table. Nutritionally important essential mineral elements and their approximate concentration
in the animal.

Major Minor
___________________ ________________________
Element g/kg Element mg/kg

Calcium (Ca) 15 Iron (Fe) 20-80

Phosphorous (P) 10 Zink(Zn) 10-50
Potassium (K) 2 Copper (Cu) 1-5
Sodium (Na) 1.6 Molybdenum (Mo) 1-4
Chlorine (Cl) 1.1 Selenium (Se) 1-2
Sulphur (S) 1.5 Iodine (I) 0.3-0.6
Magnesium (Mg) 0.4 Manganese (Mn) 0.2-0.5
Cobalt (Co) 0.02-0.1
---------------------------------------------------------

Mineral deficiency diagnosis

Nearly all essential elements, both major and trace are believed to have one or more catalytic
functions in the cell and serve other functions already mentioned. So under supply of these
elements will result in the development of deficiency symptoms.

Under mild deficiency condition, there will be a decrease in production. This is actually a
manifestation to any nutrient, so it is difficult to know the specific nutrient responsible for
this decreased production. Under mild deficiency condition, there is also a case where feed
intake is reduced. This decrease in feed intake could result in the development of deficiency
conditions of other nutrients due to the marginal intake resulted from reduced feed intake. So
a deficiency of a mineral that result in decreased feed intake may bring deficiencies of other
minerals or other nutrients, which ultimately affect production.

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If the deficiency is severe, deficiency symptoms may appear like for iodine deficiency results
goitre (swell the thyroid gland), phosphorous deficiency results rickets. This can not be
corrected, is late to take correction measures. Therefore, it is essential we identify sub-clinical
level of mineral deficiency or before such extreme conditions of minerals deficiency is
developed. But it is not easy to identify sub-clinical deficiency situations. There are three
different possible measures to identify the presence of this sub-clinical deficiency conditions.

1. Tissue analysis: plasma, liver, saliva, milk, urine analysis of minerals will give hint about
mineral level in the body.
2. Feed analysis: is a better indicator than others
3. Soil analysis: give indication to determine the sub-clinical deficiency of minerals for
grazing animals.

Different methods are preferred for different minerals to detect their probable deficiency. For
example for Zn the content in blood is constant if it lower than that level it is indication of
deficiency.

Table. Preferred sample source for mineral deficiency diagnosis.

Mineral Plasma Liver Saliva Milk Feed Soil Bone Urine

Ca + ++
P ++ +
Mg ++ +
Na ++
Cu + ++
Co ++ +
I ++ +
Zn ++
Mn +
Si + +

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Detection of sub-clinical deficiency condition is the 1st step in determining whether the
animal is getting enough of element or suffering deficiency condition. The next step is
confirmation step called critical supplementation test, whereby after detecting presence of
sub-clinical deficiency condition of a mineral, supplement that mineral to the animal and see
the animal performance. If the performance increases we are confirmed that the problem
identified in right. But there is a condition that the animal may not respond or respond
negatively. This may be due to either the animal is not suffering from the deficiency of the
mineral we are considering or may be other reason. For instance there is such a thing as the
theory of the first limiting nutrient. For instance when the animals are grazing in the dry
season, 1st limiting nutrient is nitrogen supply (protein supply) but not in wet season, and if
supplement grazing animals P in both dry and wet season animal respond only in wet season
not dry season because there is limiting factor. Therefore 1 st we have to be able to meet the 1st
limiting nutrient.

Supplementation of minerals

When we supplement protein or energy not a problem just supplement the nutrients with no
problem but when we supplement minerals, we could have series results or implication
because:

 Some minerals interfere with absorption and/or activity of other minerals. For example,
Ca and P, if oversupply one, it interferes with absorption of the other, and also promote
the excretion of the other in the urine. Other examples include copper- molybdenum-
sulphur antagonism by exerting their influence on copper retention, Cu-Zn-Fe, K-Mg
antagonism. If oversupply one, there will be less action of the other.

 Deficiency of different minerals could show similar symptoms. Example, deficiency of P

could be manifested in the development of rickets like deficiency of vitamin D and Ca. So
before supplementation, we must be sure which one is the real problem.

 Certain elements if they are oversupplied could be toxic. This is particularly true of Cu,
Se, Mo, Fl, V and arsenic as these are required in minute quantities. Therefore
supplementation of any diet with minerals should be carried out with great care and the
indiscriminate use of trace elements in particular must be avoided.

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Practical deficiency situation in tropical grazing condition are Na, P, Cu are known to be
deficient in almost all tropical grazing condition. Certain research done by ELCA (ILRI)
scientists in Borena region to identify these elements deficient and assure the same fact.

In this region Gursum & Jijiga, Woldu found Na, P are limiting but confirmed no problem of
Cu, French scientists in Awash Valley region found a series Cu deficiency which is series
problem for sheep production in the region as sheep is very susceptible for the deficiency.

Calcium

Over 70% of the ash of the body is Ca & P. In terms of quantity in the animal tissue, Ca is
found in most abundant quantity. Most of the Ca is found in skeleton and teeth, which is
about 99% of the total body calcium. The remaining 1% is found distributed in the rest of the
animal through out the organ and tissues.

The calcium in the skeleton in not stable since large amounts of calcium in bone can be
liberated by resorption. This is true to phosphorous also and takes place particularly during
lactation and egg production. Resorption of calcium is controlled by hormone secreted by
parathyroid glands, which mobilise Ca from bones to meet the requirement of the animal or
to maintain constant blood level. Since Ca is combined with P in bones, the P is also liberated
and excreted by the animal. The parathyroid hormone also plays important role in regulating
the amount of Ca absorbed from the intestine by forming Ca-binding protein. If parathyroid is
removed or fail to function blood level drops (hypocalcemia) & tetany occurs
(hyperirritability of neuro muscular system which in severe cases results in convulsion if
active demineralisation occurs).

Another hormone that controls blood Ca is calcitonin which decreases the rate of Ca
mobilisation from bone and therefore decreases blood Ca. When there is under supply of Ca
the animal tend to mobilise it from skeleton. So bones beside their structural role also serves
as stores of Ca & P which may be mobilised on demand. The situation is more organised
specially in the layers. The laying hen requires a lot of Ca in the feed and when they are
supplied with enough Ca they tend to store in a special bone called medullar bones (leg

98
region) only in this animal. This reserve is for security and is very dynamic than Ca in other
bones to be mobilised more easily on demand.

Other mechanism of controlling the Ca need of the animal is by the rate of absorption. If the
diet contains a lot of Ca, rate of absorption decrease but if the level in feed is lower the
absorption of Ca increases.

When we consider the amount of Ca that should be included in the animal diet, it is important
to consider Ca:P ratio of the diet, since as abnormal ratio may be as harmful as deficiency of
either elements in the diet. If we see ash of mammals from bones, it contains 36% Ca, 17% P,
0.8% Mg. This gives a ration of 2:1 (Ca:P) for mineral constituents of bones. The ratio
considered most suitable for farm animals other than poultry is 1:1 to 2:1 (Ca:P). The
proportion of Ca for laying hens is much higher, since the require it for egg shell production,
approximately 5:1 ratio is needed.

Function of calcium

1. Bone formation: Ca is needed in the building up of skeletal structure (mineralization of

bones).
2. Calcium is required for normal blood clotting, as it must be present for the formation of
thrombin from prothrombin.
3. Calcium is necessary for muscle contraction, myocardial function, normal neuromuscular
excitability, activation of several enzymes, secretion of several hormones and hormone
releasing factors.
4. Calcium serves in maintenance of acid bone balance to maintain pH at about neutral

Deficiency symptoms

1. Deficiency of the mineral results in malfunctioning of the mentioned purposes. One

symptom of Ca deficiency in young animals is rickets. This symptom is also shared with
the deficiency of vitamin D, and P and the imbalanced ration of Ca and P. Symptoms of
rickets are misshapen bones, enlargement of the joints, lameness and stiffness. In adult
animals Ca deficiency produces Osteomalacia in which the Ca in the bone is withdrawn

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 and not replaced or bones being demineralised. In osteomalacia the bones become weak
and are easily broken.

The condition of osteomalacia is encountered in many cases, especially in pregnant pigs. This
is because in pregnant animals normally foetus has priority for nutrient supply than the
mother. If there is under supply of Ca the animal mobilise form skeleton for mineraliztion of
bones of the foetus. This will result in demineralisation of the mother especially at the lumbar
region which results to the breakdown of these bones easily and nerve cells will be pinched
resulting in paralysis of back bone, as a result of breakage of the vertebrate bones. This is
also called posterior paralysis in pigs.

2. Calcium under supply could result to a deficiency condition called milk fever or
parturient paresis. This is a condition which mostly occur in dairy cows shortly after
calving. Blood Ca is maintained at constant concentration, but in this case there is a
drastic drop in Ca level in the blood, which may result to muscular spasm, and in
extreme cases paralysis and unconsciousness. The animal may even die unless given IV
injection of Ca or suppressing milk secretion by inflating the udder with air to build up
intramammary pressure to stop milk section.

Blood Ca is low in milk fever but low dietary intake is not the cause. It seems probable that
the parathyroid gland fails to mobilise blood Ca rapidly to meet the drain at parturition which
results from the onset of active milk secretion. High dietary Ca prior to calving is not helpful
but harmful to prevent milk fever. It increases the in incidence of milk fever because the
parathyroid becomes less active during the prolonged period of high dietary supply. A cow
subjected to Ca deficient diet shortly before parturition along with extra P during dry period
reduce incidence of milk fever by promoting parathyroid hormone secretion.

3. In case of poultry, since it is an important mineral for egg shell production, Ca deficient
diets may result to reduced egg production, thin shelled eggs, and production of shell less
eggs in extreme cases. Other symptoms in hen are soft beak and bones, retarded growth
and bowed legs.

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Source
Milk and green leafy crops especially legumes are good sources of Ca. Animal by-products
containing bone such as fish meal, meat & bone meal are excellent sources. In lactating
animals and laying hens, ground limestone, steamed bone flour and dicalcium phosphate can
be used. If rock calcium phosphate is given to animals, it is important to ensure that fluorine
is absent; otherwise the supplement may be toxic.

Phosphorous

This has more known function in the animal body than any other mineral elements.
Phosphorus is closely associated with Ca in bone & teeth and out of the total P in the animal
body 80% is found in a skeletal system. The other 10% is found attached with protein
(phosphoproteins), lipids (phospholipids), nucleic acids (RNA, DNA). The element play a
vital role is energy metabolism in the formation of sugar phosphates (Glucose-1-Phosphate,
Glucose-6-Phosphate) and adenosine di and triphosphates (ADP & ATP), NADP, NADPH
(important in transfer of H2). So P is important for bone formation, as constituents of high
energy compounds ATP,ADP, for phosphorylation of monsaccharides is during metabolism,
as component of phospholipids important constituent of cell membranes, and as constituents
of DNA and RNA.

Deficiency symptoms

1. Rickets and osteomalacia as it is required for bone formation like Ca.

2. Pica or depraved appetite has been noted in cattle. The affected animal has abnormal
appetite and chew wood, bones, rags, cloth and other foreign materials. Pica is not a
specific sign of P deficiency but can be caused by other minerals like Ca and Co.
3. In chronic P deficiency, animal may develop stiff joints and muscular weakness.
4. Phosphorous deficiency affects fertitliy or result to poor fertility of animals (especially
true for cattle). Apparent dysfunction of ovaries causing inhibition, depression or
irregular oestrus. Also reduce milk yield is cows.
5. Subnormal growth is young animals & low live weight gains in mature animals also
absorbed.

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Phosphorous deficiency is more common in cattle than sheep as the latter is more selective in
eating.

Sources
Milk, cereal grains and their by-products, meat products contains bone, dicalcium phosphate
are good sources of P. The content in dry grazing vegetation (hay & straw) is generally low.

Potassium

Potassium plays important part along with Na, Cl, and bicarbonate ions in the osmotic
regulation of the fluids and in the acid-base balance in the animal, principally functions as
cation of cells. Potassium plays an important part in nerve and muscle excitability. It also
plays role in carbohydrate metabolism.

Deficiency symptoms

In chicks, retarded growth, sickness & tetany followed by death and in calves severe paralysis
may occur due to lack of enough K.

The potassium content in plants in generally high, consequently its deficiency is rare is farm
animals kept under natural condition. One exception is when animals supplied with distillers
grains which are deficient in soluble elements like potassium.

Sodium

Like K, sodium is concerned with acid base balance and osmotic regulation of the body
fluids. Sodium also plays a role is the transmission of nerve impulse and in the absorption of
sugar and amino acids from the intestine.

Deficiency symptoms

Deficiency of Na leads to lowering of the osmotic pressure which result is the dehydration of
the body, poor growth, reduced utilisation of digested protein & energy, and reduced egg
production in hen.

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Source
Food of marine origin, meat meal, common salt (common material supplement for animals),
are good sources. Vegetables are poor sources.

Chlorine

Chlorine is associated with Na & K is acid base relationship and osmotic regulations. It also
plays important part is gastric secretion as it occurs as HCl.

Deficiency symptoms

Deficiency of Cl may bring alkalosis or an abnormal increase in the alkali reserve of the
blood caused by an excess of bicarbonate, since less Cl level is partly compensated by
increases in bicarbonate. Growth is also retarded.

Source
Fish, meat meal, common salt are good sources. The content of Cl in most feeds is low.

Sulphur

Most of the S in the animal body is in proteins containing amino acids cystine, cystine and
methionine. The vitamins biotin and thiamin, hormone insulin, metabolite coenzyme A
contain S. It is also found in bone, tendon, wall of blood vessels, and cartilage. Sulphur
containing compounds are also important in respiratory process. Most of S are found in
association with organic compounds and only few is found is inorganic form. Since most of
the S is ingested with proteins, little attention has been given to this element is animal
nutrition and its deficiency would indicate protein deficiency. But with the use of NPN like
urea, S must be included for synthesis of cysteine, cystine & methonine (sulphur containing
amino acids). In this case sodium sulphate can be used as rumen microorganisms can utilise
this supplement more than sulphur.

Toxicity may arise with too much S use due to conversions of S to hydrogen sulphide (which
is a toxic agent), by the gastrointestinal flora. This reduces rumen motility and cause nervous
and respiratory distress.

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 Magnesium

Magnesium is associated with Ca & P and about 70% of the total Mg is found in the skeleton
& rest distributed in soft tissue and fluids is of crucial to the well-being of the animal.

Magnesium is the commonest enzyme activator for different enzymes like oxidative
phosphorylation phosphate transferase, pyruvate carboxylase, pyruvate oxidase. So it is
essential for efficient lipid at carbohydrate metabolism. Magnesium also involves in cellular
biochemistry as formation of AMP, ADP, and ATP.

Deficiency symptoms

In rats convulsion & increased nervous irritability has been observed due to deficiency of
Mg. In calves tetany & death, in adult ruminants hypomagnesaemic tetany (magnesium
tetany) has been observed.

Source
Wheat bran, dried yeast, & most vegetable protein concentrate specially cottonseed cake &
linseed cake are good sources. Mineral supplement magnesium oxide is also commonly used.

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 CHAPTER 4
4. ENZYMES

A continuous series of chemical reactions takes place in plants and animals. As already said
at the beginning of this course that green plants can synthesize complex organic compounds
from simpler inorganic units in the presence of radiant energy, and in doing so fix and store
energy. Subsequently these compounds will be broken down by plants themselves or by
animals which consume the plants, and the stored energy is utilized.

To utilize this energy there is a complicated series of chemical reactions involved which is
reversible. When these reactions take place not in the animal body or laboratory the reactions
are often very slow, extreme high temperature and/or pressure would be required to increase
their velocity to practical levels. In living organisms such conditions do not exist. Yet the
storage and release of energy in such organisms must take place quickly when required,
which necessitates a high velocity of the reactions. The required velocity is attained through
the activity of numerous catalysts.

A catalyst in classical chemical sense is a substance, which affects the velocity of a chemical
reaction without appearing in the final product; or remains unchanged in mass upon
completion of the reaction. The catalyst elaborated and used by living organisms are organic
in nature and are called enzymes.

Enzymes are capable of increasing the rate of the reaction by a factor of at least 10 6.
Theoretically the reaction is also reversible and should reach equilibrium in living cells.

In living cells reaction products are removed and the reactions are largely unidirectional and
do not reach equilibrium. Rather they reach a steady state in which the concentration of the
reactants remains relatively constant. Reaction will speed up under demand, or slow down
when products are not removed rapidly enough, in order to maintain the steady state.
Enzymes affect both the forward and reverse reactions equally so that the steady states are
maintained (not changed). It is however, attained more quickly.

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Each living cell contains hundreds of enzymes and can function efficiently only if the action
of enzymes is suitably coordinated. It is important to appreciate that within the cell the
enzymes exist in distinct compartments. The cell is not a bag of randomly distributed
enzymes. The enzyme of the 1st stage in oxidation of glucose (the glycolytic pathway) are
present in the cytoplasm. Whereas those involved in the formation of acetyl- CoA from
pyruvate and its subsequent oxidation via the kreb’s cycle are limited to the mitochondria.

Enzyme action involves the formation of a complex between the enzyme and the substrate,
the substance to be acted up on. The complex then undergoes a reaction yielding the product
and the unchanged enzyme.

E+S ES E+P

In the absence of the enzyme the reaction S P would proceed through a transition state with a
free energy greater than that of either S (substrate) or P (product).

The difference between the free energy of S and that of the transition state is the activation
energy of the reaction. This is the amount of energy the molecule must acquire in order for
the reaction to take place. The rate of the reaction is proportional to the number of substrate
molecules having free energy greater than the activation energy. The formation of ES
complex creates a new reaction pathway and greatly reduces the activation energy. More
substrate molecule will have free energy in excess of activation energy and rate of reaction
will consequently be accelerated.

The change of the substrate (S) to product (P) requires 1 st activation of S that is the energy
content has to be increased or raised to high level to be ready to be changed to P. These
activation does not ensure the formation of P, as it is reversible reaction it can come back to
S.

In the reaction 1st change of S to activated form or ES complex will be formed and 2 nd change
of activated S will be changed to P. The 1st step is a limiting step since activation of S is
uphill type of reaction or is a rate determining step. If you compare the two reactions in the
figure, non enzyme catalysed reaction requires a lot of energy than the enzyme catalysed

106
once. Since the energy required is less when enzymes are present, the change of S to P is
faster.

For most reactions if you have S as starting material P is less in terms of energy since a lot of
energy will be lost as heat. The role of enzymes is only speeding up rate of the reaction by
decreasing the activation energy. How the lowering of activation energy occurs it not clear.
Enzymes can only catalyse at energetically possible reaction since energy must be there.

Most enzymes are complex proteins of high molecular weight. Most enzymes consist of a
specific protein moiety called the apoenzyme and a prosthetic group called cofactor or
coenzyme, which is essential for the activity of the total enzyme. The whole molecule is
holoenzyme (apoenzyme + coenzyme). Therefore, coenzymes are important in assisting the
enzyme action. In the absence of coenzym, the enzyme would be quite inactive. Coenzyme
assists in transfer of H2, Co2, C2, C, etc. So in the absence of coenzyme most reactions do not
take place.

For many enzymes to do their job, there must be the presence of certain compounds called
activators. Some enzymes at the time of production are present in an inactive form, which is
changed to the active state at the time and site when they are required. Example, trypsinogen
is synthesised in the pancreas, transported to the small intestine and changed to the active for
trypsin. The inactive precursor of proteolytic enzymes are known as zymogens (proenzymes).

Many enzymes require presence of metal ions in order to activate them such as arginase need
activator Mg ion for its action. This kind of mechanism confers considerable control over the
sitting and timing of enzyme action.

Coenzymes may be two kinds;

1. Prosthetic group which is permanently bonded will apoenzyme, and
2. Molecules which are initially bonded to apoenzyme but are released after the reaction.

In the animal body we could recognise two basic types of enzymes:

1. Extracellular enzymes: are those enzymes that are produced by cells where activity is
outside the cells that produce it.
2. Intracellular enzymes: are enzymes whose action occurs in the cell that produces it.

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In terms of quantity of the two in the animal body extracellular enzyme are very few in
number. Mostly this are involved in the process of digestion like those produced by liver,
pancreas where action occurs is in intestine. Intracellular enzymes are very many because
every cell could produce as many enzymes as 500. Therefore, there are quite a large number
of enzymes produced & most of them are involved in tissue metabolism & nutrient
metabolism in cells.

Classification of enzymes

This classification is based on the kinds of reaction catalysed by the specific enzymes.
Depending on the kind of the enzyme catalytic action or mode of action we have six
subgroups of enzymes.

1. Oxidoreductases: as it is clear from the name, these are enzymes that catalyse oxidation
reduction reactions. They catalyse the transfer of hydrogen, oxygen, or electrons from one
molecule to another. In oxidation reduction reaction when one substrate is reduced the
other is oxidised, i.e. the two takes place at the same time. An oxidation of one substrate
takes place at the expense of reduction of the other.
CH3 CH3

CHOH + NAD Lactate dehydrogenase CO + NADH2

COOH COOH
Lactic acid Pyruvic acid

Lactate is oxidised to pyruvate in the presence of lactate dehyrogenase. Lactic acid loose H 2
(2H) at 2nd carbon atom while NAD gained H and reduced. So the two takes place at same
time. Enzymes that catalyse such kind of reactions are called oxidoredutases.

2. Transferases: These groups of enzymes are involved in the transfer of certain entities
from one site to another, so are transferring enzymes. These can transfer groups such as
acety, amino, phosphate and the like from one molecule to another.

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Example:
COOH COOH COOH COOH

H-C-NH2 + C=O Transaminase C =O + HCNH2

CH2 CH2 CH3 CH2

CH2 CH2

COOH COOH
Alanine -ketoglutarate Pyruvate Glutamic acid

In this reaction the amino group is transferred to the ketoglutarate and the keto group goes to
the alanine. Enzymes that catalyse such kind of reaction is called transferases.

