Fundamentals of Dairy

Chemistry UNIT 10 THERMAL PROCESSING OF MILK

Structure
10.0 Objectives
10.1 Introduction
10.2 Heat Processing of Milk
10.3 Effect of Heat on Milk
10.4 Freeze Processing of Milk
10.5 Enzymes in Relation to Processing
10.6 Let Us Sum Up
10.7 Key Words
10.8 Some Useful Books
10.9 Answers to Check Your Progress

10.0 OBJECTIVES
After reading this unit, we shall be able to:
 name various heating processes used in dairy industry.
 explain effect of heat on milk.
 define freezing of milk.
 enumerate important enzymes and their role in processing of milk

10.1 INTRODUCTION
The main purpose of application of heat is preservation of milk and milk products.
In some cases controlling microbial contamination is the primary criteria. In products
like dried milk main purpose is to preserve the product from chemical deterioration
apart from microbial spoilage. The purpose of heat is to meet public health
requirements such as pasteurization and sterilization, to remove water, to destroy
enzymes, to facilitate mixing and blending processes, such as in ice cream mix,
processed cheese and cultured dairy products and to impart desirable properties
such as development of flavours.

10.2 HEAT PROCESSING OF MILK

There are several processes in which the main purpose of heat application is to
make milk safe for human consumption and increase its keeping quality. Common
process in which heat is applied are as follows:
i) Pasteurization: The main aim of pasteurization of milk is to kill all pathogenic
microoganism and make it safe for human consumption. Pasteurization of milk
is done either by High temperature short time (HTST) or Low temperature
long time (LTLT) process. In Holder process milk is heated for not less than
30 minutes at 630C while in HTST pasteurization heating not less than 71.70C
for 15 seconds is used. Pasteurization of milk is done to meet the public health
requirement. Pasteurization leads to the destruction of pathogenic bacteria, e.g.
Mycobacterium tuberculosis and most of the non-pathogenic organisms and the
enzymes present in milk. Both in Holder and HTST process alkaline phosphatase
activity is taken as an index of destruction of Mycobacterium tuberculosis.
ii) Sterilization: The purpose of heat sterilization is to destroy all micro-organisms
and their spores in milk. Sterilization is primarily employed for the preparation
of sterilized milk. In the preparation of evaporated milk sterilization at temperature
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 of 1160C for 15 minutes is employed. Sterilized milk can be stored at room Thermal Processing of
Milk
temperature for longer period.
ii) Forewarming or Preheating: Forewarming or preheating is applied for the
manufacture of condensed or evaporated milk and dried milk. Temperatures
between 880C to 1000C are employed for forewarning. Present trend is to heat
milk above 1000C to give maximum heat stability.
iv) Condensing: In condensing heating is carried out under vacuum to remove
water. In a single effect vacuum evaporator the temperature ranges between
43 to 550 C. With the widespread use of multiple effect evaporators for
condensing milk, it is not possible to specify precisely the degree of heat
treatment which may be subjected in condensing operation.
v) Drying: The purpose of drying is to completely remove water with minimum
physico-chemical changes in the dried product. The temperature employed in
spray drying process ranges between 71 to 1770C in terms of air inlet
temperatures. The precise temperature conditions vary with the particular drying
equipment.
vi) UHT Process: In the ultra high temperature process for preparing UHT milk,
the milk is heated at a high temperature of 1350C – 1500C with holding time
of few (1 to 8) seconds. This is a microbially safe milk. UHT milk can be
stored at room temperature for further use
vi) Homogenization: Homogenization is carried out to break down the fat globules
into a smaller size, resulting in stable state of dispersion. Though homogenization
can be carried out without heating but heating is generally required for proper
and satisfactory homogenization. Before homogenization heating facilitates
melting of fat and inactivation of the enzyme like lipase. If heating is not done
it leads to the development of hydrolytic rancidity with the liberation of lower
chain fatty acids. Heating destroys lipase and thus prevents lypolysis. Non-
heating and homogenization will result in fast lypolysis by lipase resulting in
rancid flavour by liberation of lower chain fatty acids from the glycerides. It
is desirable to heat the milk before homogenization. Other due to heating and
homogenization there are other physico-chemical changes which occur in milk.
These include easy digestibility of milk, soft curd formation and tasteful products.
However, homogenization results in difficulty in cream separation. Homogenization
is primarily employed in the preparation of flavoured milk, ice cream mix and
evaporated milk.