3. Hydrolases: these are enzymes that catalyse hydrolytic cleavage or enzymes that involve
hydrolysis. Example, peptidases (broke peptide linkage), esterases (break ester bond).
CH2.O.CO.R1 CH2OH

CH. O.CO.R2 + 2 H2O Lipase CH.O.CO.R2 + R3 COOH + R1 COOH

CH2 O.CO.R3 CH2OH

Triglyceride Monoglyceride Fatty acids

4. Lyases: is modification of hydrolases in that it involves lysis or decomposition of

chemical bonds but this lysis is non-hydrolytic (breaking bondage without addition of
water). Example, decarboxylation, deaminantion.
R R
Pyruvate decarboxylase
C=O CHO + CO2

COOH Aldehyde

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2-oxo-acid

COOH CH2

CH2 COS.CoA + CO2

COOS CoA
Malonyl CoA Acetyl CoA

5. Ligases: these ARE enzymes doing the opposite of lyases. In this case component things
will be brought together to form a single unit or is involved in attachment of compounds.
These enzymes catalyse certain synthesis in the body involving the breaking down of ATP &
other triphosphate to provide energy for the reaction. Certain synthesis reaction in the body
involves the breakdown of ATP or similar triphosphate, which provide the energy for the
reaction. These reactions are catalysed by enzymes known as ligases. The production of
acetyl CoA from acetate by acetyl CoA synthetase is typical example.

CH3 H CH3
+ ATP + H2O + AMP + PP
COOH + S.CoA COS.CoA
Acetic acid Coenzyme A Acetyl CoA Pyrophosphate

6. Isomerases: isomers are compounds with same chemical formula but different structural
formula. Isomerases are group of enzymes which catalyse intramolecular rearrangements
in optical and positional isomers.

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H2COH H2COH

HCOH HC OH

HOCH HO C H

HCOH HOC H

H C OH H C OH

CH2OH CH2OH
D-Glucose D-Galactose

The difference between two structural isomers is position of OH at C 4. Typical of this class of
enzymes are the epimerases such as Uridine di-phosphate glucose 4-epimerase which
catalyse the changes of configuration at the fourth carbon atom of glucose and galactose is
produced. This special reaction takes place is mammary gland which is required for lactose
synthesis a mammary gland is supplied only with D-glucose, part of it must be changed to D-
galactose.

Any enzyme can not catalyse any reaction rather an enzyme is specific for a type of reaction
it catalyses. The specificity of enzymes is variable depending on the enzyme.

1. Certain enzymes are absolutely specific, where we have one enzyme that catalyse only
one reaction called absolute specificity. The reaction catalyses only a single substrate.

NH2
E.g. C=O + H2O Urease 2 NH3 + CO2
NH2
Urea Ammonia
Urease hydrolyses only urea no any other nutrient.

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2. Relative specificity are enzymes that react with a number of substrates or is where an
enzyme catalyses similar or related reactions.
E.g. Peptidases: enzyme that catalyses decomposition of peptide bonds formed between
amino acids but no other reaction.

Specificity may arise from the need for spatial conjunction of the active groups of the
substrate with the active centre of the enzyme. The molecular geometry of both enzyme &
substrate must allow these reacting groups to come together to give a precise fit so called lock
& key model. Very slight modification result to loss of enzyme activity.

In some cases the conformation of the enzyme may not be absolute but may change in
response to the presence of the substrate to allow the formation of ES complex. This is
refereed as induced fit model. In yet others instances where more than one substrate in
involved, union of subtracts two and enzyme may not take place until and unless substrate
one and the enzyme have united.

Factors affecting enzyme activity

The effect of the enzyme in catalysing certain reactions could be modified by certain
conditions, which include:

1. Substrate concentration

In a systems where the enzyme is in excess and the S concentration remains constant, then an
increase in substrate concentration increases reaction velocity. This is due to increased
utilisation of the available active centres of the enzymes. If substrate concentration continues
to increase, utilisation of the active centres become maximal & no further increase in reaction
rate. Further increase in S concentration may lead to reduction in reaction rate as a result of
competition for the active centres by the excess substrate molecule which may bring
incomplete linkage between S and E.

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2. Enzyme concentration

When S is present is excess, increasing enzyme concentration gives a strait-line response in

reaction velocity owing to the provision of additional active centres for the formation of E-S
complexes. Further increase in enzyme concentration may result in some limiting factors,
such as availability of coenzymes. Enzymes are rarely saturated with substrate under
physiological condition.

3. Inhibitors

The catalytic action of enzymes may be inhibited by substances which prevent the formation
of a normal E-S complex. Such inhibitors may be two types competitive and non-
competitive.

A competitive inhibitor resembles the substrate in its chemical structure and is able to
combine with the enzyme to form enzyme-inhibitor complex in so doing it competes with the
substrate for the active site of the enzyme and formation of E-S complex is prevented.
Example, sulphonamide drugs.

A non-competitive inhibitor does not resemble the S in its chemical structure and not
complete with it for active site of the enzyme. It does however combine with the E at other
positions on the surface to form E- inhibitor complex. Since these complexes have available
active sites they are able to react with the S to give E-S complex and these breaks down to
yield E, inhibitor and product, but the rate of reaction is lower than that of the usual pathway.
Such inhibitors are termed reversible non-competitive inhibitors. There are also irreversible
non competitive inhibitors which are enzyme poisons which inactivate the enzyme and loss
its catalytic activity. E.g. Acetoacetamide, oxidising agents, organophosphorous nerve
poison.

4. Availability of energy

There is a need to give minimum supply of energy for the enzymes to catalyse the reaction,
otherwise the activity will decrease.

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5. pH of the medium

PH of the area in which the enzyme act have bearing with the activity of the enzyme. Many
enzymes are more effective in the region of pH 6 to 7 (neutral pH), which is that of the cell.
But some like extracellular enzymes show maximum activity in the acid or alkaline pH range.
But in any case the actual range of pH which in which the enzyme is working is only 2.5 to
3.0 units (5-8), outside this range the activity drops off very quickly. This is due to changes in
the degree of ionisation of the substrate enzyme (where the linkage between the active centres
is electrostatic which affect with the formation of E-S complex). In addition extremes pH
results to denaturation and subsequent loss of enzyme activity.

6. Temperature

Efficiency of enzyme catalysed reactions is increased by raising the temperature. The speed
of the reaction doubles for each increase of 10 oC). As the temperature rises however
denaturation of the enzyme protein may begin resulting in loss of efficiency or loss of active
centres. Above 50oC destruction of enzyme becomes more rapid, and most enzymes are
destroyed when heated to 100oC. All enzymes have a temperature range with in which they
are more efficient. So low temperatures will decrease enzyme catalytic efficiency.

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 CHAPTER 5
DIGESTIVE PROCESSES IN DIFFERENT SPEICES OF FARM ANIMALS

Many of the organic components of foods are in the form of large insoluble molecules which
have to be broken down into simpler compounds before being absorbed into the blood and
lymph.

Depending up on the type of feed animal consume animals are classified into three basic
groups.

1. Carnivorous animals: are animals that consume meat and meat like products (dog, cat).
2. Herbivorous animals: are animals that depend up on forages, herbage or any plant
material (ruminants).
3. Omnivorous animals: are animals that could consume either plant material or flesh (man,
pig).

Depending upon the feeding habit of the three groups of animals, the anatomical structure of
the digestive system is variable. The 1 st group is the once having the simplest anatomical
structure of the digestive system, 2nd most complicated and the last intermediate between the
two. The length of the gut is also smallest for the 1 st group, longest for 2nd and the 3rd
intermediate.

The digestive system is a complex system including all organs involved directly or indirectly
to the process of reception of feed or food particles, digestion of feed or food nutrients,
absorption of digested nutrients & excretion or elimination of waste material. Depending up
on this general definition two groups of organs belong to the digestive system.

1. Alimentary tract, or gastrointestinal tract (GIT), or gut or digestive tract: This is a tube
that runs from the mouth to anus. The various parts are mouth, pharynx, esophagus,
stomach, small and large intestine, and anus.
2. Accessory digestive organs: these organs involve in indirect manner to digestive process.
E.g. teeth, tongue, liver, pancreas the produce enzymes to or have some help to facilitate
the digestion process and are essential components of the digestive system.

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Digestion is a process whereby large insoluble feed particles are broken to simple, soluble
and absorbable particles. Absorption on the other hand is the passage of the digested nutrients
though the mucous membrane into blood circulation or lymph.

When we see digestion, we could recognize three forms:

1. Mechanical digestion: the mechanical activities are mastication and the muscular
contraction of the gut. As the name implies it involves mechanical or physical breakdown
of feed particles to result to decrease in size of feed particles.
2. Chemical digestion: this refers to digestion brought about by enzymes secreted by the
animal in the various digestive juices, through it is possible that plant enzymes present in
unprocessed foods may in some instants play a minor role is food digestion.
3. Microbial digestion: this is also enazymic, but is brought about by the action of bacteria
and protozoa and fungi which is more presently discovered to play some role. Microbes
are of special significance in ruminant digestion. In monogastrics microbial activity
occurs in the large intestine.

Mouth

As already mentioned, the alimentary tract contains different parts which start with the
mouth. The relative importance of the mouth and its component teeth, lips, tongue, cheeks,
salivary glands, varies with species. The function of mouth is most species is for prehension
or bring in feed, mastication (mechanical digestion), insalivation (mixing the feed with
saliva) of foods.

A. Prehension

Prehension means seizing or capturing of feed or feed material and directing it into the
mouth. So the 1st function of mouth is feed collection. This prehension process involve
certain structure of the mouth as lips, tongue, teeth, the relative importance of which may
vary in farm animals depending up on species, type of feed consumed, and age of the
animal.☼

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With regard to species for horses the principal organ of prehension are the lips whereas lips
of ruminants are less mobile and their main prehension organ is the tongue. Pigs effectively
use the pointed lower lips. Dogs & cats held food with their forelimbs and the movements of
the jaw & head bring the food to mouth. Cattle lips are immobile & tongue mobile but for
sheep lips more important than tongue as upper lips very mobile having W kind of shape
called half cleft. So for prehenesion in sheep and goats lips are important.

All ruminants not have upper incisor of the front teeth. These are replaced by tough structure
called dental pad. So the front teeth not play role is prehension. The lower incisor contact
with dental pads which play important role. The tongue of ruminant species (cattle) contains
pin like structure called filiform papillae are very useful when cattle have to take concentrate
feeds or grain in general.

B. Mastication

The process of mastication is basically accomplished by teeth, which means mechanical

breakdown or physical grinding process. The extent of mastication is variable amongst
species determined by the most parts by the kind food they eat and the physical structure of
the mouth and teeth. Ruminants are more efficient in grinding grasses and other forages they
consume as compared to monogastrics although much of this occurs during rumination when
bolus regurgitated and remasticated rather than the time forage consumed. This is due to
special modification in that ruminants normally grind the feed by the type of lateral
movement of the upper and lower jaw but monogastrics vertical movement, where the former
can better masticate the feed consumed. In contrast some ruminants such as cattle usually
swallow small grain seeds with very little chewing, so their grain should be ground or
cracked before feeding. Goats and sheep are generally more efficient in chewing grains than
cattle. In birds any grinding is done by the action of the grit in the birds gizzard as they have
no teeth & swallow whole feed. Carnivorous often swallow large chucks of meat with little
mastication.

If see ruminants when they graze they do consume quickly and masticate slightly so that it
can be swallowed after being mixed with saliva. This process of mastication is partial. All
ruminants ruminate. The time spent for rumination depends on the fiber content of the feed.
Grazing cattle commonly spend about 8 hours/day for rumination, 8 hr/d for grazing the 8 hrs

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for rest. Each bolus of feed regurgitated is chewed 4-0-50 times, and thus receive a through
mastication than during eating.

The process of rumination can be divided into different phases.

1. The 1st phase is small boluses are brought to the mouth called regurgitation. The content
of the rumen are continually mixed by the rhythmic contraction of its wall, and material at
the anterior end is drawn back into the esophagus & returned by a wave of contraction to
the mouth. These are small boluses swallowed after being mixed with saliva.
2. The 2nd phase is reswallowing liquids. The bolus regurgitated contain liquid and solid
portion, so the liquid will be squeezed and swallowed again.
3. Remastication and reinsalivation.
4. Reswallowing of bolus and other bolus come. This decrease physical size of the feed to
manageable size
The major factor inducing the animal to ruminate is probably the tactile stimulation of the
epithelium of the anterior rumen, some diets with little or no roughage may fail to provide
sufficient stimulation for rumination.

C. Insalivation

This means mixing feed consumed with saliva secreted into the mouth by three pairs of
salivary glands. The salivary glands are:
1. Parotid glands, which are situated in front of each ear.
2. Submaxillary (submandibular) glands, which lie on each side of the lower jaw, and
3. Sublingual glands, which are located underneath the tongue.

Smaller glands are found in the checks (buccal glands) and lateral areas of the lips (labial
glands). In many species, the secretions from different glands are slightly different from one
another. After production all will be mixed together. So the difference in composition not has
significance.

Saliva has got important functions to accomplish, which include:

1. To facilitate effective mastication, because the insalivation process softens the feed
consumed by the animal. This softening is important to facilitate process of swallowing
without injury.

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2. Saliva contains 99% water, the remaining 1% consists of mucin (mucous materials),
inorganic salts, enzyme (salivary -amylase), lysozymes. As saliva has some enzymes, it
has an enzyme action to play. The enzyme constituents are variable from species to
species. In man, rats, pigs saliva contains -amylase (ptyalin) that can break  (1-4)-
glucose linkage contain 3 or more D-glucose units. But the enzyme is not of great
significance in domestic animals. In horse, cat & dog and ruminants - amylase is
lacking.

In ruminants instead of - amylase, we salivary lipase an enzymes that hydrolyze lipids. So

lipid digestion in ruminants start in the mouth. There is also pancreatic lipase is small
intestine which is more effective than salivary lipase as salivary lipase is much diluted.

3. The enzyme lysozyme has been detected in many tissues and body fluids. It is capable of
hydrolyzing the  - (1-4) - N - acetyl - glucosaminidic linkage of the repeating
disaccharide unit in the polysaccharide of the cell walls of many different species of
bacteria, thereby killing and dissolving them. This enzyme breaks down bacterial cell
membrane. So saliva could kill bacteria and said to be important disinfectant.

4. Buffering effect: saliva help to neutralize acid formed by rumen microorganisms in

ruminants. Saliva can be a source of bicarbonate phosphate buffer for the rumen and
provides a mechanism of recycling urea.

In ruminant digestion, there is a lot of fermentation reaction in rumen which will produce a
lot of acids and pH of saliva is alkaline which will neutralize or buffer rumen action. In
monogastrics, there is a production of HCl in the stomach which can be buffered by saliva.

5. Saliva has got some effect especially important for ruminants because of its antifrothing
agent. Ruminants require fiber for proper digestion which has get pinching effect on the
internal environment of reticulo rumen important for ruminant digestion. When ruminants
graze on young clover rich pasture or pasture rich in legumes, there will be excessive
production of gases like CH4, CO2, H2 which may not be lost by eructation and the gas is
trapped in the rumen in foam which may result to bloat then to collapse or death of the
animal. The reticulo-rumen will bulge or swell as a result of bloat. This condition may be

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reduced by antifrothing agents and saliva will decrease the occurrence of bloat by decreasing
foam or froth formation which will aid in elimination of excess gasses from rerticulo rumen.

The amount of saliva production is dependent upon the feeding habit. Ruminant produce
significant quantity of saliva than monogastrics and saliva has more roles in ruminants, and
also ruminants consume high fiber which necessitate more saliva.

Stomach

The stomach of adult pig which is representative of monogastrics have the capacity of 8 liters
and consist of a simple compartment which functions not only as an organ for digestion of
food but also for storage. The stomach of pig can be divided into three regions viewed from
the exterior.

1. Cardia (entrance), is the part adjacent to esophagus.

2. Fundus, is the largest and middle part.
3. Pylorus (terminus), is the upper of small intestine.

The cardia and pylorus being sphincters (candiac sphincter, and pyloric sphincter) play role in
controlling the passage of feed through the stomach. The inner surface of the stomach is
increased in area by enfolding of the epithelium, and contains a variety of secretary cells
which collectively secrete the gastric juice. That is different parts has different glands which
secrete different things but will be mixed up at the end resulting the gastric juice.

Cardia glands secrete mucuos (alkaline). Fundic glands secrete pepsinogen, mucous, HCl,
intrinsic factor which is required for vitamin B 12 absorption. Pyloric glands secrete mucuos
and small amount of pepsinogen. Therefore, gastric juice constitutes different products
including; water, pepsinogens, enzyme rennin and gastric lipase, inorganic salts, mucin
(mucous), intrinsic factors, and electrolytes.

Different factors are concerned in stimulation of glands to secret gastric juice.

1. Cephalic phase; stimuli like sight and smell of food act via vagus nerve.
2. Gastric phase; by chemical sensors and distension of the stomach.
3. Presence of digesta in the duodenum elicit secretion by neural & hormonal message.

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Hydrochloric acid (HCl)

This is produced by the fundic glands. The function of HCl includes;

1. It activates the zymogen pepsinogen to its active form pepsin by removing low molecular
weight peptides from each precursor molecule. Also activate rennin an enzyme which
occurs in gastric juice of calves, young piglets to coagulate milk.
2. By decreasing the pH of stomach (up to 2), it kills most foreign bacteria ingested with
food and prevents unnecessary fermentation from occurring.
3. Different enzymes require different pH to function properly. Pepsin requires low pH (2 -
3.5 for pepsin followed in pigs) for its efficient action which is provided by HCl. So HCl
create appropriate condition for the enzyme action in the stomach.

Mucin

This is mucous type of product produced whose function include;

1. Lubrication; facilitate the movement of feed with in the stomach.
2. This is important to prevent attack of stomach cell by HCl which may be destroyed unless
protected. There is also pepsin proteolytic enzyme which could digest the stomach unless
protected. Musin secreted in large quantities fill the upper surface of the stomach and
prevents cell digestion.

Pepsinogen

Pepsinogen which is changed to pepsin by HCl, by removing low molecular weight peptides
from each precursor is protein digesting enzyme and is specific in action. Pepsin
preferentially attacks those peptide bonds adjacent to aromatic amino acids (e.g.
phenyalanine, tryptophan, tyrosin). It also has a significant action on linkages involving
glutamic acid (acidic amino acid), cyseine. Pepsin has also a strong clotting action on milk.

In a protein chain pepsin looks for aromatic amino acids or acidic amino acids. Therefore,
end product of digestion of protein in stomach will be mixtures of polypeptide of different
chain length and few amino acids.

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Young animals like calves, lambs, kids, piglet basically depend on milk. So there is
additional enzyme rennin or chymosin produced by stomach of young animals. This enzyme
is essential to bring about coagulation of milk proteins (similar in action with pepsin). This
facilitate for a better attack by pepsin and other protein digestive enzymes and better
utilization of milk protein. Rennin makes milk to remain in the stomach for longer time than
the same substance in the liquid form. The reaction takes place in the presence of calcium
ions.
Casein + rennin  paracasein (soluble)
Paracasein + Ca  calcium paracaseinate (coagulum)

In carnivores; in addition to the high protein, meat contains a lot of fat. So there should be
another mechanism where the excess fat could be degraded. So there is gastric lipase in low
concentration in the gastric juice which hydrolyze fat that contain short or medium length
fatty acid chains. Most fat digestion occurs in small intestine. Carnivorous have the largest
gastric lipase, herbivorous the lowest.

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 Small Intestine

The small intestine is divided into three parts:

1. Duodenum; is the 1st part of the small intestine. Ducts from the pancreas and liver enter
duodenum a short distance behind the pylorus.
2. Jejunum, is indistinctly separated from duodenum. The jejunum & ileum are continuous
and there is no gross demarcation between them.
3. Ileum; is the last part of small intestine. It enters large intestine at ileo-ceco- colic
junction.

Next to the stomach the partially digested digesta goes to the small intestine in small
quantities controlled by pyloric sphincter. The kind of digestion of that occurs in small
intestine is essentially the same in all farm animals. This is a site where most of the digestion
and absorption activities take place in the gut. The small intestine is the principal site of
absorption of amino acids, minerals, vitamins, and lipids and in non-ruminants soluble
carbohydrates.

Most digestion takes place in the small intestine because this organ has a capacity to produce
a lot of enzymes that hydrolyze different nutrients. This is also a site where enzymes
produced by some accessory glands (liver, pancreas) are accumulated or poured through
tubes.

There are four different kinds of secretions or juices secreted either by small intestine or
accessory glands which are important in digestion.

1. Secretion of the duodenal glands or Brunner’s glands

This is produced by the duodenum of small intestine and is alkaline secretion which enter the
duodenum through the ducts situated between the villi, duodenal juice.

Function:

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A. The secretion is alkaline product so it neutralizes the incoming food of stomach, since
the food is acidic in nature. In doing so it protects the duodenal wall from the HCl
entering the stomach, which may damage the cells of the duodenum.
B. The other function is, it acts as lubricant (lubrication function) so that the movement of
the feed through the intestine is smooth.

2. Bile

Bile is produced by liver and stored in the gall bladder until required except in horses which
contain no gall bladder and continuos flow occurs after production. Bile passes to the
duodenum through bile duct.

Gall bladder not only store bile but also concentrates bile, adds mucuos to the bile, serves as a
relief mechanism to prevent excessive pressure in the hepatic duct coming from the liver
substance.

Release of bile occurs by a hormone cholecytokinin. Bile secretion by liver is stimulated by

secretin and gastrin, also concentration of bile salts in blood absorbed from intestine. Bile
contains salts of bile acids (sodium and potassium salts of bile acids) glycocholic and
taurocholic) which play an important part in digestion by emulsifying fats i.e. physical
degradation of fats to decrease the size which facilitate enzymatic action and activation of
pancreatic lipase as it is produced in an inactive form. These salts increase solubility of fats &
absorption of fats & fat soluble vitamins, and also aid in obtaining an alkaline pH in the
intestine.

Bile also contains bile pigments (coloring materials) biliverdin and bilirubin whose function
is not established, and are end products of haem catabolism. Bile also contains cholesterol
and mucin, the latter acts as a stabilizer for maintaining fat in an emulsified state and the
former is precursor to make bile salts.

3. Pancreatic juice

This is secreted by pancreas which lies in the duodenal loop (upper portion of small
intestine). The content of pancreatic juice opens into the duodenum through the pancreatic

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duct. Pancreas has two function endocrine (hormone production) and exocrine (production of
pancreatic juice).

Secretion of pancreatic juice is under hormonal control by two hormones produced in the
mucusa of duodenum in response to the presence of food and acid from the stomach. There
are two phases for the synthesis

A. First phase is when the acid (HCl) enters the duodenum; the hormone secretin is liberated
from epithelium of small intestine to the blood. When this hormone reaches the pancreas,
it stimulates the pancreatic cells to secrete a watery fluid containing bicarbonate ions but
very little enzymes.

B. Second phase is when peptides and other digestive products reach the duodenum, another
hormone pancreozymin (cholecytokinin) is liberated from mucusa to blood then the
pancreas stimulate the secretion of proenzymes and enzymes to the pancreas. Together
make pancreatic juice.

This pancreatic juice contains a lot of digestive enzymes which include: trypsinogen,
chymotrypsiongen, procarboxypeptidases A and B, preoelastase, -amylase (pancreatic
amylase or amylopsin and pancreatic diastase), and lipase (pancreatic lipase), and lecithinases
(hydrolyse bond linking fatty acids to the - hydroxyl group of lecithin), nucleases (hydrolyse
DNA & RNA to component of nucleotides).

Protein digesting enzymes are produced as proenzymes (zymogens). Trypsinogen is

converted to active trypsin by enterokinase (enzyme of succus entericus). Once enterkinase
change some trypsinogen to trypsin, the trypsin itself can catalyze the reaction thus
constituent autocatalytic reaction or self catalytic reactions. Trypsin also converts
chymotrypsinogen into active enzyme chymotrypsin. Procaroboxypeptidases are converted
by trypsin into carboxypetidases. These enzymes have pH optima of around 7 to 9, and the
proportions of different enzymes change in response to the nature of the diet.

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4. Succus entericus

The internal side of the small intestine is made up of certain projection like structures called
villi which mainly assist in the process of absorption by increasing surface area of the
intestine. In the villi there are small depressions called crypts of lieberkhun scattered
throughout the small intestine which contains special glands that produce succus entericus.

This juice contain; enterokinase (activate trypsinogen), maltase, sucrase, lactase, oligo 1,6 -
glucosidase (which attacks -(1,6) links of limit dextrins), aminopeptidases, dipeptidases,
ribonucleases (hydrolyse RNA) deoxyribonuclease (hydrolyse DNA), Nucleosidases (attack
linkage between sugar & nitrogenous base liberating free purines and pyrimidines),
phosphatases (complete hydrolysis by separating the orthophosphoric acid from ribose or
deoxyribose).

Small intestine as already said is a site where most of the digestion takes place, as there are
lots of enzymes secreted or poured to small intestine. Bile, succus entericus, pancreatic
enzymes, and brunner’s gland secretions.

Process of digestion

Proteins

Protein degradation starts in the stomach by pepsin which is specific to bonds having
aromatic amino acids, cysteine and gluctamic acid. In the small intestine, there are different
proteins digesting enzymes. These enzymes have specific activity and are of two types.

1. Exopeptidases: are enzymes that attack the peptides from the end of the chain, splitting
off the terminal amino acid which has a free - carboxyl group. These attack protein
chain at the outer chain of the molecule. Example, carboxypeptidases, aminopeptidases,
dipeptidases.

Aminopeptidase and dipeptidases are exopeptidases. Carboxypeptidase is specific, whatever

length is a protein chain there is always 1 NH2 & 1 COOH end. This carboxypeptidase is

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specific to attack protein molecule at carboxylic end. Aminopeptidase attack the protein
molecule from the amino end.

2. Endopeptidases: these are enzymes attack peptide bonds in the interior of the molecule
or at the center of protein chain.

Trypsin and chymotrypsin split the whole protein. Trypsin attack peptides or proteins and
chemotrypsin attack peptides. Trypsin is very specific and only acts upon peptide linkages
involving the carboxyl groups of lysine and arginine. Chymotrypsin is specific enzyme
attacking peptide bonds involving the carboxyl groups of tyrosine, tryptophan, phenylalanine,
and leucine.

By the action of all these variable enzymes, proteins would be degraded into amino acids
which are absorbable forms of proteins.

Carbohydrates

Pancreatic  - amylase similar to salivary - amylase and attack - (1-4) glucan links in
starch & glycogen. Amylopectin on the other hard contain in addition to - (1-4) glucoside
linkage a number of branched  (1,6) glucosidic linkage which are not attacked by -
amylase. The product hence includes a mixture of branched & unbranched oligosaccharides
termed limit dextrins in which - (1-6) bonds are abundant.
Starch - amylase Limit dextrins  - amylase, or Maltose
Glycogen (intermediate) oligo –1,6-glucosidase

Maltase

Glucose
 - amylase; hydrolyse (1-4) linkage to limit dextrins then to maltose.
 Oligo-1,6- glucosidase; attack  (1-6) linkages of limit dextrines.
 Maltase; hydrolyse maltose to 2 glucose units.
 Sucrase; hydrolyse sucrose to glucose & fructose.
 Lactase; hydrolyse lactose to glucose & galactose.

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In this way absorbable units of monsaccharides are produced as digestion end products of
carbohydrates.

Fats

The degradation of fats takes place in the small intestine. The primary objective of lipid
digestion & absorption is to arrange the lipid in a form that is water miscible since the
microvilli of the small intestine are often considered to be covered with an unstirred aqueous
layer.

Fat hydrolysis is helped by emulsification of fats which is brought about by the action of bile
salts, which also has the property of making micelles.

The pancreatic lipase hydrolyses the triglyceride droplets into fatty acids and monglycerides.
The enzyme does not completely hydrolyse triglycerides and the action stops at the
monglyceride stage, which reduce the lipids into a finer and finer emulsion.

The enzyme lipase acts on the 1st and 3rd carbon atom of glycerol unit and fatty acids are
preferentially removed from 1st & 3rd carbon atom position, leaving a monoglyceride which
have a polar (glycerol) and non polar (fatty acid) end, which is itself in excellent emulsifying
agent.

CH2OH

Triglyceride Lipase C- fatty acid + 2 Fatty acids

CH2 OH
Monoglyceride
(Absorbable form of lipids)

Although triglycerides are insoluble in micelles, monoglyceides and most fatty acids with the
exception like stearic acid dissolve forming mixed micelles.

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The bile, monoglyceride and free fatty acids become oriented into a mixed micelle
containing a lipid core and a polar exterior. The micelle has fewer diameters than fat droplets.
All but the bile is absorbed into the mucosa, eventually move to intestine for reabsorption and
recirculated through liver. Most of triglyceride is absorbed by the time the engesta reaches
the jejunum, with in the mucosa, fatty acids and monoglycerides are resynthesized into
triglycerides.

Digestion & absorption is superior with short chain length fatty acids, more unsaturated fatty
acids, as triglycerides rather than free fatty acids. In all probably the ability to participate to
form micelle is a reason for greater absorbability.

Large intestine

Generally large intestine could be seen as having three basic parts, caecum, colon and rectum.
The three parts may have different sizes and structures in different farm animals. For
example, the caecum of poultry has two caeca wings like structure.

The caecum and colon are more important for some species of animals called equines
(horses, donkeys, mule). In such animals these organs constitute the largest part of gut. In
horse for example, 60% of capacity of digestive tract is caecum and colon, whereas the rest
parts constitute only 40%. This is a compensation of unclassified stomach (undifferentiated
stomach) as opposed to ruminants which have a classified stomach. In this part of the gut of
equines a lot of microbial activity takes place. This kind of fermentation is more or less
similar to rumen microbial action.

Digestion in the large intestine for materials which is not digested in above part of the gut as
cellulose and hemicellulose is brought about by enzymes which has been carried down in the
food from the upper part of the tract or occurs as a result of microbial activity.

Extensive microbial activity occurs in the large intestine specially caecum in pigs. The
microorganisms metabolize both dietary and endogenous residues resulting in the formation
of a number of products. Indole, sketole, phenole, hydrogen sulphide, amines, ammonia and
volatile fatty acids (mainly acetic, propionic and butyric acids). In the pigs cellulose digestion
is accomplished to a limited extent in the large intestine. Some of B vitamins also get

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synthesized here but not enough for pig’s requirement. Poultry has two ceca & a colon but
get little or nothing out of hind gut fermentation; the microorganisms in birds are actually
more of a handicap than an advantage.

The large intestine contains bacteria & protozoa which digest food constituents in the same
way as rumen microbes. It has been estimated that in horse hind-gut fermentation accounts
for 30% of the digestion of dietary protein, 15-30% of the digestion of dietary soluble
carbohydrates, 75-80 % of the digestion of dietary cell wall carbohydrates. With diets of hay
& concentrates, horses digest about 85% of the organic matter that could be digested by
ruminants. Therefore, there is a significant fermentation taking place in the large intestine
which result to synthesis of B vitamins, volatile fatty acids, microbial proteins, gases also
formed. Inorganic elements and water are reabsorbed in the large intestine.

However, such herbivorous like equines are in a disadvantage as compared to ruminants due
to:
 Because the location of large intestine is beyond the main site of absorption small
intestine, many of the products of digestion like amino acids and vitamins may not
absorbed.
 Because digesta are not held for sufficient time for chemical action as opposed to
ruminants in which the main products of rumen fermentation has ample opportunity not
only to be absorbed in the remainder of tract, bot also has many opportunity to be acted
upon by the enzyme of the host in the lower tract like stomach and small intestine.

The disadvantage of rumen digestion is that all foods constituents are exposed to forestomach
fermentation, which may bring a loss of nutritive value for quality feeds.

Large intestine has no secretion of enzymes, so no enzymatic degradation unless there are
enzymes coming with the food from small intestine. But there are mucous glands producing
mucous for lubrication.

Large intestine is a point where a lot of water absorption takes place. In caecum lot of
fermentation takes place since engesta is rich with water, but as go down content of water
decreases or digesta becomes drier. So in colon fermentation becomes less and rectum no

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fermentation but rectum is a temporary storage place for feces, which will be voided via the
anus.

Composition of feces
 Left over water
 Undigested feed residues
 Digestive secretions (enzyme, mucous)
 Epithelial cells from the tract
 Bacteria (deferent types)
 Products of microbial decomposition, example, indole and sketole (found in all animals)

In monogastric animal there is fermentation or bacterial action in large intestine (ceacum).

Most bacteria found are proteolytic and they degrade the incoming protein to indole and
sketole not amino acids. These two compounds have a special smell which provide the
particular smell to feces. In addition there is production of gases CH4, H2S, H2, and CO2 due
to mirobial fermentation in large intestine. In ruminants most of fermentation takes place is
rumen and gases are remove via the mouth while in equines it is removed via the anus by the
process of belching. This is why we hear equines farting most of the time.

Digestion in the fowl

The gut of poultry differs from other monogastric animals (pigs) in many aspects.
1. In the fowl the lips and checks are absent and replaced by another structure called beak
and the teeth are also absent. Taste in poultry is limited.

2. If we see structure of gut of poultry we have beak and then esophagus. Esophagus in birds
is modified to form a pear-shaped sac called crop or diverticulum not found in higher
forms of farm animals. The main function of crop is as a reservoir for holding food and
plays little role in the digestion process. Some microbial activity occurs there and results
in the production of lactic and acetic acids. Action of salivary amylase also occurs here.

3. The esophagus terminates at the proventriculus of glandular stomach, or end of esophagus

has proventriculus or glandular stomach. This is also called true stomach, because there

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 are certain glands that produce gastric juice, similar to the structure and function of pig’s
stomach. This contains pepsinogen & HCl.

The need for crop becomes obvious when you see the size of proventriculus which is small in
capacity. Therefore, crop serves as an additional store so that the feed will be stored
temporary until transferred to proventriculus and only small quantity of food is gradually
brought to proventriculus. The proventriculus has minimum inherent motility and food passes
through as a result of esophageal contraction.

4. The glandular stomach leads to the gizzard which has no counter part in the pig. This is a
modification of gut of poultry, he structure of which is made up of very strong muscles
which are in constant motion thereby facilitating physical breakdown of feeds. The
gizzard wall produces koilin, a protein-polysaccharide complex similar in its amino acid
composition to keratin, which hardens in the presence of HCl. Gizzard is a muscular
organ which undergoes rhythmic contraction and grinds the food with moisture into a
smooth paste.

Poultry has another assisting mechanism for physical degradation. These are small stones in
the gizzard called grit, which facilitate physical degradation of feed by about 10%. This
structure or grit could be assumed as substitute of teeth found in other farm animals.

After feed materials get mixed with gastric juice in the proventriculus the feed goes to the
gizzard and chemical degradation is limited in the proventriculus because of hard nature of
the feed. In the gizzard there will be physical degradation which increase the surface areas of
the feed to be attacked by enzymes of proventriculus, but gizzard not produce enzymes.
Therefore, proventriculus & gizzard are equivalent in function to the mammalian stomach.

From the gizzard the feed goes to small intestine which is similar to other farm animals. In
fowl two bile ducts and three pancreatic ducts pour to small intestine.

From small intestine feed goes to large intestine which you find two large blind sacs (ear like
structure) called caeca at the junction of small intestine and large intestine. The caeca
functions mainly as absorption organs, but not essential to the fowl as surgical removal
causes no harmful effects. It does not play significant role in fermentation to poultry.

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The whole structure of large intestine is much shorter in poultry and found very short colon in
fowl whose function is to transport digesta to cloaca. The large intestine terminates in the
cloaca, a special structure not equivalent to the anus since functions as an orifice where
digestive, urinary and reproductive system products are removed under this common
opening. We have elimination of feces (grayish or black portion) and urine (white portion)
together. Urine is mostly uric acid. Egg is also removed by this same office.

The enzymes present in gut of fowl are similar to other mammals, although lactase has not
been detected. You find salivary -amaylase whose action in the stomach continues in the
crop. Pancreatic juice contains same enzymes as the mammalian secretions. Digestion of
carbohydrate, proteins and fats in the small intestine believed to be similar to pig. Intestinal
mucosa also produces similar enzymes like mammals.

The effect of enzymes in the gut is age dependent. Certain enzymes are active at early age
(lactase, rennin) but other as the animal’s age increases.
Size of the gut of different farm animals and also the relative size (capacity of different
portions) is important and different in different species of farms animal (see attached Table).

Table. Approximate capacity of the Digestive tracts of certain animals (volume in litres)

Human Horse (450 Sheep (80kg) Cattle (575 kg)

Body wt/kg Pig kg)
(190kg)
Rumen-reticulum - - 17 125
Omasum - - 1 20
Abomasum 8 8 2 15
Total stomach 8 8 20 160
Small intestine 9 27 6 65
Large intestine 10 55 4 35
Total gut 27 90 30 260

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The capacity of the gut varies depending on physiological state of the animals, and type of
diet, as gut is capable of considerable stretching depending on above factors. Volume
increases when animals fed bulky diets and decrease when fed concentrate diets, as less food
is needed to satisfy need of the animal.

If we see the ratio of length of the gut to body length, for sheep/goats it is 27:1, for swine
14:1, for dog/cats 4:1. So herbivorous has largest and carnivorous the shortest ratio.

Digestion in ruminants

The stomach of ruminants is divided into four compartments, rumen, reticulum, omasum and
abomasum. In young ruminants, calves, kids, lambs the 1st two called fermentation bags are
undeveloped and milk reaching the stomach is channelled through a tube like fold of tissue
called oesophageal groove or reticular groove that direct the milk directly to the third &
mainly fourth parts of the stomach, the omasum and abomasum. This is because fermentation
of milk in foregut is not essential.

When young animals start to eat solid food (fibrous feed) the 1 st two compartments, often
considered together as the reticulo-rumen enlarge greatly until in the adult they comprise
85% of the total capacity of the stomach. The proportion of the 1 st two and the last two
compartments at three ages are shown below

_______________________________________________________
New born calf At two months age Adult
_______________________________________________________
Rumen and
Reticulum 30 67 85

Omasum and
abomasum 70 33 15
---------------------------------------------------------

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In the adult, oesophageal groove doesn’t function under normal feeding conditions, and both
food and water goes into the reticulo-rumen. However the reflex closure of the groove to
form a channel can be stimulated even in adults, particularly if they are to drink from a teat.

Ruminant animals are important group of farm animals. Due to the differentiated stomach,
they are in a position to change inedible materials (grass, by products) to useful and highly
nutritious product like meat and milk.

The process of digestion in ruminants starts in the mouth. The food mixed with saliva will go
through oesophagus to the 1st part of stomach rumen. Next to rumen the structure found is
reticulum then omasum and abomasum. The abomasum is also called true stomach since this
is more or less equivalent in function to stomach of monogastric animals which produce
gastric juice.

The largest proportion of the ruminant stomach is the rumen and reticulum which are said to
be fermentation bags. The chemical breakdown of food in the reticulo-rumen is brought about
by enzymes secreted, not by the animal itself but by micro-organisms. The reticulo-rumen
provides a continuous culture system for anaerobic bacteria and protozoa, and also some
fungi that produce enzymes that hydrolyse various nutrients.

Rumen contents contain 85-93% water on average, but they often exist in two phases. A
lower liquid phase, in which the final feed particles are suspended and a drier upper layer of
coarse solid material (floating fibrous food).

Bacteria and protozoa are responsible for fermentation occurring in the reticulo-rumen. The
bacteria number 109 -1010 per ml of rumen content while protozoa are present in much
smaller number i.e. 106 ml rumen fauna but being larger may equal to bacteria in total mass.
Over 60 species of bacteria are identified.

The number of different microbes is variable depending on the type of diet consumed. With
high concentrate feed the number of protozoa decreases because concentrates result to much
and fast fermentation to take place in the rumen which reduces the optimum p H of the rumen
(5.5. to 6.5 is an ideal pH for bacteria and protozoa) which is deleterious to rumen protozoa.
The proportion of bacterial species also change with diet type.

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A normal rumen flora (bacteria) and fauna (protozoa) is established quite early in life, as
early as 6 weeks of age in calves. Ruminants get protozoa from other ruminants.

Ruminants without protozoa are apparently normal and healthy. Benefits get from protozoa is
therefor questionable. Protozoa attack cell wall & take soluble sugars, also ingest and digest
bacteria and change to prozoal protein which may comprise about 25% microbial protein
digested by host animals. But protozoa have the undesirable characteristics of being retained
in the rumen, preventing its use by host. With better diets faunated animals are advantageous.

20% of nutrients absorbed by host is synthesised by the microbial biomass in the rumen.
Bactrial DM contain 10% N of which 80% is in the form of amino acids, 20% being nucleic
acid N. some amino acids are contained as peptidoglycan of the cell wall membrane, and are
not digested by the host animals.

Rumen Reticulum
Omasum Abomasum

The 1st two chambers, the rumen and reticulum accounts for more than 50 % of the total
digestive tract. This large capacity is essential to allow feed retention to give enough time to
break cellulose and other complex carbohydrates, which mammalian enzyme can not. They
are only separated by a fold in the wall and there is no specific orifice which joins the two
organs together. However, there is a considerable difference in the appearance of the wall of
the rumen and reticulum.

The rumen contains a lot of small infoldings to increase the internal surface area and also
contains small projections in internal side of rumen called rumen papillae. Running from side
to side across the rumen are a series of muscular pillars which are capable of contraction. The
rhythmic movement of these pillars causes the whole rumen to contract and expand leading to
a through mixing of its contents.

The reticulum is the most cranial compartment. It is aslo called honeycomb, as it contains
honeycomb like compartments. Its location is just behind the heart. Materials enter the rumen
from oesophagus at the junction of rumen & reticulum. For this reason foreign bodies such as

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stone or nails (wire) frequently accumulate in the bottom of the reticulum & are in a very
good position to penetrate into the heart.

Materials which is in the process of digestion passes freely backward and forward between
the rumen and reticulum for which reason they are often considered as merely being parts of
one large organ, termed the reticulo- rumen.

Digesta leaves the reticulo-rumen though a small passage called the reticulo-omasal orifice,
and enters the third chamber of the gut called the omasum which is about 6% of digestive
tract in capacity. The omasum is located to right of rumen & reticulum just caudal to liver. It
contains leaf like structure or folding that increase the internal surface area. One important
role of this chamber is the absorption of large amounts of water from the digesta as leaf like
structures are made up of lot of absorptive places. Because of this absorption, the content of
omasum is dry. Omasum contains short, blunt papillae which grind roughage or help in
physical degradation as the leaf like structures are in constant motion giving rise to this
physical degradation. The omaso-abomasal orifice leads to abomasum from omasum.

The abomasum is about 8% of the capacity of gut. The four compartments comprise 60-65%,
small intestine 25%, large intestine 10%, ceacum 5%. The abomasum is true stomach which
produces gastric juice and accomplish similar role like the stomach of mongastric animals.

A lot of chemical changes take place in the different stomach parts of ruminants, as well as
different sites of the gut. To study the different changes that are taking place across the gut,
surgical modification or surgical opening at different sites of the gut takes place.

Since ruminants are helpful, and not compete with humans for grains as monogastrics due to
the microbial activity in the reticulo-rumen, a lot of research was undertaken on such species
of farm animals to understand how digestion takes place in the reticulo rumen and to device
means to modify such activity for more efficient digestion and better productivity eventually.
Therefore, one best study is by making surgical modification in the rumen called rumen
fistulation.

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1. Rumen fistulation

This means we make small hole or opening on the rumen and fix it with fisula. The rumen is
found on the left side of an animal. Make opening between the hip bone and lumbar vertebrae
which you find rumen. This special point is called paralumbar fosa (small depression region).

Open skin next rumen, join the side of the outer skin and the rumen and fix the outer skin to
internal rumen. When fixed it is permanent opening to sample and use at any time things like
pH, bacteria, rumen degradability, etc. Fistual would be fitted in the hole in paralumbar fosa.
After surgical operation animal should be given antibiotics until the wound heel. Mostly use
for cattle, also smaller structure for sheep.

2. Oesophageal fisula

Fistula can be made at any point of gut. This is made on the oesophagus of the animal next to
mouth. At the middle of oesophagus open the skin & make the fistula. This is important for
grazing animals. Farm animals are selective type of plant eaters. We find many grass species
on grazing land and then we try to study nutrient of grazing animals, if we collect samples
from the yard and undergo chemical analysis the sample may not be a representative sample
of what animals eating. To exactly know what type of plant species animal eating & analyse
nutrient contents, when animal grazes & swallows samples could be taken through
oesophageal fistula and analysis can be made. This will give you a representative sample of
what an animal consumes

3. Tracheal fistula

There is a lot of fermentation in the reticulo-rumen resulting to the production of different

gases and when we want to study the quantity of these gases, the option is to measure the gas
exchange. The gas exchange is through nose and mouth. But the gasses coming through
mouth and nose are mixture of gases coming from reticulo-rumen and lungs. Therefore there
should be some mechanism to separate gasses of the two. To do this tracheal fistula is made,
whereby the trachea leads to lungs and oesophagus to GIT. Tracheal opening when animal
exhale gas goes through opening while the gases coming from oesophagus is only through
mouth and nose.

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4. Abomasal and intestinal cannulas

These are a tube fitted to any part of GIT of the animal. You may fit one point of cannula at
the abomasum other at the duodenum or you may fit both points in the small intestine and can
measure different things such as flow of digesta across the gut, difference in the protein
content, how much carbohydrates or nutrients are digested, etc. So such kind of things could
be accomplished in such a way.

Digestion of carbohydrates in the reticulo-rumen

(Fermentation of carbohydrates)

Carbohydrate degradation in the reticulo-rumen interms of farm animal production is very

important phenomena, thereby grazing animals or ruminants depend upon grazing vegetation
which are almost carbohydrates with less proportion of fats, proteins and minerals. Thus the
degradation of carbohydrates is very important aspect of utilisation of feeds of ruminants.

The diet of ruminants contain considerable quantities of cellulose, hemicellulose, starch &
water soluble carbohydrates mostly in the form of fructans, pentosans, xylans, and also find
lingin in association to these carbohydrates. Young pasture frequently sole feed for ruminants
contain about 40% cellulose and hemicellulose, and 20% water soluble carbohydrates. In
mature herbages (hays and straw) the proportion of cellulose and hemicellulose is much
higher (60%) and water soluble carbohydrates content decrease. The  linked carbohydrates
are associated with lignin which may comprise 2-12%. So depending on age of the plants, the
composition of carbohydrate will differ.

Carbohydrates will be fermented in the rumen of ruminants so that they can utilise the energy
contained in it. The breakdown of carbohydrates in the rumen may be divided into two
stages.

1. Digestion of complex carbohydrates into simple sugars which is accomplished by

extracellular microbial enzymes or enzymes produced by microbes found in the
reticulorumen action of which is outside the microbes that produce them.

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Cellulose is one major carbohydrate consumed by ruminants which could be decomposed by
one or more -1,3- glucosidases to cellobiose which is then converted either to glucose, or
through the action of phosphorylase to glucose -1- phosphate.

Glucose
Cellulose  -1, 3- glucosidases Cellobiose
Phosphorylase Glucose –1- phosphate

Starch and dextrines are 1st converted by amylases to maltose and isomaltose and then by
maltases, maltose phosphorylases or 1,6-glucosidases to glucose or glucose-1- phosphate.

Maltose Maltose Glucose

- Starch Amylases
Isomaltose
Maltose phosphpoylase 1,6-Glucosidases
Glucose-1-Phosphate

Fructans are hydrolysed by enzymes attacking 2,1 and 2,6 linkage to give fructose, which
may also be produced together with glucose by the digestion of sucrose.

2,1 and 2,6 linkage

Fructans hydrolysing enzymes Fructose Phosphorylase Fructose -6-P

Sucrose Sucrase Fructose Phosporylase Fructose-6-P

+
Glucose Phosphorylase Glucose-6-P

Pentoses are the major product of hemicellulose breakdown which is brought about by
enzymes attacking -1,4 linkage to give xylose and uronic acid. The latter are then converted
to xylose. Xylose may also be produced from hydrolysis of xylans which may form a
significant part of the dry matter of grasses.

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2. The 2nd stage in rumen degradation is that the simple sugars produced in the 1 st stage of
carbohydrate digestion in the rumen are rarely detectable in the rumen liquor as they are
immediately taken up and metabolised by intracellular enzymes of micro-organisms intra-
cellularly. For this second stage, the pathways involved are similar in many respects to
those followed in the metabolism of carbohydrates by the animal itself.

Glucose Glucose – 1 - P Fructose- 6 - P Fructose-1,6-

diphosphate Pyruvate

Pyruvate forms intermediate product. Pyruvate production is the 1 st stage both under
anaerobic or aerobic condition from glucose. This releases some energy for the microbes and
produces four atoms of hydrogen. Pyruvate under aerobic condition oxidise to CO 2 and H20
with further production of energy. One kg of glucose in this way result 16 MJ of energy but
only 1/6 as much under anaerobic as there is incomplete oxidation.

Under anaerobic environment of the rumen the pyruvate is oxidised in a variety of ways to
result different volatile fatty acids (VFA) is cell of micro-organisms. The main acids
produced in the rumen are acetic, propionic and butyric acids, and gasses CO 2 and CH4
(methane). These are main end products of metabolism of carbohydrates in the rumen.

Additional smaller quantities of VFA (branched type can be produced in the rumen from
deamination of amino acids. Isobutyric is derived from valine, 2-methly butyric from
isoleuine, valeric from proline, 3-methylbutric from leucine.

Interms of quantity the 3 VFA acetate, propionate and butyrate are the most important, and
also gases CO2 and CH4. The total concentration of VFA in the rumen liquor varies between 2
and 5 g/liter or 70-150 mmol/liter depending on the kind of the animal diet, and the time
sample taken or time elapsed since the previous meal.

The relative proportion of the different VFA also vary with feed type. The predominant acid
is acetic, and roughage diets high in cellulose give rise to acid mixtures particularly high in
acetic acid. As the proportion of concentrates in the diet increase, the proportion of acetic
acid fall and propionic acid proportion rise. With all concentrate diet propionic acid may even
be more than acetic acid because of the decrease in the number of cellulolytic bacteria which

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are favoured by high cellulose diets, but promote starch fermenting bacteria which promote
propionate production which is needed in fattening animals.

Kinds of reactions from glucose to produce VFAs

1. Acetic acid, C6H1206 + 2H20 2 C2H402 + 2 C02 + [8H]

2. Propionic acid, C6 H12 06 2 C3 H602 + 2(0) – 4H
3. Butyric acid, C6H1206 C4H802 + 2C02 + 4H

When these VFAs produced for acetate and butyrate a lot of hydrogen is produced. Unless
removed it may be accumulated and make the rumen environment very reduced. But to keep
the hydrogen level at constant, there is a mechanism where the excess hydrogen reacts in a
methnogenic bacterium with C02 and converted it to methane.

CO2 + 4H2 CH4 + 2H20 + energy

The quantity of methane produced in quite large about 7% of its food energy. So an effect
directed to decrease the production of CH 4 formation may economise energy loss. Some CH 4
may also be derived from formate by the process of methagenesis (HCOOH + 6H
CH4 +2H20).

Of all the gasses produced in the rumen methane account for 30 to 40%, CO 2 account for
40%, hydrogen for 5%, and the oxygen and nitrogen variable based on the content in the
ingested air. Most of gases are removed by eructation. If the gas accumulates it causes bloat.

If there is a possibility of decreasing hydrogen production, we can economise the energy.

This could be accomplished by decreasing the reaction that produces most of the hydrogen,
acetic acid formation. For these different chemicals are produced to be used as feed additive,
example, rumensin also called momensin. Small quantity of momensin decrease hydrogen
formation and methane production too by changing the molar proportion of VFA enabling the
animal to conserve energy.

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Much of the VFA (>90%) is absorbed in foregut rumen, retiulum and omasal walls. Some
may pass through the abosmasum and be absorbed in the small intestine (about 80% VFA is
absorbed in the rumen wall). After the VFA absorbed by diffusion through the rumen wall
they go to the portal blood circulation then to the liver.

Acetic acid is the major end product of carbohydrate digestion, in the ruminants. This VFA
pass almost unchanged to the rumen wall to the liver which is little affect by the liver and
goes to the peripheral blood or systemic blood in significant amounts. Acetic acid is used by
a various tissues as a source of energy and synthesis of fatty acids.

Propionic acid passes across the rumen wall where a little is converted to lactate, the
remainder carried to the liver where it is changed into glucose which may be changed to liver
glycogen, or to fatty acids for triglyceride synthesis. The remainder of glucose goes to
systemic blood supply and is carried to various tissues and used as source of energy or fatty
acid synthesis, & for glycogen synthesis. Only a small amount of propionate present in the
peripheral blood supply, which can be used directly for energy production.

Butyric acid (butyrate ) is changed in its passage across the rumen wall or metabolised by
rumen epithelium to - hydroxybutryric acid (BHBA) and passes into the portal blood then to
the liver. The remaining small amount of butyrate that may appear in the portal blood will be
removed entirely by the liver, leaving negligible amount in the arterial blood. BHBA pass
liver to systemic blood and serve as source of energy and for synthesis of fatty acids in
various tissue notably skeletal muscle.

Factors influencing the microbial digestion of fiber.

The utilisation of fibrous feeds, cellulose and hemicellulose materials of fermentation is

dependent upon many influencing factors. Some of which include:

1. One most important influencing factor is the kind and number of micro-organisms found
in the recticulo-rumen, which has effect in rate of fermentation of fiber. This in turn is
under the influence of the character of the food. Example, Addition of easily fermentable

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 carbohydrates, such as starch, cane sugar, molasses to ration of cattle reduces digestibility
of the fiber as bacteria attack soluble carbohydrates preferentially.

The kind and number of microbes are different from one ruminant species to another and
even within species it is possible to find varying numbers and kinds of microbes to utilise the
fiber better.

2. The nature of the feed, this in turn may influence the kind & numbers of micro-organisms
present in the reticulo-rumen. Starch fermenting bacteria or amylolytic bacteria increase
with much soluble carbohydrates and cellulolytic bacteria decreases because of a decline
in pH.

3. Protein content of the feed, this would determine the rate of fermentation which depend
on the number of micro-organisms. Microbes require minimum input of protein to
multiply. If vegetation contains less than 7% CP, the micro-organism number decrease,
they instead they die as they have short life span. This will greatly reduce fiber
degradation.

4. Stage of maturity of plants (degree of lignification), the complex polysacchardes in

mature plants are less digested than they are in young, growing plants. The difference is
mainly to the presence of certain substance notably lignin (cutin also), which are
deposited in the cell wall with age. The degree of lignification affects digestibility of
cellulose & hemicellulose. The lignin is not only indigestible itself, but it also lowers the
digestibility of cellulose & other complex carbohydrates.

Lignin is resistant to attack by anaerobic bacteria, probably because of low oxygen content
and its condensed structure which inhibits hydrolysis. Young pasture containing only 5%
lignin, 80% cellulose may be digested but in older herbages with 10% lignin proportion of
cellulose digested may be less than 60%.

Digestion of protein in the reticulo-rumen

Rumen microbes synthesise a large variety of protein and enzymes from different nitrogen
sources, from proteins of varied nature and amino acid content, and from NPN compounds

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such as amino acids, amines, ammonium salts, nitrates, uric acid, urea, biuret, etc.
Monogastric animals could only utilise true protein but ruminants can also utilise NPN.

Food proteins of plants and animal origin is hydrolysed to polypeptides then to smaller
peptides and amino acids by extracellular microbial proteases. The amino acids are degraded
further by intracellular microbial deaminases to ammonia and organic acids, and CO 2.

The ammonia produced together with small peptides and amino acids is utilised by rumen
micro-organisms to synthesise microbial proteins. 60-90 % daily nitrogen intake of ruminants
is converted to ammonia, which is a preferred or essential source of nitrogen for rumen
microbial protein synthesis. 60-80 % bacterial nitrogen is derived from ammonia, balance
from amino acids or peptides.

NPN sources also readily degraded in the rumen to ammonia then to microbial protein. After
this when the organisms are carried through to the abomasum and small intestine they will be
digested by the proteolytic enzymes of the host and absorbed as amino acids. An important
feature of the formation of microbial protein is that bacteria are capable of synthesising
indispensable and dispensable amino acids, thus rendering their host independent of dietary
supplies of the former.

Ammonia is an important intermediate in microbial degradation and synthesis of protein. If

the diet contains less protein or protein resistant to degradation, concentration of rumen
ammonia will be low (50 mg/l) and the growth of rumen microbes will be slow as a result
breakdown of carbohydrates will be retarded. If protein degradation takes place more rapidly
than synthesis, ammonia will accumulated in the rumen liquor and optimum concentration
will exceed (85 to 300 mg/liter). But it is more realistic to relate it with to fermentable
organic matter since for each kg of OM fermented a constant quantity of nitrogen is taken by
rumen microbes for protein & nucleic acid. When ammonia concentration gets high, the
ammonia which can not be fixed in the rumen is absorbed through the rumen wall and
transferred in the liver to urea. Some of urea recycled back to the rumen via saliva, also
directly through rumen wall but the greater part is excreted in the urine thus wasted. With
most food each kg of OM fermented in the rumen yield approximately 200 g of microbial
protein. Some rapidly fermented feeds (immature forage) yield up to 260 g/kg of OM
digested.

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So when there is a high production of ammonia, it may accumulate in the blood (as liver will
be overtaxed to convert all of it to urea) and is toxic, cause’s ammonia toxicity. So this
should immediately be converted to non toxic compounds by two means.
 By transferring ammonia to amino acids then to microbial proteins.
 Excess absorbed goes to portal blood then to liver where it is converted to urea which is
non toxic as compared ammonia.

If the animal is supplied which excess nitrogen, there will be excess ammonia production
which will be converted to urea is liver and animal has mechanism to remove excess urea by
excreting it in the urine. But under nitrogen deficiency condition excretion of urea is
decreased and quantity returned to rumen as urea exceed that absorbed from the rumen as
much of the ammonia is converted to microbial protein. This means quantity of protein
reaching the intestine may be greater than in the food. In this way ruminants are able to
conserve nitrogen by returning to the rumen urea that otherwise be excreted in urine.

Then ammonia in the rumen is not supplied from proteins, but also a much as 30% of
nitrogen in the ruminant food could be simple organic compounds such as amino acids,
amides, amines or inorganic compounds such as nitrates. Most of these are readily degraded
in the rumen to ammonia.

In practice it is possible to capitalise the ability of rumen microbes to convert NPN to protein,
by adding such NPN compounds to the diet. The substance most commonly employed is
urea. Ammonium salts may also be used.

O
ll
NH2 –C- NH2 + H20 urease 2NH3 + C02
Urea Ammonia

Urea entering to the rumen is rapidly hydrolysed to ammonia by bacterial urease, and
rumen ammonia concentration is liable to rise considerably. For this ammonia to be
efficiently incorporated into microbial protein, two conditions must be met.

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 1. The initial ammonia concentration must be below the optimum (otherwise ammonia
may be lost).
2. Micro-organisms must have a readily available source of energy for protein synthesis.

Feeding practice intended to meet these conditions include mixing urea with other foods to
prolong the period over which it is ingested and deaminated and also to provide energy
sources having rate of fermentation comparable to urea. Such foods should be low in rumen
degradable protein, and high in readily fermentable carbohydrates.

Derivatives of urea have been used for animal feeding with the intention of retarding the
release of ammonia. Biuret resistant to fermentation but less superior than urea has been used.

Another NPN which can be utilised by ruminants is uric acid which is present in high
concentration in poultry exereta. So these are sometimes dried for inclusion in the diet of
ruminants.

60-90% the daily nitrogen intake of ruminants is converted to ammonia in the rumen for
synthesis of microbial protein. The other 10-40 % could directly pass to lower gut without
being fermented in the rumen called bypass protein or undegraded dietary protein (UDP). The
other is rumen degradable protein (RDP). Resistant of protein varies between the protein
sources, as some proteins are resistant to microbial attack but digested in the lower gut by
enzyme of the host. So bypass proteins are proteins that pass without degradation in the
reticulo rumen.

As a consequence of their forgut fermentation, ruminants are provided with two major
sources of proteins.

1. The protein synthesised by the microbes (microbial protein), and

2. The UDP, which escapes microbial digestion in the rumen. Digestion of these two
mixtures of microbial protein & UDP in the abomasum and small intestine supplies the
amino acid for the host animal.

The bypass protein in animal feeding has got practical implication. There is a measure of
protein quality called biological valve (BV). BV is measure of proportion of food protein

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which can be used by the animal for synthesising body tissues and compounds which is
defined as proportion of nitrogen absorbed that is retained by the animal.
BV= N intake - (faecal N-MFN) - (urinary N-EUN)
N intake - (faecal N- MFN)

If you compare BV of microbial protein with plant and animal protein sources, BV of
microbial proteins is about 80%, protein of plant origin generally has less than 80% BV and
proteins of animal origin like fish meal, meat meal has greater than 80% BV. This means
animal origin protein sources are better than microbial proteins. Whatever protein source
supplied to rumen microbes, they will change it to microbial protein.

If supply plants proteins having less than 80% BV, the micro-organisms change it to
microbial protein of 80% BV means upgrade the protein quality. If on the other hand supply
animal proteins like fishmeal (95% BV), it will be changed to 80% BV degrading the quality
of protein. Therefore, there is no need of feeding ruminants will high quality protein as it is a
loss, but use high quality proteins mostly to monogastrices.

Protein supplements are generally the most expensive ingredients in ruminant ration. Thus
there is an interest maximising their utilisation. Post ruminant infusion or supplementation
with good quality protein sources protected from rumen fermentation by some means has
resulted in improved nitrogen retention & animal performance, as rumen microbial protein
synthesis may reduce maximum utilisation of high quality dietary proteins. Therefore making
some quality proteins bypass for lower tract digestion by treatments like mild heat treatment,
chemical such as formaldehyde or tannins is helpful.

Digestion of lipids in the reticulo-rumen

Compared to carbohydrates and proteins, lipid comprise small but non negligible proportion
of ruminants diet with the lipid content of forages ranging up to 3%. In fact in ruminant diets
fat content in excess of 2-3 % of feed DM are inhibitory to microbial activity in the rumen.
Lipids for ruminant animals are basically three types

 Galactolipid, found in grasses and clovers which form major dietary fat of ruminants.

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 Triglycerides, most abundant in seeds of plants important when animals are fed
concentrates.
 Phospholipids, feeds like soybean has high amount of phospholipids.

The galactolipids will be hydrolysed by bacterial lipases into free fatty acids, glycerol and
galactose. Triglycerides into free fatty acid and glycerol. Phospholipids are hydrolysed into
fatty acids and glycerol with phosphate attached. After this secondary type of reaction takes
places. Galactose is a monosaccharide, so will be converted to VFA (acetic, propionic,
butyric). Glycerol is a three carbon compound (trihydroxy alcohol), so it will be changed to
propionic acid not to acetic (C2) and butyric (C4) compounds.
Glycerophosphus choline +2FA Lecithiase

The principal fatty acids in lipids fed to ruminants via plants include linoleic, linolenic and
oleic acids. Once they are released from ester combinations the unsaturated fatty acids
(linolic & linolenic) are rapidly hydrogenated by microbial enzymes that can affix ‘spare’
atoms of hydrogen to the carbon chain of unsaturated fatty acids, first to monoenoic fatty
acids and the to form their saturated analog stearic acid, as the intraruminal environment is a
highly reduced one containing lot of free floating hydrogen. Therefore, in the recticulo-
rumen lipid digestion results in the formation of two basic end products, saturated fatty acids
and VFA. Unlike the short chain VFA, long chain fatty acids are not absorbed directly
through the rumen wall rather goes down to the lower tract being attached with feed particles
or associated protozoa or bacteria. This will enter small intestine where it is digested by
enzyme of host and absorbed. Eventually ruminants use this for energy, synthesis of its own
fat depots or for milk fat synthesis.

The hydrogenation of fatty acids in ruminants explain why a large proportion of the fatty
acids in tissue fat from ruminants or the milk fat of ruminants is saturated. For non ruminants
it is possible to vary the fatty acid composition of body fats by altering dietary fats. Not for
ruminants unless they are provided with rumen protected fats.

Bacteria and protozoa are also capable of synthesising a number of odd chain fatty acids from
propionic acid (C3) and branched chain fatty acids from the carbon skeleton of the amino
acids valine, leucine, & isoleucine which are also incorporated in milk and body fat of
ruminants contributing to the characteristic composition of ruminants tissue lipids.

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The capacity of the rumen microbes to digest lipids is strictly limited. Although gross energy
content of fats is higher than any other component of the diet, unfortunately large amounts of
fatty acids in the rumen can have series effect on the ability of microbes to breakdown other
components of the diet. Saturated fatty acids affect rumen fermentation less than do the
unsaturated once.

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 CHAPTER 6
METABOLISM
Source and fates of major metabolites

Metabolism is a general term given to the sequence of chemical processes that take placed in
the living organism. These reactions continue as far as the living body exists. These processes
can be categorised into three

1. Anabolism; describes the metabolic processes in which complex compounds are

synthesised from simpler substances.
2. Catabolism; describes metabolic processes that involve the degradation or breaking down
of complex compounds to simpler molecules.
3. Waste product transformation; as a result of the above two metabolic processes, waste
products arise which has to be chemically transformed and ultimately excreted. The
reactions necessary for such transformation form the general part of metabolism.
Example, when protein is catabolized, ammonia is liberated which can not be excreted as
it is. It has to be transformed into urea which is categorised as 3rd type of metabolism.

As a result of various metabolic processes energy is made available for any mechanical work
and for chemical work such as the synthesis of carbohydrates, proteins and lipids.

The starting point of metabolism is the substances produced by food digestion. End products
of carbohydrate digestion in simple stomach animals are monosaccharides mainly glucose,
fructose, and galactose. For all practical purpose we regard end product of carbohydrate
digestion in monogastrics as glucose, with very small galactose and fructose. This is absorbed
into the portal blood and carried to the liver.

In ruminant animals, the major part of carbohydrate is broken down in the rumen to acetic,
propionic and butyric acids, together with small amounts of branched chain and higher
volatile acids. Butyric acid is changed in to - hydroxybutyric acid (BHBA) in its passage
across the rumen wall and passes into the portal blood as BHBA. Acetic acid & BHBA pass
from the liver via the systemic blood to various organs & tissues where they are used as
sources of energy and fatty acids.

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Propionic acid is converted into glucose in the liver and joins the liver glucose pool. This
may be converted partly into glycogen and stored, or to fatty acids, reduced coenzymes and
L- glyceerol-3-phosphate and used for triacylgycerol synthesis. The remainder of glucose
enter the systemic blood supply and is carried to various body tissues where it may be used as
an energy source, as a source of coenzyme for fatty acid synthesis and for glycogen synthesis.

Digestion of proteins results in the production of amino acids and small peptides which are
absorbed via the intestinal villi into the portal blood and are carried to the liver where they
join the amino acid pool. They may then be used for protein synthesis in situ or may pass into
the systemic blood where they join the amino acid produced and as a result of tissue
catabolism in providing the raw material for the synthesis of proteins and other biologically
important nitrogenous compounds.

Amino acids in excess of the above requirement are carried to the liver and broken down to
ammonia and keto acids. The keto acid may be used for amino acid synthesis or as energy
source via the carbohydrate metabolism. Some of the ammonia may be used in ammination
but practically all of it is converted into urea and either excreted in the urine or recycled in
saliva.

In ruminants a considerable amount of ammonia may be absorbed from the rumen into the
portal blood, transformed into urea by the liver then excreted or recycled via the saliva or
rumen wall. In the case of birds ammonia is transformed into uric acid for excretion.

Most of dietary lipids enter the lacteal as chylomicrons which enter the venous blood vessels
via the thoracic duct. The chylomicrons are about 500 nm in diameter with a thin lipoprotein
complex. A very small proportion of dietary triacylglycerols may be hydrolysed to glycerol
and low molecular weight acids in the digestive tract and these are absorbed directly into the
portal blood supply.

Circulating chilomicrons are absorbed by the liver and the triacyglycerols hydrolysed. The
fatty acids so produced, along with free fatty acids absorbed from the blood by the liver, may
be catabolized for energy production or used for the synthesis of triacylglycerols. This then
re-enter the blood supply in the form of lipoproteins and are carried to various organs and

152
tissues where they may be used for lipid synthesis, energy production, and for fatty acid
synthesis.

Except in the case of the liver, hydrolysis is a prerequisite for absorption. Fatty acids
catabolized in excess of the liver’s requirement for energy are changed to - hydroxybutyrate
and acetoacetate which are transported to various tissues and used as a source of energy.

Different tissues may very in their ability to metabolise certain metabolites. Liver due to the
enzyme glucokinase, it metabolises most of the substrate, especially if you take the
carbohydrate metabolism, this is the main organ carbohydrate metabolism takes place. Brain
relies only on glucose with in the blood as an energy source, if no glucose brain can
metabolise other forms of carbohydrates. This difference can be due to the presence and
absence of certain enzymes which accounts for the biochemical variations in tissues.

For the metabolic condition to be undertaken efficiently certain criteria are necessary, or there
are two phenomena to be fulfilled for efficient and normal metabolic process to occur.
1. Products of certain reactions must be made available at the right time and in sufficient
amounts for other reactions to take place.
2. Energy required for the reaction to take place must be made available at the proper time,
place and in the required form.

Proper time, means at the time metabolic process taking place; place, the cell the metabolic
process taking place, and energy form, certain reactions give off energy others require
energy. For such kind of reactions energy releasing compounds like ATP must be there.

Generally during metabolism a lot of energy is liberated. If this process is not controlled or if
the diet directly changed into energy, the cell will be destroyed. Therefore, metabolism of
nutrients has got control mechanism to prevent such kind of distraction. These control
mechanisms are:

I. Organ level
A. Hormones, the release of certain hormones result to certain reactions to occur and vise
versa, which is therefore, one of the control mechanisms.

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B. Circulating levels of nutrients or waste products, if we take liver for example, when
glucose level is high in the blood, it starts to transfer the excess glucose into glycogen and
store it.

II. Cellular level

A. Selective permeability, here the cell permits only certain substrates while undertaking
different metabolic processes. Specially this phenomena works with minerals.

B. Suppression or induction of enzymes, in this phenomena certain substrates suppress or

induce certain reactions.

C. Feedback inhibition, here when too much of certain substrates more than enough
accumulates in cells, it in turn send feedback or inhibit the following reaction.

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 Energy metabolism or Bioenergetics

Bioenergetics or biochemical thermodynamics is the study of energy changes accompanying

biochemical reactions. These reactions, as occurring in every cell are accompanied by an
exchange of energy in the system. Bioenergetics is the study of change of energy and how
energy is used in the animal body.

The term energy causes from two Greek words en means in and ergan meaning work or
active. Therefore, energy is defined as the capacity to do work. The work of the cell is to
contract, to actively transport molecules and ions or to synthesise macromolecules from
simpler once. This amount of energy is provided by the chemical energy stored in the food.
Cells can effectively extract that energy from food, giving up so little waste to their
surroundings which is a miracle of life.

There are various forms of energy; chemical, mechanical, thermal, electrical and radiant, all
of which are inter convertible by suitable means. The radiant energy of the sun is utilised by
green plants to produce complex plant constituents and is stored as chemical energy. These
complex compounds are consumed by animals and bracken down, releasing energy which is
used by the animal for doing mechanical work, for transport, for maintenance of integrity of
cell membrane, for synthesis, and for providing heat under cold conditions.

The chemical reactions taking place in the animal body are accompanied by changes in the
energy of the system. That portion of the energy change, which is available to do work, is
termed as the free energy change, designated as G. When G is negative the reaction is said
to be exergonic reaction and takes place spontaneously, and when G is large & negative, the
reaction proceeds almost to completion.

When G is positive the reaction is termed as endergonic and free energy has to be fed into
the system in order for the reaction to take place. If G is large & positive there is little
tendency for the reaction to take place. These are synthetic process reactions which take in
energy and the energy is obtained from exergonic reactions(catabolic reactions).

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Chemical energy is energy possessed by chemical compounds in every cell. It is the most
fundamental form of energy in life processes. Every activity of living cell is traceable to
release of chemical energy. Therefore, it can be said that animal body is a chemical engine.
Electrical energy is energy generated due to movement of electrons or nerve impulses.
Mechanical energy is energy directly involved in living matter. Radiant energy is energy that
travels is waves.

When exergonic reactions take place considerable amount of energy is given off which has to
be trapped before carried to other reactions. Therefore before the energy released can be
utilised for synthesis and other vital body process, a link between the two has to be
established. This link is provided by mediating compounds, which take part in both
processes, picking up energy from one and transferring it into the other. The most important
of these mediating compounds by far are compounds containing high energy bonds;
adenosine triphosphate (ATP), adenosine diphosphate (ADP), and adenosine monophosphate
(AMP).

Unless there are such mediating compounds, the amount of energy may affect the cell. These
energy rich compounds trap energy from the exergonic reactions & transfer it to the
endergonic reactions.

Adenosine is formed from purine base adenine and the sugar D- ribose. Phosphorylation of
the carboxyl group at carbon atom 5 of the sugar given AMP. Successive addition of
phosphate residues gives ADP, and then triphosphate ATP. In its reaction with in the cell,
ATP functions as a complex with magnesium.

The addition of the last two phosphate bonds require considerable amount of energy which
may be obtained directly by reaction of AMP or ADP with an energy rich material i.e. AMP
picks up energy from exergonic reactions and change into ADP by gaining energy in
phosphate bond. In the same way ADP get changed to ATP.

These energy rich compounds are formed in two types of reactions.

1. For example in carbohydrate metabolism one of the step is the change of

phosphoenolpyruvate to pyruvate

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Phosphoenolpyruvate + ADP Pyruvate + ATP
CH2 CH3

C:O-P + ADP Mg2+ C:O + ATP

COO- COO-
Phospheonolpyruvate Pyruvate

In this reaction, one molecule of ATP in produced from ADP. This kind of reaction where
ADP gets phosphate bond from the substrate is called substrate level phosphorylation or
when production of ATP from ADP takes place directly from a reaction is called substrate
level phosphorylation.

2. The alternative way is production of ATP indirectly, from inorganic phosphate during the
oxidation of certain compounds like reduced NAD+ and reduced FAD.

ADP + inorganic phosphate (Pi) ATP

Example,
NADH (+H+) + O + 3ADP + 3Pi NAD + + 3ATP + H20
Oxidation of each mole of reduced NAD+ yields 3 moles of ATP
Oxidation of each mole of reduced FAD yields 2 moles of ATP
Such kind of production of ATP from ADP and inorganic phosphate is called oxidative
phosphorylation.

The energy fixed as ATP may be used for doing mechanical work (muscular contraction)
which is provided by the breaking of ATP to ADP and inorganic phosphate. The energy may
also be used to drive reactions during which the terminal phosphate group is donated to a
large variety of acceptor molecules, amongst these is D-glucose

ATP + D- glucose ADP + D-glucose phosphate

In others, such as the 1st stage of fatty acid synthesis ATP provides energy and is broken
down to AMP and Pi.

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Acetate + Coenzymes A + ATP Acetyl coenzyme A + AMP + Pyrophosphate

The role of ATP in trapping and utilising energy may be illustrated diagrammatically.

Fig. Role of ATP in the utilisation of energy.

.
ATP

ADP

AMP

The quantity of energy that is made available by the rupture of each of the two phosphate
groups of ATP varies according to the conditions under which the hydrolysis takes place.
Most authorities agree that under the condition in intact cells, it is about 52 kJ/mole but it will
vary with pH, magnesium ion concentration and the concentrations of ATP, ADP and
phosphate. The phosphate bonds are commonly referred to as high energy bonds, represented
by ~P.

Fixation of energy in the form of ATP is a transitory phenomena and any energy produced in
excess of immediate requirement is stored in more permanent form in such compounds as
phosphocreatine of muscle, which is formed from creatine when ATP is in excess.

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NH3 NH~P

C:NH2+ Creatine C: NH2+

+ ATP
N. CH3 kinase N.CH3 + ADP

CH2 CH2

C00- C00-
Creatine Phosphocreatine (creatine phosphate)

Summary of role of ATP

It prevents the cell from being damaged, by capturing the energy. By doing so it makes the
energy available for useful work or for all metabolic processes of the cell. Therefore, high-
energy phosphate bonds are small package of energy. In ATP the last two phosphate groups
are attached by high energy bonds (~).

When the 1st phosphate group is hydrolysed which is not ~ an energy exchange of -1 t0 -5
kcal/mole occurs. When either of the two terminal phosphates are hydrolysed about -5 to -15
kcal/mole are liberated. These are refereed to as high energy bonds.

For living organisms there are two advantages to have energy stored in high energy
phosphate bonds.

1. The energy in such bonds is readily available to the cell for immediate use. The process
of extracting the energy from a monophosphate bond is a one step reaction.
2. Perhaps most important, the amount of energy in a high energy phosphate bond is
approximately that amount which is the most useful for producing biochemical reactions.
This means that there is less wastage of energy. As a result, biochemical reactions with in
living organisms are quite efficient. They do not release more energy than can be used at
any one time.

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When the supply of ATP is insufficient to meet the demands for energy, more ATP is
produced from phosphocreatine by the reverse reaction. Materials like phosphocreatine are
minor, temporary stores of energy. Most of the energy is stored in the body as depot fat
together with small quantities of carbohydrates in the form of glycogen. Protein may also be
used to provide energy under certain circumstances. In addition to using the stored energy,
the body derives energy directly form nutrients absorbed from the gut. One of the chiefs of
this is glucose.

Eventhough ATP plays major role in energy transformation there are other compounds with
phosphate bonds and having similar role. These include guanosine triphosphate (GTP),
uridine triphosphate (UTP), and cytidine triphosphate (CTP). These energy mediating
compounds are not as active as ATP, though they also trap energy.

Biological oxidation reduction reactions

The biological oxidation reduction reaction is oxidation reduction process which goes with in
the animal body. Fundamentally such reactions are the same whether in living or non-living
system. If the reaction takes place in the laboratory a lot of heat is generated, rather it is
mediated by so called high energy bonds or those energy trapping materials like ATP.
Otherwise the cell can not tolerate the energy given off. The biological oxidation reduction
process is not 100% efficient (not as efficient as the one in the laboratory) in the conservation
of energy, as only part of the energy is conserved in the form of high energy bonds, the rest
being evolved as heat.

Chemotrophs (chemical consuming organisms) derive their energy from the oxidation of food
molecules such as glucose, fatty acids and in many instances amino acids. During oxidation
reaction one of three thing occur or oxidation involves one of the following three things
 Combination with oxygen,
 Removal of hydrogen, or
 Specifically the loss of electrons.
Therefore, during oxidation the substance oxidised losses electron and the substance reduced
picks electron. The ultimate result when oxidation is complete in animal tissues is CO 2 + H20.

160
The transfer of electron in the tissues is not a direct process but effected by special acceptors
or electron carriers. They contain specific vitamins as an integral part of their structure. Three
of the most important electron carries are NAD, NADP, and FAD. All these are nucleotides
(adenine, ribose, phosphate), with nicotinamide central to NAD and NADP and riboflavin
moiety (dimethyl isoalloxazine) centre to FAD.

 Nicotineamide adenine dinucleotide (NAD) accepts a hydrogen ion and two electrons
(formally a hydride ion) to yield the reduced form, NADH.

NAD NADH + (H+) (One of H accepted by NAD and other remain in the solvent)
or
NADH2 (Less accurately written)
 Flavin adenine dinucleotide (FAD) accepts two hydrogen to be reduced.
FAD FADH2

 NADP NADPH2 or NADPH + (H+)

These nucleotides pick electron and get reduced and transfer the electron to other compounds
which is oxidised.

Both reduced NAD and FAD are central to the production of ATP in the oxidative
phosphorylation system. On the other hand reduced NADP is almost exclusively an electron
donor for important reductive biosynthesis e.g. Fatty acid synthesis which occurs throughout
the body.

In addition to this electron carrier compounds, there are other compounds having other
radicals which can pick electron or other compounds that exist which have high energy,
group transfer potential. Whereas ATP carries phosphorous, other carry molecules such as
acyl radicals with sufficient free energy to force reactions to proceed. One of the most
important is coenzyme A (CoA). When combined with acetate as acetyl CoA it has a G
of -7.5 kcal/mol, much as does ATP. Again it is a nucleotide with the vitamin panthothenic
acid at its core. There are also other carrier molecules, which include ATP, NADH, NADPH,
FADH2, CoA, Lipoamide, thiamin pyrophosphate, Biotin, Tetrahydrofolate, Uridine

161
diplosphate glucose, cytidine diphosphate diacylglycreol. Biochemical carriers are stable
unless a specific catalyst is present (enzyme).

Basic units of energy

In contrast to matter which has a mass and space, energy neither occupies space not has
weight. Energy therefore can be measured only by its effect up on matter. The greater the
effect, the greater the amount of energy. Traditionally heat units has been used to represent
the various forms of energy involved in metabolism, since all the forms are convertible into
heat. The basic unit used since last two centuries is the calorie.

A calorie (cal) is the oldest unit of energy and is defined as the amount of heat required to
raise the temperature of 1 gram of water from 14.5 to 15.5 oc at atmospheric pressure. This is
also specific heat of water. Since calorie is small units kilocalorie = 1000 calorie and
megaclorie = 1000000 cal = 1000 kcal has been used. Calorie is used in nutritional and
physiological studies.

Recently it is agreed to use joule as energy unit in nutritional, metabolic and physiological
studies. The joule is defined as 1 Newton per meter. One can convert caloric into joule. The
convention factor is 1 cal = 4.184 J. 1 kilojoule (KJ) = 1000 J, 1 megajoule (MJ) = 1000 KJ.

The amount of energy locked up by the bonds that hold a molecule of feed stuff together can
not be determined by direct means, rather is determined indirectly by an instrument called
bomb calorimeter. In this instrument a known amount of feed will be ignited in the presence
of oxygen which results to the production of heat which will be quantified indirectly by
measuring the rise of water temperature found in an insulated water jacket, by the mercury
level of the attached thermometer. That is why we use carbon as basic energy unit.

All the energy contained in feeds will not be utilised by animals. When we determine energy
with bomb calorimeter we are determining the total energy contained in the feed called gross
energy (GE). This can be sometimes estimated by multiplying the percentages of
carbohydrates, proteins and fats with 4.15, 5.65 and 9.40 calorific values respectively.

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Gross energy = heat of combustion. The GE of a feed provides no clue about the amount of
energy available for livestock production. The amount of digestively energy (DE) is more
useful and it is the portion of feed energy consumed, which is not excreted in the faeces.

DE = GE - Faecal Energy.

The entire DE is not available for productive purposes and there are other energy losses like
in the urine and combustible gasses (primarily as methane 7%). When those losses are
subtracted from DE, the remaining energy is called metabolisable energy (ME).

ME = DE - Urinary energy - CH4 energy (gasses)

Net energy (NE) is the net remainder of the useful energy after all the losses accounted (ME -
heat increment) i.e. faecal + urine + methane + heat increment. This is the part of energy
retained and used by the animals for production proposes. This is ideal method of expressing
the nutritive energy of a feed. This requires respiratory chamber or animal calorimeter to
determine heat increment or NE. These GE, DE, ME, NE are terminology used to describe
energy content of feeds.

Carbohydrate metabolism

Absorbed carbohydrates in the form of glucose, galactose and fructose are metabolised in
three fundamental ways to serve for immediate source of energy, as a precursor of liver and
muscle glycogen, and as a processor of tissue triglycerides. The relative amount used for each
is dependent up on the energy status of the animal and the amount of carbohydrate being
absorbed.

The ultimate fate of the chemical energy bonded in the carbohydrate is for the production of
high energy bonds useful for the work of the body with the concomitant production of CO 2
and H20.

Theoretically oxidation of glucose in bomb calorimeter looks like as follows;

C6H1206 + 602 6CO2 + 6H20 + Heat (2870 kJ).

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But in the living organism glucose is not directly converted to CO 2 and H20 at one step. If it is
converted at one step and all the energy released, the cell will die by the heat load. That is
why nature provides with a gradual process of carbohydrate oxidation.

Glucose is metabolised by a series of metabolic pathways. There are

A. Glycolytic pathway (Embden - Meyerhof pathway) or glycolysis
B. Tricarboxylic acid cycle (TCA cycle ) or kreb’s cycle or citric acid cycle
C. Pentose phosphate pathway, the phosphogluconate oxidative pathway or hexose
phosphate shunt.

The 1st that is glycolysis occur under anaerobic condition and results in the production of
pyruvate (2 molecules of pyruvate from 1 molecule of glucose).

Two moles of ATP are used in the initial phosphorylation of glycolysis at steps 1 and 3
(Endergonic reaction) and all intermediate compounds contain phosphate.

1. Glucose is phosphorylated to form Glucose-6-phosphate (G-6-P).

2. G-6- P is isomerized to Fructose-6-P (F-6-P)
3. F- 6-P is further phosphorylated to F-1,6-P
4. F-1,6-P is split into dihydroxyacetone-P + glyceraldehyde-3-P. From this point
carbohydrate metabolism proceeds from the latter and the former is converted to the latter
as they are interconvertable. In effected from F-1,6-P two moles of glyceraldehyde-3-P is
produced.
5. Glyceraldehyde-3-P is then oxidised to 3- phosphoglyceryl phosphate. The H thus
released is takes up by NAD convert to NADH2 which may be reoxidized in the
mitochondria electron transport system leading to the production of 3 moles of ATP
(oxidative phosphorylation). In the absence of 02 (anaerobic glycolysis) NADH 2 is
utilised in the formation of lactate from pyruvate.
6. 3- phosphoglyceryl phosphate reacts with ADP to form ATP and 3- phosphoglycerate
7. 3-phosphoglycerate is converted to 2- phosphoglycerate essentially migration of the
phosphate group.
8. 2-phosphoglycerate is dehydrated to form phosphoenol pyruvate
9. Phosphoenolypyruvate reacts with ADP to form ATP & pyruvate.

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One molecule of ATP is produced at each step 8 (6) and 11(9). Four moles of ATP are
produced from one moles of glucose. Since two moles of ATP is used, the net production of
ATP from ADP is two moles per mole of glucose. This is an example of substrate level
phosphorylation.

Under aerobic condition NADH2 produced at step 7 may be oxidised via the oxidative
phosphorylation pathway and three moles of ATP are produced per mole of reduced
coenzyme. Under aerobic condition therefore glycolysis yields eight moles of ATP per mole
of glucose.

When there is 02 shortages (oxygen dept) as in muscular activity pyruvic acid may be used to
oxidise NADH2 forming NAD and lactic acid, in the presence of lactate dehydrogenase.
Lactate (dead end for glucose oxidation) is transported to the liver resynthesis to glycogen
since no enzymatic mechanism in the muscle to do so. In case of oxygen dept we get 2 moles
of ATP from glycolysis as NADH2 is not oxidised or oxygen not available for the oxidation
of reduced NAD+ which must be converted to the oxidised form.

CH3 CH3
Lactate dehydrogenase
C:0 CHOH
NADH (+H+) NAD+
C00- C00-

Pyruvate Lactate
The lactate is eventually carried to highly aerobic tissues like heart & liver which undergo
oxidative breakdown to C02 & H20 with further release of energy or may be reconverted into
glucose. Recent evidence suggests that even in highly aerobic muscle tissue much of the
glucose used for energy is converted to lactate.

Under aerobic condition the pyruvate is oxidised to CO2 and H20 with further release of
energy. The 1st step in this process is the oxidative decarboxylation of pyruvate in the
presence of thiamine diphosphate to acetyl CoA which enter TCA cycle (Not pathway).

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CH3 CO2

C:0 + HS. CoA Pyruvate dehydrogenase CH3

C00- NAD+ NADH2 C0S.CoA

Pyruvate Coenzyme A Acetyl- coenzyme A

The acetyl CoA is then oxidised by TCA cycle. In a quantitative sense, this cycle is the most
important phase in the oxidation of foodstuffs, since approximately 90% of the energy
released from food is a result of TCA cycle oxidation.

Although metabolites may enter the cycle at any point, the cycle is usually visualised as
beginning with the condensation of acetyl CoA with oxaloacetate to form citrate. Proteins
(glutamine) can enter at - ketogluterate, acetyl CoA. Fats enter at acetyl CoA and
carbohydrates at acetyl CoA or succinyl CoA.

Steps

1. Formation of acetyl CoA. NAD+ NADH2

2. Condensation of oxaloacetate and acetyl CoA to form citrate
3. Isomerization of citrate to isocitrate
4. Dehydrogenation of isocitrate to form oxalsuccinate. NAD NADH2
5. Decarboxylation of oxalosuccinate to form -ketoglutarate.
Oxidative decarboxylation of - ketoglutarate to form succinyl CoA, (NAD NADH2)
(4 carbon chain) then to succinate GDP GTP
7. Dehydrogentaion of succinate to form fumerate FAD FADH2
8. Addition of H20 to fumerate to form malate
9. Dehydrogenation of malate to form oxaloacetate
NAD NADH2 and oxalacetate is available to condense another mole of acetyl CoA
and thus to repeat the cycle.

166
During oxidisation
Of reduced NAD 3 moles of ATP is formed
FAD 2 moles of ATP is formed
GTP to GDP 1 moles of ATP is formed

TCA cycle involves four dehydrogenation, three of which are linked to NAD+ and one to
FAD and results in 11 moles of ATP being formed from ADP. In addition one mole of ATP
arises directly with the change of succinyl coenzyme A to succinate. The oxidation of each
mole of pyruvate thus yields 15 moles of ATP.
_______________________________________________________________

Step moles ATP formed

Pyruvic acid Acetyl CoA 3
Isocitrate Oxalosuccinate 3
 Ketoglutarate Succinyl CoA 3
Succinyl CoA Succinate 1
Succinate Fumerate 2
Malate Oxaloacetate 3
Total ATP per mole pyruvate 15
Total from two moles of pyruvate (glucose) 30____________

The total ATP production from the oxidation of one mole of glucose aerobically is then
ATP
1 mole of glucose to 2 mole of pyruvate 8
2 mole of pyruvate to C02 +H20 30

Total per mole of glucose 38

ATP consumed in the process during glycolysis is 2.

When glucose is completely oxidised

Glucose + 602 6CO2 + 6H20 + 2870KJ (heat of combustion)

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But with in the animal body it yields 38 moles of ATP. The capture of energy by the
formation of 38 high phosphate bonds is therefore 38 x 52= 1976 KJ/mole of glucose, while
the total energy is 2870 KJ/mole under laboratory condition. The efficiency of free energy
capture by the body is thus:
= 1976 = 0.69 (69%)
2870
such calculations assume perfect coupling of reactions and normal environmental cell
condition(theoretical). If certain reactions are blocked not get such efficiency.

The different cycles are not going on at the same point rather are localised at different points
of the cell. Glycolysis takes place is the cytosol (cytoplasm) of the cell while the
decarboxylation of pyruvate to acetyl CoA and TCA cycle takes place is the mitochondria
matrix under only aerobic condition. Oxidative phosphorylation also takes place with in the
mitochondria. The principle behind for such localisation is not understood but scientists think
that this localisation is to integrate reactions in proper way.

The major way of glucose metabolism is the once mentioned above i.e. glycolysis & TCA
cycle in conjunction with the electron transfer systems (oxidative phosphorylation). Another
pathway by which glucose is metabolised is pentose phosphate pathway or hexose phosphate
shunt or phosphogluconate oxidative pathway (alternate pathway).

This alternate route of oxidation of carbohydrates quantitatively accounts for only a very
small percentage of oxygen taken up by the cell. Indirectly it is not important for ATP
production as such in skeletal muscle. It is however a way of converting glucose to C0 2 and
H20 without going through the TCA cycle. Its most important function is generating NADPH
(+H+) or NADPH2 which is needed to furnish hydrogen for reduction steps when the body
synthesise fatty acids and steroids. Certain tissues like mammary gland, adipose tissues &
liver required with carries like NADPH2 for fat synthesis so useful for such reactions.

The reaction involves the removal of one carbon atom of glucose as CO 2 and production of
two moles of NADPH2 that provide reducing power for the synthesis of FA.

Glucose-6-P + 12 NADP+ 6C02 + P043- + 12 NADPH2

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Unlike reduced NAD reduced NADP do not undergo oxidative phosphorylation to produce
ATP but to provide hydrogen to actively fatty acid synthesising tissues. Reduced NADP+ can
be converted to reduce NAD+ via an energy linked transhydrogenase and thus serve
indirectly as a source of ATP.

The other function of this pathway is the synthesis of 5- carbon sugars ribose, which is
needed by the body to make nucleotides and nucleic acids such as DNA, RNA, ATP, etc.
within this pathway, there exist as number of intermediates e.g. Glyceraldehyde-3-P,
fructose-6-P, fructose-1, 6-diphosphate, all of which could be part of glycolytic pathway.
Thus this reaction can be fitted to production of ribose + NADPH2 with the leftover returned
to glucolytic pathway.

Glycogen as an energy source

When glycogen reserves are depleted because glycogen breaks down or is hydrolysed faster
than glucose units that are added, the process is called glycogenolysis. The release of energy
form glycogen necessitates its break down to glucose which will be then degraded by
pathways mentioned.

Glycogen is broken down in the cells though the action of inorganic phosphate and glycogen
phosphorylase enzymes, which catalyses the rupture of 1,4- glucosidic linkage to glucose-1-
phosphate and a limit dextrin with a terminal 1,6 linked glucose is produced. The 1,6 linkage
groups will be attacked by oligo- 1,6 glucosidase releasing free glucose, and glucose-1-P is
produced by further activity of the phosphorylase. The net effect of glycogen breakdown is
production of Glucose-1-P + little glucose. Glucose-1-P is converted by phosphoglucomutase
to Glucose-6-P

Glucogen Glycogen phosphorylase + pi G-1-P

+
Limit dextrins (1,6 linkage)

Oligo-1,6-glucosidase

G-6-P Phophoglucomutase G-1-P Phosphorylase Glucose

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Glucose-6-P enters glycolysis or pentose phosphate pathways. The production of glucose-6-P
from glycogen does not involve expenditure of ATP except for that used in the conversion of
residue glucose to glucose-6-p. Energy production from glycogen is thus slightly more
efficient than it is from glucose.

The glycogen content of muscle is rapidly used in severe exercise, also liver glycogen.
Several factors initiate the conversion of glycogen to glucose such as physical exercise,
fasting, release of adrenaline, failure of insulin supply and other hormonal activities.

Propionic acid as an energy source

Propionate is an important end product of carbohydrate metabolism in the rumen of

ruminants. The acid then passes across the rumen wall where a little is converted to lactate.
The remainder is carried to the liver where it is changed into glucose. In changing propionate
in the liver the first step is conversion to succinyl-coenzyme A. In this process 3 moles of
ATP is utilised. The succinyl CoA enters the TCA cycle, and is converted to malate and
equivalent of 3 moles of ATP is produced. The malate is transported into the cytosol where it
is converted to oxaloacetate and then phosphoenolpyruvate.
Phsphoenolpyruvate
Malate Malate dehydrogenase Oxaloacetate carboxylase Phosphoenolpyruvate

NAD+ NADH2 ATP ADP + pi

The phosphoenolpyruvate may then be converted to fructose diphosphate by reversal of step

10,9,8,7, and 5 in glycolytic pathway. This then converted to fructose-6-P by
hexosediphosphatase and then to glucose-6-P by the reverse of step 2 and finally to glucose
by glucose-6- phosphatase.

170
The glucose may be used eventually to provide energy and we may prepare an energy
balance sheet as follows.
_________________________________________________________
Moles of ATP
Released Utilised
____________________________________________________________________

2 moles of propionate to 2 moles of succinyl – coenzyme A - 6

2 moles of succinyl CoA to 2 moles of malate 6 -
2 moles of malate to 2 moles of phosphoenolpyruvate 6 2
2 moles of phosphoenolpyruvate to 1 mole of glucose - 8
1 mole of glucose to CO2 and H20 38 -
Total 50 16
Net gain of ATP 34
_____________________________________________________________________
There is thus a net gain of 17 moles of ATP per mole of propionic acid.

Propionate has got also another route. In that all of the propionate may not be removed and
converted to glucose by the liver which may be then found in the peripheral blood. Another
source is from the oxidation of fatty acids with an odd number of carbon atoms found is
ruminants body. Such propionate could be used for direct energy production.

The pathway would be the same as that described as far as phosphoenolpyruvate. This will
then follow the glycolytic pathway via pyruvate, then to acetyl CoA and the TCA cycle. The
balance sheet for this process is;

171
_________________________________________________________
Moles of ATP Released Utilised
___________________________________________________________________

1 mole of propionate to 1 mole of succinyl –CoA - 3

1 mole of succinyl to 1 mole of malate 3 -
1 mole of malate to 1 mole of phosphoenolpyruvate 3 1
1 mole of phosphoenolpyruvate to 1 mole of Acetyl-CoA 4 -
1 mole of acetyl-CoA to CO2 and H20 12 -
Total 22 4

Net gain of ATP 18

_____________________________________________________________________

This pathway is thus marginally more efficient than that via glucose. This is via acetyl CoA.
Actually if conditions allow, the cell utilise nutrients to get the most energy out of it.

Butyric acid as an energy source

Butyrate in the rumen is converted to - hydroxybutyrate (D-3-hydroxybutyrate) in its

passage across the ruminal or omasal walls. There is a sequence of reaction for this
conversion but is accompanied with a net energy of zero (5 moles utilised & 5 produced).

The - hydroxybutyrate may then be used as source of energy by a number of tissues notably
skeletal and heart muscle. The reaction involves the conversion of 1 mole of -
hydroxybutyrate to two moles of acetyl CoA. The acetyl CoA is metabolised via the TCA
cycle. The energy release from butyrate by synthetase pathway is;

172
_________________________________________________________
Moles of ATP Released Utilised
____________________________________________________________________

1mole of butyrate to 1 mole of - hydroxybutyrate 5 5

1mole of - hydroxybutyrate to 2 mole of acetyl- CoA 3 2
2 mole of Acetyl- CoA to CO2 and H20 24 -
Total 32 7

Net gain of ATP per mole of butyric acid 25

_____________________________________________________________________

If the change of acetoacetate to acetoacetyl-CoA takes place via the succinyl CoA pathway,
there is a saving of two moles of ATP and the net gain per mole of butyrate is equivalent to
27 high energy phosphate bonds.

Acetic acid as an energy source

Acetate is the major product of carbohydrate digestion in ruminants and the only VFA
present in peripheral blood in significant amount. It is used by a wide variety of tissues as a
source of energy. The 1st reaction in this case is the conversion of acetate to acetyl-CoA.
Acetate + Coenzyme A Acetyl – CoA synthetase Acetyl–coenzyme A + H20

ATP AMP+ppi

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The acetyl- CoA is then oxidised by TCA cycle. Therefore energy balance sheet is;

_________________________________________________________
Moles of ATP Released Utilised
____________________________________________________________________

1mole acetate to 1 mole acetyl –CoA - 2

1 mole of acetyl –CoA to CO2 and H20 12 -
Total 12 2

Net gain of ATP from 1 mole of acetate 10 mole

_____________________________________________________________________
Two high energy phosphate bonds are used in the initial synthetase mediated reaction.

Carbohydrate synthesis

In trying to build, all the materials and sources has to be available and take time but to
demolish it is not problematic as construction. The same principle also works with in the
body. To synthesise a metabolite, the source material has to go a series of reaction.

Glucose synthesis (Gluconeogenesis)

Glucose is usually considered to be the main fuel. This is certainly true in non-ruminants, and
even in the ruminant where other metabolites may substitute: glucose still holds a central
position and is vital for certain key functions such as brain metabolism (otherwise metabolic
disorder called ketosis results), nourishment of the foetus, & meet requirement for lactation, it
serves as source of synthesis of two important carbohydrates milk sugar or lactose and
glycogen, and synthesis of triglycerides in adipose tissue.

In non-ruminants glucose is major end product of carbohydrate digestion. This simplifies

energy metabolism as glucose is absorbed directly and go to liver and various tissues of the
body to be used as source of glycogen, depot fat and as source of energy. In ruminants the
situation is entirely different as they absorb very little glucose from GIT, as most
carbohydrates will be fermented to VFA. Out of the VFA, propionate is capable of being

174
converted into glucose in the liver. It is the most important precursor of glucose contributing
as much as 30-54% of the total body glucose. The acid after absorption through the rumen
wall is taken up to the liver for conversion. A small proportion of propionate is changed to
lactate in the rumen wall, which also latter on converted into glucose in the liver.

The metabolic route begins with conversion to propionyl- CoA and carboxylation to
methylmalonly-CoA followed by rearrangement of carbon skeleton to succinyl-CoA that
enter CTA cycle in form of succinic acid and in a few step it is converted to another
important intermediate, oxaloacetate.

Oxaloacetate not change to pyruvate since pyruvate not change to phosphoenolpruvate but
oxaloacetate changes to phosphoenolpyruvate for the reverse reaction. Oxaloacetate may go
to TCA cycle or to form glycogenic non specific amino acids like aspartate, glutamate or
alanine by reduction amination.

Propionate produces 50% of the glucose requirements while glucogenic amino acids
contribute another 25% and lactate 15%. The glycogenic amino acids may be derived from
digestion of microbial protein or catabolism of body proteins. Alanine and the
glutamine/glutamic acid couplet are said to be the most important amino acids.

Glucose in the blood may also come from liver glycogenolysis. The last source is from body
fat in adipose tissues which during lipolysis to glycerol and free fatty acids, both get
transported to the liver where glycerol is converted to glucose.

Glycogen synthesis (glycogenesis)

Glycogen is a complex polysaccharides made up of a condensed glucose units. The formation

of glycogen occurs practically in every tissue of the body, but chiefly in the liver and muscle.
Glycogen has the ability to add on further glucose units when these are available in the body.

The actual source material for glycogen formation is uridine diphospahte glucose (UDPG)
which can be produced from variety of source

175
Galactose Appropriate enzymes & Steps
Glucose
Fructose UDPG
Mannose
ATP ADP UTP UDP

Galactose Galactose –1-P UDP-galactose

UDP glucose 4 epimerase

ATP ADP UTP UDP

Glucose Glucose-6-P Glucose-1-P UDP- Glucose

ATP ADP

Fructose Fructose-6-P
ATP ADP

Manose Mannose-6-P

Figure. Formation of UDP-Glucose (UDPG)

Glycogen is produced by the reaction of UDPG with primer molecules, the most active of
which is gluycogen itself. Molecules with as few as four glucose residues may serve as
primers but the reaction rate is slow. As the complexity of the primer increases, so too the
reaction rate. The synthesis involves the reaction of UDPG with the fourth hydroxyl group of
the non-reducing end of the primer chain in the presence of an enzyme glycogen synthetase.
The reaction occurs between the 1st & 4th Carbon atom of adjacent glucose moieties.

UDP- glucose + (Glucose)n Glycogen synthetase (Glucose) n+1 + UDP

The 1,6 linkage responsible for the branching with in the glycogen molecule are formed by
transfer of the terminal oligosaccharide fragment of six or seven glucose residues from the

176
end of the glycogen chain to a 6-hydroxyl group in a glucose residue in the interior of the
chain. This takes place in the presence of branching enzyme, or more correctly, amylo - (1,4-
1,6) transglycosylase.

Lactose synthesis

Milk sugar (lactose) is synthesised in mammary gland of lactating animals. It is formed by a

condensation of one glucose and one galactose molecule. Glucose is readily available, but the
galactose has to be synthesised, virtually in its entirety form glucose, which involves a
configuration change at carbon atom 4. The glucose is 1 st converted to glucose-6-P, glucose-
1-P and then UDP- glucose from which UDP-galactose is produced by the action of UDP
glucose-4- epimerase.

ATP ADP Phosphoglucomutase

D-Glucose Glucose-6-P Glucose-1-P
Hexokinase Glucose-1-P uridyl
transferase
UDP-Glucose-4-epimerase
UDP-D- galactose UDP –D- Glucose

Lactose is then formed by the action of UDP- galactose with glucose

Lactose synthetase
UDP- galactose + D- glucose UDP + Lactose

In such reaction the major compound to initiate the reaction is UTP (converted to UDP).
Therefore energy in the form of UDP or UTP is required

Fat metabolism

The fat that is used for energy production can be of from 3 sources.
1. Fat absorbed from the gut
2. Fat mobilised from the body store, and
3. Fatty acid synthesised from carbohydrates and proteins.

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Fat catabolism (fat as an energy source)

The triglycerides are utilised as source of energy by the action of lipases which catalyse the
production of glycerol and fatty acids. The two products are broken down in 2 different ways
for the release of energy.

The glycerol is glycogenic so enter the glycolytic pathway as dihydroxyacetone phosphate.

Glycerol kinase Dehydrognase
Glycerol Glycerol-3-Phophate Dihydroxyactone
Phosphate

By reverse
Acetyl CoA Pyruvate Glyceraldehyde-3-Phosphate reaction of
TCA cycle Glycolysis

CO2 + H2O Glucose

Glycolysis
+ TCA cycle

CO2 + H20
If glucose is used to produce energy, efficiency of glycerol as source of energy with be as
follows:
_________________________________________________________
Moles of ATP
Released Utilised
____________________________________________________________________

2 moles of glycerol to 2 moles of dihyroxyaceton phosphate 6 2

2 moles of Dihydroxyacetone phosphate to 1 moles of glucose - -
1 mole of glucose to C02 and H20 38 -
Total 44 2
Net yield of ATP per mole of glycerol 21
_____________________________________________________________________

178
On the other hand if dihydroxyacetone phosphates go to glycolytic and TCA cycle and
changed to CO2 and H20, efficiency of glycerol as an energy source will be as follows.
_________________________________________________________
Moles of ATP Release Utilised
___________________________________________________________________

1 mole of glycerol to 1 mole of dihydroxyaceton phosphate 3 1

1 mole of dihydroxy aceton phosphate to 1 mole of pyruvate 5 -
1 mole of pyruvate to CO2 and H20 15 -
Total 23 1
Net yield of ATP from 1 mole of glycerol 22
_____________________________________________________________________

The major part of energy derived from fat is provided by the fatty acids. The pathway for
degradation is the - oxidation, which is the splitting of 2 carbon atom at a time to form
acetyl-CoA or progressive shortening of the carbon chain by two carbon atoms at a time. The
acetyl-CoA will enter the TCA cycle for the release of energy. Therefore, fat catabolism to
CO2 + H20 occurs by means of the sequential combination of - oxidation cycle and TCA
cycle.

The 1st stage of - oxidation is the reaction of the fatty acid with CoA in the presence of ATP
( AMP) and an enzyme fatty acyl-CoA ligase to give an acyl-CoA. This occurs in the
cytosol. The fatty acyl-CoA is the transferred to mitochondria which then undergoes a series
of reactions to give as acyl-CoA with 2 less carbon atom than the original and a mole of
acetyl-CoA.

When acetyl-CoA split 5 moles of ATP is released. The remaining acetyl-CoA undergoes the
same reaction and the process continues until the chain has been completely converted to
acetyl-CoA which enters TCA cycle and changed to CO2 and H20 with the release of 12
moles of ATP.

179
Since the initial ligase reaction is only necessary once for each molecule, more ATP is
produced for the same expenditure of energy, by the oxidation of long rather than short chain
fatty acids. Example moles of ATP produced from palmitate is shown below;

_________________________________________________________
Moles of ATP Released Utilised
____________________________________________________________________

1mole of palmitate to palmitoyl CoA - 2

1 mole of palmitoyl CoA to 8 moles Acetyl CoA 35 -
8mole of acetyl CoA to Co2 and H20 96 -
Total 131 2
Net gain of ATP per mole of palmitate 129
_____________________________________________________________________

Fat synthesis

Fat (triglycerides) of the depot fats are derived from glycerides in the blood from end product
of digestion, or may be synthesized in the body from fatty acids and glycerol.

Fatty acid synthesis

There are three systems of fatty acid synthesis:

1. The one centered in the cytosol and results in the production of palmitate from acetyl-
CoA. This is the most active one.
2. Elongation of fatty acid chains by two carbon addition, with malonyl CoA as donor,
found in endoplasmic reticulum and mitochondria.
3. Desaturation of the preformed fatty acids which occur in the endoplasmic reticulum.

Some literatures devide the above three steps as two

1. Cytoplamic system
2. Mitochondria system of fatty acid synthesis. This requires ATP, reduced NAD and
NADP and involves incorporation of acetyl CoA into long & medium chain fatty acids.

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Cytosolic synthesis of palmitate

In nonruminants acetyl CoA is synthesized from amino acids, fatty acids and carbohydrates
in the mitochondria which has to be transported to the cytoplasm. The mitochondria
membrane is impervious to acetyl-CoA which has to be complexed with carnitine or changed
to citrate. Regeneration of acetyl-CoA then takes place.

Citrate + CoA ATP-citrate layse Acetyl – CoA + Oxaloacetate

ATP ADP

In the ruminant acetate is directly absorbed from the gut and is changed to acetyl-CoA in the
presence of acetyl-CoA synthetase and be a source of acetyl-CoA for fat synthesis.

The cytoplasmic system is active in liver, kidney, brain, lungs, mammary gland and adipose
tissue. The system requires reduced NADP+, ATP, CO 2 and manganese ion. The 1st step is
the transformation of acetyl-CoA to malonyl-CoA.

CH3 COOH
+ ATP + H20 + C02 Acetyl-CoA carboxylase
CoS.CoA Mn 2+ CH2 + ADP +Pi

CoS. CoA
Acetyl –CoA Malonyl- CoA

 The malonyl-CoA then reacts with acyl-carrier protein (ACP) in the presence of malonyl-
CoA-ACP transacylase to give the malonyl- ACP complex. All intermediates of fatty acid
synthesis appear to be protein bound to ACP.
 Acety-CoA is also coupled with ACP in the presence of acetyl-CoA-ACP transacylase to
form acetyl-ACP complex. Acetyl-ACP combines with malonyl-ACP to form Aceto
acetyl-ACP complex.
 Successive reaction of acetyl-ACP & malonyl-ACP will give rise to the chain length
being increased by 2 carbon atoms to give butyryl-ACP complex.

181
 The butyryl-ACP complex then reacts with another malonyl-ACP complex resulting in
further elongation of the chain by 2 carbon atoms to caproyl-ACP. Chain elongation will
take place by successive reactions of the fattyacyl-ACP complexes with malonyl-CoA
until palmitoyl-CoA complex is produced, when it ceases. Plamitic acid is produced by
the action of deacylase (transaylation). The overall reaction looks like;

CH3. Cos. CoA COOH (CH2). CoS. CoA

Acetyl – CoA + 7 Malonyl – CoA + 14 NADPH (+H+)

CH3 (CH2) 14C00- + 7C02 + 14NADP+ + 8HS. CoA

Palmitate Coenzyme A.
This above system mainly produces palmitic acid.

Chain elongation

This system requires ATP (change to AMP) and 2 moles of reduced NADP and is some
literatures reduced NAD. It involves the incorporation of two carbon units (requires malonyl-
CoA) into medium and long chain fatty acids. The products of the system which is centred in
the microsomes are saturated acids with 18,20,22,24 carbon atoms produced from palmitic
acid. A mitochondria system for elongation of fatty acid chains does exist but is active only
under anaerobic conditions.

Desaturation of preformed fatty acids

Double bonds may be introduced into fatty acid chains by the action of fattyacyl-CoA
desaturases present in the microsomes. Thus palmitoleic and oliec acids are produced from
the corresponding saturated acids by a 9 desatures system which introduces a double bond
between carbon atom 9 and 10.

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 02 H20
CH3. (CH2) 6 CH2 CH2 (CH2) 6 C00- CH2(CH2) 6CH:CH(CH2) 6C00-

Palmitate NADH2 NAD+ Palmitoleate

02 H20
CH3 (CH2) 7. CH2, Ch2 (CH2) 7 C00 - CH3(CH2) 7CH: CH (CH2) 7CO0-

NADH2 NAD+
Stearate Oleate

Mammalian cells also contain 6 and 5 desaturases but do not have systems capable of
introducing double bonds beyond carbon atom 9. As a result it is not possible for mammalian
tissues to synthesis either linoleic (18:2 9, 12) or - linolenic acid (18:3 9,12,15). These have to
be provided in the diet and are referred as essential fatty acid.

Glycerol synthesis (synthesis of glycerol-3-P)

The usual precursor is dihydroxyacetone phosphate produced during glycolysis of glucose.

CH20H CH20H
Glycerol-3- phosphate dehydrogenase
C:0 CH0H

CH20 ~P NADH+H+ NAD CH20~P

Dihydroxyacetone phosphate L-glycerol –3 phosphate

Free glycerol absorbed from the gut or as a result of hydrolysis of triglycerides can be also
changed to glycerol-3-P in the presence of glycerol kinase with the expenditure of a high
energy bond as ATP.

Synthesis of triacylglycerols

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The biosynthesis of triglycerides involves the reaction of L-glycerol-3 phosphate with two
molecules of activated fatty acids in the form of fatty acyl-CoA to phosphatidic acid which
will then hydrolysed to give D--- diglyceride. The diglyceride will react with the third
fatty acyl-CoA to result to triglyceride.

Protein metabolism

Amino acids as sources of energy

Amino acids are not utilised as source of energy unless there is energy shortage and amino
acids are in excess. When amino acids are available in excess of the animals requirement or
when the animals is forced to catabolize body tissues to maintain essential body processes,
amino acids may be broken down to provide energy.

Amino acid degradation takes place in all animal tissues but mainly in the liver, the kidney
shown considerable activity also. Muscular tissue is relatively inactive.

The first stage in the oxidative degradation of amino acids is the removal of the amino group
by one or other two main pathways.
1. Oxidative deamination
2. Transamination i.e. inter conversion of keto and amino group

In the 1st case the amino group from amino acid breaks down leaving keto acid. The amino
group will be free to be eliminated or recycled. In the 2 nd case the amino group will be moved
to another keto acid to synthesise another amino acid and keto acid used as source of energy
so synthesis and breaking go side by side.

The ammonia produced will be exerted in case of deamination and the carbon skeleton is
used as a source of energy as they are nothing more than a carbohydrate eligible to enter TCA
cycle.

The pathways of degradation in which ammonia is removed and carbon skeleton is produced
are complex for many of the amino acids. All amino acids which do not enter in form of

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acetyl-CoA or acetoacetate that have the potential of being converted to glucose are called
glucogenic helpful for gluconeogenesis. Those entering at acetyl-CoA or acetoacetate provide
ketones and called ketogenic (example, leucine & lysine are obligatory ketogenic).

Transamination reaction are catalysed by enzymes know as aminotransferases. The most

important transaminase involves glutamic acid and - ketoglutaric acids, but aspartic-
oxaloacetic transaminase is also a significant one. The reaction promotes the following
events:

1. Excess amino acids (essential or dispensable) can be relieved off their ammonia (to
glutamic) and keto acid used for energy (TCA cycle)
2. Dispensable amino acids can be synthesised from glutamic acid and TCA cycle
intermediates.

Some important transaminase reactions is the reaction between aspartate and - ketoglutarate
in the presence of aspartate amino transferase to yield oxaloacetate and glutamate. Alanine
and - ketoglutarate also reacts to yield pyruvate and glutamate.

The glutamate so formed plus the one become available from the gut; i.e. from protein
breakdown may undergo oxidative deamination (cytosol & mitochondria) in the presence of
glutamate dehydrogenase and yields - ketoglutarate + NH4+.

The - ketoglutarate may then be used in further tansamination or enter TCA cycle.
Glutamate is the only amino acid in the mammalian tissue which undergoes oxidative
deamination at an appreciable rate. It is also a universal donor of an amino group to keto
acids. The initial transmaination which gives rise to it is therefore of major importance when
amino acids are being used as source of energy.

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Energy production from deamination of glutamate

_________________________________________________________
Moles of ATP Released Utilised
____________________________________________________________________
Deamination of glutamate to -ketoglutarate + NH3 3 -
1mole of - ketoglutarate to oxalacetate 9 -
1 mole of oxalate to phosphoenol pyruvate - 1
1mole of phosphoenolpyruvate to C02 +H20 16 -
Total 28 1
Net 27
Oxalacetate also enter TCA cycle and yield 15 moles of ATP
__________________________________________________________________

In the case of deamination the ammonia produced must be changed to urea to be eliminated
which requires an energy cost of 4 ATP. This energy must be accounted in calculating energy
production.

The final product of amino acid degradation is acetyl-CoA which enter TCA cycle for energy
production. The acetyl- CoA may be produced directly as in the case of (tryptophan, leucine,
isoleucine), via pyruvate (alanine, glycine, serine, threonine, & cysteine) or via acetoacetyl-
CoA (phenylalanine, tyrosine, leucine, lysine and tryptoplan). Other amino acids are
degraded by pathways of varying complexity to give products such as -ketoglucarate,
oxaloacetate, fumarate and succinyl CoA which enter TCA cycle and yield aceyl-CoA via
phosphoenol pyruvate.

During amino acid catabolism ammonia is produced and is toxic. Some of this may be used
in ammination process (reverse of deamination or used for amino acid synthesis). In this case
ammonia reacts with - ketoglutarate to give glutamate, which is then used for the synthesis.
The reaction is the reverse of oxidative deamination except that NADP+ takes the place of
NAD+. Most of the ammonia is however excreted from the body as urea in mammals, and
uric acid in birds.

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Deamination of amino acids occur in all the organs of the body. The ammonia conversion to
urea involves two stages, both required an energy supply in the form of ATP.

1. The formation of carbamoyl phosphate from CO2 and ammonia in the presence of
cabamoyl phosphate synthetase.
O
C02 + NH4+ + H20 carbamoyl phosphate synthetase NH2 –C.0P
2ATP 2ADP + 2 pi

The carbamoyl phosphate then reacts with ornithine to start a cycle of reaction to produce
urea.

Aspartate is produced by reaction of glutamate with oxaloacetate. oxaloacetate is produced

from fumerate produced in production of arginine form arginosuccinate.
Fumerate enter the TCA cycle and changed to malate then to oxaloacetate. We then have a
second associated cycle linking the urea and TCA cycle.

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Amino acid synthesis in the body

The dispensable amino acids can be synthesised in the animal body when they are in short
supply in the diet.

List of some of the precursors and dispensable amino acids from which they are synthesised.
____________________________________________________________________
Amino acid Precursors Process
____________________________________________________________________
1. Glutamate -keto glutamate + NH4+ Amination
2. Glutamine Glutamate + NH4+ Amination
3. Alanine Glutamate + Pyruvate Transamination
4. Aspartate Glutamate + Oxalacetate Transamination
5. Serine Glutamate + 3- phosphohydroxy
pyruvate (3- phosphoglycerate) Transamination
or alanine or glysine +
3-phosphohydroxy pyruvate Transamination

6. Proline Glutamate - H20 Dehydration

7. Hydroxy proline Proline Hydroxylation of
proline
8. Aspargine Aspaaratate + NH4+ Amination
9. Glycine C02+NH4+ Amination
10. Arginine Keto acid + urea or ammonium
salts From urea cycle
11. Tyrosine Phenylalanine Hydroxylation
12. Cysteine Methionine + Serine Combination
____________________________________________________________________

The last two take essential Amino acids as precursors. The importance of glutamic acid in
this synthesis is obvious, being involved in the synthesis of the first 6 amino acids.

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Protein synthesis

Three things can happen to the amino acids absorbed from the gut,
1. It can be used for protein synthesis
2. It can be utilised in the synthesis of hormones and enzymes
3. It can be deaminated or transaminated so that the carbon skeleton is used as a source of
energy.

To synthesise protein all the amino acids required must be there in the needed amount and
right time. These amino acids can come from the diet or synthetic process in the body or from
tissue catabolism. If not get the amino acid from the 3 sources there will not be a protein
synthesis.

The amino acid absorbed from the gut into the blood stream are transported into cell. This
requires a supply of energy since the concentration of amino acids in the cell may be up to
100 times more than that in the blood and transfer into the cell has to take place against a
very considerable concentration gradient. A continues exchange takes place between the
blood and cellular amino acids but not between the free amino acids and those of the tissue
proteins. The tissue proteins themselves undergo breakdown and resynthesis, their stability
varying with different tissues. Thus liver proteins has a half-life of seven days where as
collagen is so stable as to be considered almost completely inert.

Protein synthesis with in the animal body requires nucleic acids, the most important once are
DNA and RNA. DNA is important as
 Carrier of genetic material
 It has also inherited information necessary to synthesise all the protein required by the
cell.
 DNA also serves as the template for the synthesis of three RNAs (Ribosomal RNA
(rRNA), messages RNA (mRNA), and transfer RNA (tRNA)).

DNA contains sugar deoxyribose, 4 nitrogen bases one attached to each sugar group, and
phosphate (PO4). The nitrogen bases are cytosine, thymine, adenine or guanine. DNA
consists of a double strand spiral or helix, each strand consisting of alternate unit of the

189
deoxyribose and phosphate groups. Thiamine is paired with adenine (T-A) and cytosine is
paired with guanine (C-G).
The sequence of bases along the DNA strand carries the genetic information of the living cell
and affect the kind of protein to be synthesised, since DNA is blue print for mRNA.

With regard to RNA, they are of three types:

1. ribosomal RNA- rRNA
This constitutes over 2/3rds of the mass of the ribosomes, and is the site of polypeptide
synthesis in the cytoplasm.
2. transfer RNA-tRNA
This is the smallest RNA, which carries the activated amino acid to the site of protein
synthesis.
3. Messenger RNA- mRNA
This take the blue print arrangement or sequence of amino acid is transcripts on mRNA.

RNA differs from DNA in nature of their sugar moiety and also type of nitrogenous base
present. They contain sugar ribose and RNA contain the pyrimidine uracil in place of thiamin
(couplet formation is U-A, C-G). Unlike DNA, most RNA also exists in the form of a single
folded chain arranged spirally.

The process of protein synthesis can be divided into 4 stages.

1. Activation of individual amino acids
2. Initiation of peptide chain formation
3. Chain elongation &
4. Chain termination

1. Activation
The 1st step in protein synthesis is enzymatic and requires the presence of ATP to give
complex as follows:
Amino acid + ATP+ Enzyme Amino synthetase Amino–acyl -AMP-Enzyme +
Pyrophosphate
The amino- acyl group is then coupled to a molecule of tRNA
Amino–acyle-AMP-Enzyme + tRNA amino–acyle-tRNA + AMP +
Enzyme

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There are at least one tRNA for each amino acid but only one amino acid for a given tRNA.
There are 64 tRNA 3 for termination. The difference in different tRNA is in the arrangement
of interior of the molecule which consists of a sequence of three bases, the nature and
arrangement of which are specific for a particular amino acid.

When amino acid has been coupled with tRNA, it is carried to one of the site of protein
synthesis, the ribosome. After transcription mRNA moves to the ribosome, originally
transmitted from nuclear DNA. It is composed of a sequential series of 3 bases (at a point
having a specific arrangement of 3 bases) called a codon (a base triplet code). The tRNA
carrying the specific amino acid for a particular codon will have a complementary
arrangement of 3 bases called anti-codon. When the two paired identifies the sequence of
amino acid to be placed on the polypeptide chain.

There are 64 possible base triplet combinations and 61 of these have been shown to code for
20 amino acids involved in protein synthesis. There is thus more that one codon per amino
acid and the code is said to be degenerate. However, any one codon codes for one amino acid
only and so also degenerate the code is not ambiguous.

Example of known codons on mRNA

_________________________________
Codon Amino acid
_________________________________
UUU Phenylaanie
UUA Leucine
UUC Serine
UCA Serine
CCC Proline
CGA Arginine
AGC Serine
AGA Arginine
_________________________________
U- Uracil, C-Cytosine, A- Adenine, G- Guanine

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Initiation of peptide chain formation

The 1st tRNA codes for is for methonine and is placed at AUG codon. The peptide linkage is
formed is a process called translation. tRNA bring the 1 st amino acid to the ribosomes and
attach it to mRNA and when the 2 nd comes peptide bond is initiated or formed. The bond
formation or chain elongation continues until the chain is complete. tRNA is released to be
used again.

Termination

Chain elongation continues until a codon is reached which does not code for any amino acid
like UAA, UAG, or UGA. It then ceases and the formed peptide chain is liberated by
hydrolysis and the methionine residue removed enzymatically.

The polypeptide is the primary structure. The chain then becomes arranged in a secondary
spiral form stabilised by hydrogen bonding. The tertiary structures involves extensive coiling
and folding of the chain and is stabilised by hydrogen bonding, salt linkage and sulphur
bridges. The quaternary structure involves polymerisation of these basic units.

For protein synthesis to take place all the amino acids required must be available at the right
time and place. Otherwise the rest amino acids may be catabolized and wasted if incomplete
mixture is present. During protein synthesis energy is required (8-10p/ per mole of amino
acid in the form of ATP and UTP.

The manufacture of protein is the principal synthetic activity of the cell. Despite high rate of
synthesis, the deposition of protein is not that much. In fact the major focus of protein
synthesis is not the deposition of new tissues but the replacement of the old tissue proteins,
hormones and enzymes. The arrangement of amino acids in a protein chain determine the
characteristic of the protein.

192
 Interrelationships between carbohydrates, protein and fat metabolism

The metabolism of these major nutrients are interrelated. If you feed a liberal amount of
carbohydrates the animal become fattened. This indicates the case of conversion of
carbohydrates into fat. The most important reaction here is production of aceyl-CoA as it is
starting material for fat acid synthesis. But conversion of long chain fatty acids to
carbohydrates is not there, since acetyl-CoA is not converted to pyruvate. But terminal 3
carbon of a fatty acid having an odd no of carbon atom is glycogenic and also glycerol. But it
is possible to get carbon of fatty acids to glycogen up on the reversal reaction of TCA cycle
through oxaloacetete and phosphoenol pyruvate.

Many of the carbon skeleton of dispensable amino acids can be produced from carbon
skeleton of carbohydrates via the citric acid cycle, while the amino group comes from
transamination reaction. Glycogenic amino acids which yield glucose and glycogen can serve
for fatty acid synthesis. The ketogenic amino acids can yield acetate and to acetyl-CoA which
can be used for fat synthesis except in animals receiving a high protein diet. ACP proteins are
important in fat synthesis.

The consistence of these nutrients as complex compounds like lipoprotiens (in cell
membrane, egg yolk, lipid transport), glycoprotiens (glucosamine, cartilage, skin) is also
important. The presence of proteins as enzymes, hormones are important in metabolic
process. The energy release from carbohydrates, fats or proteins can serve for synthetic
purposes of any nutrients.

Generally the metabolism of the 3 major nutrients is interrelated and is important for the
normal functioning of the animal body.

193
 CHAPTER 7
SPECIAL FEATURES OF METABOLISM IN RUMINANTS

The special feature of metabolism in ruminants lies in the presence of micro-organisms in the
reticulo-rumen. These microbes through their enzymes can break down complex
polysaccharides to simple sugars, in the process utilise the energy source to build their body
tissues and VFA (acetic, propionic & butyric acids) will be released. Therefore, the
difference between monogastrics and ruminant animals are due to the presence of a high rate
of fermentation in the reticulo-rumen, ruminants can synthesis of all members of the vitamin
B complex and of vitamin K, and essential amino acids by rumen micro-organisms.

With the exception of equines where there is high microbial fermentation (large intestine),
there is slight fermentation in monogastrics. But since fermentation is ruminant is very high,
we mention it as a difference with monogastrics. But there is small fermentation process in
absolute terms in monogastrics.

The presence of micro-organisms in the rumen is one of the differences between ruminants
and monogastrics. The rumen microbes include bacteria, protozoa and some fungi. Bacteria
9over 60 species) are present in largest number. The protozoa (35 species) are present in
much smaller number but being larger may equal to the bacteria in total mass. The fungi are
relatively small and may even absent. Though fungi play role in digestion, their contribution
to the fermentation of food has not yet been quantified.

The higher number of different species of bacteria and protozoa results to the production of
varied types of proteins containing dispensable and non dispensable amino acids. This
diversified species of microbes result to diversified protein type and amino acid content.

The substrates the microbes utilise and products of fermentation are variable between
microbes. There are actually interactions between microbes in the rumen in that end product
of one, e.g. succinic acid produced by gram -ve rods will be converted to another product
propionate by selenomonas ruminantium. The other point is that the activities of a given
species of bacteria may vary form one strain of that species to another.

194
The total number of bacteria and relative concentration of individual species vary with the
animal diet. A normal rumen flora (bacteria) and fauna (protozoa) is established quite early in
life (6 weeks of age calves). The rumen protozoa population have proved to be more
susceptible to modification than the bacterial population, principally because protozoa can be
totally eliminated from the rumen. Ruminants reared from birth in isolation from other
ruminants do not develop a protozoa population. The presence of protozoa in the rumen is
both advantageous and disadvantageous. The advantages are:

 Their contribution to digestion of polysaccharides

 Have valuable role in aiding the absorption of the minerals calcium, magnesium, and
phosphorus form the gut.

Protozoa however has undesirable effect of locking up microbial protein in the rumen and
preventing its passage to the small intestine. So defaunation although decreases digestion of
polysaccharides it increases the quantity of microbial protein reaching the duodenum by
about 25%. In this case protozoa put the animal at the disadvantage.

The current view of rumen protozoa is that with low-protein forage based diets their presence
is detrimental to the host, and defaunation can therefore increase animal productivity. With
concentrate-based diets, better supplied with protein, the presence of protozoa is beneficial.
Ironically it is difficult to keep ruminants free of protozoa when they are on a forage diet, and
difficult to maintain protozoa on a concentrate diet.

Carbohydrate metabolism in the reticulo-rumen

As you well remember carbohydrate break down or metabolised in the rumen takes place in
two stages.
1. Digestion of complex carbohydrates to simple sugars by extra cellular enzymes of micro-
organisms in the rumen.
2. The simple sugars produced in the 1 st stage will be taken up by the microbes and are
change to VFA mainly to acetate, butyrate and propionate. The change of pyruvate to
different VFA are taking place in different series of reactions. The 2 nd stage is similar to
what is happening in metabolism of carbohydrates in the animal itself. The VFA are the

195
 major source of energy for the animal. The microbes are digesting the feed by their
enzymes for their own benefit and the host animal get benefited form the by-product.

In this fermentation process gasses mainly methane, C0 2, and H2 are produced. C02 is
produced partly as a by product of fermentation and partly by the action of organic acids with
the bicarbonate present in the saliva. CH 4 is formed by the reaction of C0 2 and H2 is
methanognic bacteria. Part of the methane can be derived from format through CO 2 and H2.
The gases are then lost by eructation.
The fates of VFAs are already discussed.

Protein metabolism in the reticulo rumen

The nitrogenous compounds contained in the feed will be either protein or NPN. All these
nitrogen sources will be change in the rumen to ammonia, which would be utilised in
microbial protein synthesis in the rumen. The rate of proteolysis is closely related to the
solubility of the protein in the rumen fluids, rumen p H, composition of micro-organisms,
chemical structure, concentration of VFA & free amino acids.

In spite of a strong protealytic activity in the rumen, the amino acid concentration in the
rumen fluid is very low because of the presence of microbial deaminases, the activity of
which increases with increasing protein content of the diet. The carbon skeleton is changed to
branched VFA and mostly used as source of energy or fat synthesis and not for amino acid
synthesis even if it is absorbed.

The ammonia with some amino acids and peptides are used for the synthesis of microbial
protein. Considerable protein is utilised by the rumen microbes for their rapid proliferation.
During this build up process the microbes utilise preferentially ammonia and fix it as
excellent body proteins composing of essential and non-essential amino acids, in the presence
of soluble carbohydrates, particularly starch. When the micro-organism number increases in
billions, they are carried to the abomasum and are absorbed as units of amino acids mostly in
the region of the small intestine.

The output of microbial protein from the rumen is a function of the amount of N and the
energy available for microbial growth and the anaerobic nature of the ruminant fermentation.

196
With most feeds each kg of organic matter digested in the rumen yields approximately
200gram of microbial proteins. Some rapidly fermented foods rich in soluble carbohydrates
yield more microbial protein. Conversely food that are not easily fermented in the rumen
(even if have high digestible nutrients) give a lower yield of microbial protein.

Excess ammonia produced is directly absorbed through the rumen wall and goes to the liver
where it is changed to urea. Most of it will be excreted and some recycled through rumen
wall or saliva and as source of ammonia for microbial protein synthesis. The rate of
absorption is dependent on rumen pH, as ammonia is being absorbed much more rapidly in
the unionised form. Lowering the pH of the rumen due to carbohydrate fermentation would
thus decrease ammonia absorption. This could particularly account for the increased N
retention found when carbohydrates are fed with a N source which is readily converted to
ruminal ammonia.

If has been estimated that up to 60-90% of the daily N intake by the ruminant is converted
into ammonia and 60-80% of the synthesis is achieved when the concentration of ammonia in
rumen is 8.5 - 12.0 mg/100ml. Raising rumen ammonia above this level will result to loss of
N and also exert an undue pressure on liver and kidney for the exit of the excess gas in the
form of urea.

Production and utilisation of rumen ammonia is dependent on the availability of energy to

rumen microbes. Carbohydrates provide carbon skeleton and energy as ATP for rumen
microbial protein synthesis. When carbohydrates are available the ATP production from
carbohydrate utilising species increase and a larger fraction of amino acids and ammonia can
be incorporated into protein. An improvement in the utilisation of ammonia can be achieved
when animals are fed readily fermentable carbohydrates.

Under most dietary regimens approximately 2/3 rd of the protein reaching the small intestine
has been synthesised in the rumen which will be digested by the host enzyme and serve as
source of amino acid. The amino acid content of the microbial protein do not vary
appreciably with most diets. Undegradable protein in the rumen (UDP) is therefore the
principal component that affects the profile of amino acids reaching the duodenum.

197
The rate and extent of ruminant proteolysis therefore not only affects microbial protein
synthesis but also the quantity and quality of UDP that reaches the duodenum. Both UDP and
microbial protein serves as source of protein for the host.

The rate of growth of microbes in the rumen is always greater than the rate at which microbes
flow from the rumen to abomasum. This is because

 Protozoa are retained and only a small proportion moves down the tract. These retained
apparently lyse in the rumen and are fermented.
 Protozoa by their predatory action engulf and digest quite a high proportion of bacterial
pool.
 Bacteria and protozoa spontaneously lyse because of such things like action of infective
ages, lack of substrate, and change in environmental conditions as decrease in rumen pH.
The net effect of this interaction is a continuos recycling of nitrogen within the rumen.

Sulphur like nitrogen is an essential element for microbial protein synthesis as it is needed to
microbial sulphur containing amino acids. Recommended sulphur/nitrogen ratio has been
found to be 1:10 in urea based diets. High concentration of ammonia in the rumen does not
stop normal bacterial growth, it is only the excess amount of free ammonia which is absorbed
through the rumen wall and most of this gets lost as urea through urine.

Protein supplements are generally the most expensive ingredients in ruminants rations, thus
there is an interest in maximising their utilisation. The rumen microbes has a levelling effect
on the protein supply of the ruminants which has a deleterious effect on quality protein rich
concentrates by converting it to microbial protein. This loss in protein quality can by
protected by protection of the diet from being attacked in the rumen by the microbes.
Therefore suitable processing of high protein concentrates may improve their usefulness to
the animal. The implications of this result are that somehow the synthesis of protein by the
rumen microbes is ineffective and/or inefficient.

There are different methods of protein protection from ruminal degradation.

1. Heat treatment
2. Chemical treatment
3. Feeding proteins in liquid suspension

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4. Feeding encapsulated proteins or amino acids
5. Post ruminal infusion
These all decrease rumen microbial attack and thus increase the amount of by-pass protein
which will be digested in the small intestine.

1. Heat treatment; when proteins are treated with heat it become resistant to microbial attack
& by pass rumen fermentation and available to the small intestine enzymes. But if the
heat is over the protein may be denatured so be careful on the application of the heat.

2. Chemicals like formaldehyde and tannins are used, the former being used more often.
This treatment modifies the structure of proteins in such a way as to impede microbial
attack but still permit digestion by mammalian digestive enzymes. But there are
difficulties in achieving precisely the right degree of protection.

3. The 3rd one is to feed the proteins in liquid suspension by doing so the rate of passage will
increase their by limiting the microbial attack on the proteins which then will be available
in the lower tract. As it is in liquid form it will not stay long in rumen.

4. The 4th one is preparing the protein by encapsulating it with some synthetic material. So
protein with in the capsule pass undegraded in the rumen and digested in the small
intestine.

A more practical way of getting the protein pass the rumen degradation to use foods to which
microbes are unaccustomed and therefore unadapted. These are principally feeds of animal
origin such as fish meal.

Control of rumen fermentation is not only important for protecting protein but also to protect
soluble carbohydrates. In intensive fed ruminants energy rich supplements which naturally
escapes rumen fermentation is provided and i.e. the triglyceride fat.

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 Lipid metabolism in the reticulo-rumen

Compared to carbohydrates and proteins, lipids comprise a small proportion of the ruminant
diet. In fact high fat in ruminant diet are inhibitory to microbial activity in the rumen. The
fermentation of fibre is reduced and food intake fall as result of low rate of digesta flow.

The digestion and saturation of fats in rumen, presence of branched chain and odd number
carbon atoms, the depot fat which is not similar to dietary fat, differentiate ruminant from
non-ruminant for fat metabolism. This is due to rumen digestion or microbial modification of
dietary lipids.

Besides hydrolysis and hydrogenation of plant lipids, microbial activity in the rumen leads to
biosynthesis de novo of long chain fatty acids and complex lipids, using as substrate the
short-chain fatty acids produced as end-products of microbial carbohydrate and amino acid
metabolism.

In the rumen most of the lipids are present in association with feed particles, others may be
associated with bacterial and protozoa fractions. This reaction product pass out the rumen and
fatty acids & some structural lipids of micro-organisms enter the small intestine where they
are digested by the enzymes of the host and become available for absorption.

The principal fatty acid in lipids fed to ruminants are linoliec, linolenic and oleic acids.
Considerable hydrogenation of unsaturated acids takes place in the rumen with a consequent
overall reduction in the available essential fatty acids (EFA). Despite this the possibility of
ruminants suffering from EFA deficiency is remote since they are able to conserve their
dietary supply efficiently. There are reasons for this

1. For young ruminants which are born with very little linoleic acid in its tissue, maternal
origin is major source but some may be available as a result of microbial synthesis in the
undeveloped rumen.

2. Animals with functioning rumen meet their requirement firstly from digestion as
microbial lipid composition of mixed rumen bacteria 30% is phospholipids while the rest

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 70% contain free fatty acids mainly linoleic and linolenic. There is evidence that rumen
bacteria takes up linoleic acid from rumen and incorporate it into their cell membrane.

3. Ruminants are able to utilise EFA much more efficiently than non-ruminants through
selective retention of this substance in their essential role which represent species
metabolic adaptation by incorporating into cholesterol esters and phospholipids, but only
partial in non-ruminants.

4. Even after rumen hydrogenation, the digestion of these diets contain linoleic acid
equivalent to about 0.8% of gross energy intake escape rumen (rumen by pass) to satisfy
the animal requirements.
As a result no EFA deficiency in adult ruminants or young animals with a functioning rumen
is encountered.

Two main functions of EFA has been postulated

1. As Precursor of prostaglandin, and
2. They are widely distributed in phospholipids and cholesterol esters which intern
constitute a significant part of all cell membrane and lipid transport moieties.

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 CHAPTER 8
METABOLIC DISORDERS IN RUMINANTS

When one considers the major non-infectious dysfunction or diseases that affect domestic
ruminants most of them are related to sudden changes in the diet, production or environment,
that is an induced stress. Many of these diseases are more prevalent in animals with a high
production potential.

Some of the diseases are related to excessive production, others to improper nutritional
management and many to combination of the two factors. These factors result to metabolise
disorders (dysfunction) and disease. There are actually three terminologies.

1. Metabolic diseases are disease either due to excess or deficiently of metabolic catalysts
(enzyme). Not commonly encountered
2. Production related disease caused by inappropriate management (acute disease).
3. Nutritional deficiency disease is chronic disease due to deficiency of nutrients for longer
time.

The 2nd once come spontaneously but the 3 rd appear slowly and can be treated by
supplementation.

The dysfunction of the rumen affects other organs and disease of other type also will have an
effect on the rumen. Therefore there is a great deal of overlap and no metabolic disease is
restricted to one system.

Bloat (Tympany, Tympanites)

Bloat is a disorder of ruminants and is an excessive accumulation of gases in the rumen,

distending the rumen and reticulum to a dangerous degree. Excess ruminal gas production
(C02, C0, CH4, small amount of others including poisonous H25) which are results of nutrient
fermentation. This will not cause bloat unless there is a failure or inability to eructate the
gases.

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Bloat can be divided into two according to the cause of it. They are 1) frothy bloat (primary
ruminal tympany) and 2) free gas bloat (nonfrothy bloat, secondary ruminal tympany). The 1 st
one is caused when the gas is mixed in the rumen in the form of a very small bubbles, like the
foam that one gets while shaking an emulsion with air, or when the gas trapped in a foam,
due to excessive foaming of ruminal digesta. This is the most common form of bloat. The 2 nd
one is caused due to oesophageal obstruction or any other factor like anatomical alteration in
reticular area, ruminal irritation preventing normal eructation which will result in the
accumulation of free gas in the rumen. Nonfrothy bloat is the least form of bloat encountered.

Frothy bloat is classified into two types

1. Pasture bloat (legume bloat), is seen when legume pasture is grazed. It is very common
on immature, rapidly growing legumes.
2. Feedlot bloat, occur when concentrate rations are fed. High concentrate rations, especially
when finely ground are the major cause of feedlot bloat associated with increased
ruminal acidity. Feedlot bloat can also be free gas bloat as high fermentation decrease pH
and create ruminities or oesophageal inflammation and avoid normal eructation.

Legume bloat may occur when graze either alfalfa or clover. Protein content and rate of
digestion reflect the forage potential to cause bloat. Legumes such as alfalfa and clover have
a higher percentage of protein and fermented more quickly and causes bloat. Legumes with
high protein content but slowly digested do not cause bloat and also grasses as they contain
less proteins.

Theories for occurrence of stable gas bubbles causing frothy bloat include:

 Soluble plant proteins and presence of saponins play a promising role in formation of
stable foam. Saponins are soap like emulsifying agents found is the feed.
 Increased bacterial slime, i.e. muccopolysaccharides capable of forming a stable froth.
 A genetic tendency to bloat. Animals from bloaters tend to produce less saliva than
normal animals. Animals that will bloat on any feed are called chronic bloaters, are
animals unable to belch because of some physiological abnormalities.
 An increase in RNA as a result of distraction of protozoa cell bodies might increase
viscosity and the tendency to bloat.

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A. Factors increasing bloat (ruminal froth) include
1. Dietary factors
 Finely ground feeds
 Plant pectin
 Plant proteins
 Plant saponins

2. Animal factors
 Genetics susceptibility
 Salivary macromolecules

3. Rumen microbial population factors

 Mucinolytic bacteria
 Bacterial slime or mucopolysacchrides
 Protozoal population

B. Factors decreasing bloat (ruminal froth)

1. Quantity of saliva (particularly mucin)
2. Plant tannins and falvolans.

Feedlot bloat occurs when cattle or sheep have been fed high concentrate, low roughage
rations for approximately 60 days or longer. This timing may be due to the increases in the
level of grain feeding or due to the time it takes for rumen slime producing microbes to
proliferate to large enough numbers.

Frothy bloat is acute bloat which can kill the animal in as short as half an hour.

Free gas bloat is which results from physical obstruction of the oesophagus or pharyngeal
passageways. This obstructive could be due to foreign bodies or pressure up on the
oesophagus due to tumours, abscesses, swollen lymph nodes (lympophadenopathy) and
similar enlargements. Free gas bloat can also be caused by interference with oesophageal
groove function which create no movement of compartments and consequently no eructation
of free gasses, and due to lesion of the wall of reticulum that may interrupt the normal reflex
which is essential for escape of the gas from the rumen. Except in the case of complete

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obstruction, this form of bloat arise more gradually and are chronic or intermittent depending
up on the cause.

Chromic ruminal tympany occurs frequently in calves up to months old without apparent
cause and with spontaneous recovery.

Symptoms

1. Distension of the paunch on the left side in form of the hipbone. This is followed by
distension of the right side.
2. Protrusion of the anus
3. Cyanosis (bluish coloration) of the tangue and also its protrusion
4. Respiratory distress as bloating will push the diaphragm forward seriously limiting the
respiratory capacity (dyspenea).
5. Compress the veins of abdominal cavity, obstructing the general circulation.
6. The above mentioned mechanisms result to anoxia (condtion in which there is no enough
oxygen for tissue oxidation) which is the immediate cause of death in those cases which
are fatal.
Post-mortem examination
1. Marked congestion and haemorrhage of lymph nodes, head, neck, epicardium, & upper
respiratory tract.
2. The lungs are compressed and intratracheal haemorrhage may occur.
3. The cervical oesophagus is congested and haemorrhaged while the thoracic oesophagus
pail and blunched, liver also get pail.

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Diagnosis
In free gas bloat, the gas can be expelled by gas tube but for froth bloat it can not be done by
gas tube.

Treatment
 If the life of the animal is compromised one can undergo surgenry may be used as the last
resort. A knife may also be used in emergencies.
 If the life of the animal is not in danger, the other recommended measured is to use a
large stomach tube carefully inserted through the oesophagus to rumen that may expel the
gases. But this is appropriate in free gas boat.
 In frothy bloat the animal should be treated by administrating antifrothing agents like
poloxalene (10 gram per 45 kg body weight). Intraruminal injunction not give food
results. Other antifrothing agents are corn oil, peanut oil, soybean oil, vegetable oil,
paraffin.
 Mild cases may be home treated by keeping the animal on its feet and moving and
drenching above mentioned oils and poloxalenne (bloat guard).

Control
Feeding management is most important in controlling bloat. The incidence is therefore
lessened by;
 Avoiding straight legume pasture and immature legumes.
 Feeding a courser grass hay prior to turning out into lush pasture.
 Feeding dry forage along with pasture.
 Keep salt and water conveniently accessible at all times.
 In case of grazing young pasture probably it is hard to avoid bloat, in this case
antifrothing agents shall be used in the following ways.
 By drenching the animal
 By spraying on the pasture
 By spraying on the animal body so that it can be liked by the animal

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Poloxalene, oxytetracyclin (teremycin), Laureth-23 are antifrothing medicaments. Oils and
fats have been used successfully to control bloat. In feedlot the ration should contain 10-15%
roughage and the grain should not be finely ground.

Acidosis (lactic acidosis )

This is a metabolic disease caused by an increase in lactic acid producing bacterial (D and L
forms). This happen when there is a sudden shift from a high roughage to a high concentrate
ration. The soluble carbohydrates are rapidly fermented to organic acids thereby reducing pH,
and when rumen pH continues to fall lactic acid producing bacteria (lactobacilli)
predominates further reducing pH. This reduces rumen motility and appetite. This acidity also
cause gastro-enteritis causing ulcers. The microbes may also go to other organs and cause
infections, particularly in liver causing liver abscesses. Toxic products like histamine,
alcohol, tyramine, thiaminase may also be produced and absorbed causing cardiac, hepatic,
CNS & renal damages.

The lactic acid produced will be absorbed. Series acidosis may decrease blood pH, which
may increase blood glucose and pyruvate, plasma Mg & Ca levels may decrease. In addition
diarrhoea and dehydration occur due to the gut fluid hypertonicity. In severe cases coma,
death occur.

Treatment
 Removing rumen content and replacing by contents of an animal on a normal ration
(rumenotomy, lavage).
 Feeding a high level of antibiotic to suppress lactic acid producing bacteria.
 Drenching (intravenous injection) with a solution of sodium bicarbonate to restore the
acid base balance.
 Lessening total amount of the ration and returning to a high forage feed.

Control
 Best controlled by avoiding accidental access of animals to high concentrates.
 Changing gradually from low to high concentrates feeds.
 Adding buffer salts such as sodium bicarbonate to the ration.

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Ketosis

It is also called acetonemia in cattle and pregnancy disease in sheep. The clinical signs for the
metabolic disorder are same in both species but in ewes it strikes just before lambing
specially in those carrying twins and triplets, but in cows, they are usually affected with in the
first one - six weeks after calving (peak production).

Under conditions of nutritional and/or physiological stress, where energy demand exceeds the
available tissue glucose, fat is mobilised to acetyl-CoA, because of lack of oxaloacetate (lack
of energy form carbohydrates), it can not be converted to energy via TCA cycle and is
converted to ketones.

2 Acety CoA Aceto acetyl CoA + CoA liver Acetoacetic acid + CoA

Acetoacetic acid extra hepatic tissue 2 Acetyl CoA Co2 +H20

NADH2
-CO2 (spontaneous)
NAD Acetone
-hydroxybutyrateacetone

Since acetoacetate and -hydroxybutyrate are acidic acidosis develops. The ketone appears in
the urine and urine tests can be used to for diagnosis. Acetone is exhaled via the lungs and in
series cases it can be detected by the sweet odor. Other signs of ketosis include anorexia, drop
in milk production in cows, in ewes symptoms like go off feed, grinding of teeth, frequent
urination, dullness, trembling, weakness, collapse & finally death are observed.

Cause
 Important nutritional management (starvation).
 Genetic selection for high milk production resulted to high incidence of lactation ketosis.
 Decrease glucogenic ability such as hepatic dysfunction.
 Uncontrolled diabetes mellitus due to lack of insulin for glucose transport to cells.
 Lack of glycogenic precursors.

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Treatment
 This consists of making some form of glucose available to the tissues, like injection of
glucose, propylene glycol or sodium propionate daily (glucogenic substances, either with
grain or drench).
 Cortisone or ACTH are effective as they mobilise tissue amino acids, some of which can
be converted to glucose.
 Intravenous injection of corticosteroid.

Control
 Proper nutritional management i.e. maintaining an adequate feed intake to ensure
reasonable level of rumen propionate concentration.
 Do not make the animal too fat or obese.

Parakeratosis of the rumen

When rations are fed in highly processed form as pellets, finely ground feeds, morphological
changes can occur in the epithelium of the rumen. The papillae of rumen become keratinized
or hardened. This condition is called parakeratosis. This decreases feed absorption and feed
efficiency.

Treatment
No as it is not easily recognised.

Control
Addition of roughage to the diet & increasing feed particle size.

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Reticulitis

Reticulitis or hardware disease is a condition where foreign objects accumulate and puncture
the reticulum. Ruminants when they graze will consume nails, wires or other foreign objects
which will puncture reticulum and may pierce diaphragm and enter the thoracic cavity then
go to heart or lung where they may cause series damage or death. Sharp objects may injure
the lining of stomach causing infection and inflammation condition called traumatic gastritis.

Symptom
 Loss of appetite
 Digestive disturbance
 Decreased rumen movement

Control
 Avoiding foreign objects.
 Installing storage magnet in feed processing equipment and silo.
 Permanently placing magnets in reticulum to hold objects.
 Surgery is good cure for the disease but has to be done before the condition has
progressed.

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