10.3 EFFECT OF HEAT ON MILK

I) Effect on salt system: The heat-induced changes in the milk salt system can
be covered under three cateogories:
 Readily reversible shift in salt balance by changes in temperature
 Irreversible shift in salt balance.

Variations in temperature and concentration adversely affect salt balance. Calcium

phosphate is less soluble at high temperature than at low temperature. Thus, the
concentration of soluble calcium and phosphate is decreased during heating. Dissolved
or soluble calcium and phosphate during heating is transferred to the colloidal state.
This transfer action occurs on the colloidal micelles of caseinate phosphate. This
transfer of soluble calcium and phosphate causes extensive changes in the structure
of the micelles produced by heat treatment. Dissolved calcium and phosphate tend
to revert to the original system but it is not completely transferred to the original
structure after heat treatment. At the same time aggregation of the caseinate-
phosphate micelles may occur (reversibly or irreversibly).
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Fundamentals of Dairy II) Effect on Acidity: During heat treatment CO2 is removed from the milk
Chemistry
system. This causes a decerase in acidity of milk. The effect is through the
release of H+ions. This process is affected by the insolubilization of calcium
and phosphate.

3Ca ++
+2HPO4- → Ca3 (PO4)2+2 H+

On the basis of available data, heat treatment lead to an increase in the dissolved
citrate in milk.
III) Effect on the milk proteins: The heat-induced changes in milk are of great
practical importance to the dairy industry. During denaturation the original
three-dimensional structure changes. Denaturation consists of non-proteolytic
changes in the structure of protein. Amongst the heat induced changes caused
by denaturation of whey proteins are:
 Development of cooked flavour
 Development of anti-oxygenic properties
 Impairment of clotting properties
 Imparting of soft curd characteristic to milk
 Prevention of age-thicking in evaporated milk
 Improvement in the baking quality for non-fat dry milk in the bakery industry

These changes are related to whey proteins. The whey proteins are present to the
extent of 0.6 to 0.7% in milk. Beta-lactoglobulin is the major whey protein of milk
accounting for 50 percent of the total whey proteins. The observed changes in milk
are: release of H2S production, of cooked flavour, development of anti-oxygenic
properties and lowering of curd tension. All these changes are related to whey
proteins.
a) Heat denaturation of whey proteins: Heat denaturation of whey proteins
occur between 680C to 800C. Heat denaturation starts from 680C onwards
when milk is heated for 30 minutes or 710C for 15 minutes. The denaturation
of whey proteins occurs at a higher temperature than pasteurization. The order
of denaturation of whey proteins are immunoglobulin, blood serum albumin,
beta-lactoglobulin while alpha-lactalbumin is the most heat resistant whey protein.
b) Changes associated with whey protein denaturation: Above 750C –SH
groups are released from whey protein, which are highly reducing in nature.
These groups are susceptible for oxidation. The activation of-SH groups
accompanies by an important phenomenon of anti -oxygenic property of heat-
induced changes in whey protein. Sulphahydryal (-SH) groups are powerful
reducing agent. The ability of these groups to bind oxygen results in anti-
oxygenic property. As a result it lowers the oxidation-reduction potential of
milk, which shows the activation of these groups. Formation and activation of
-SH also results in the liberation of volatile sulphides. These volatiles also
include H2S. The release of H2S is one of the most important component
responsible for cooked flavour of milk. Cysteine amino acid containing maximum
number of -SH group is responsible for producing H2S. Whey proteins are a
rich source of cysteine and are a main cause of cooked flavour. Beta-lactoglobulin
is very rich in -SH group.

Another important change resulting, as a function of heat denaturation of whey

proteins is the soft curd forming property of milk. It is accompanied by two
important changes in curd. These are the development of a soft curd characteristic
in the curd and partial loss of clotting property in cheese manufacture. These are
related to changes in the flocculation of serum protein particles. The impairment of
milk clotting property seems to be due to interaction of casein with whey protein
(beta-lactoglobulin). The denatured whey proteins bind with casein and thus affect
52 its clotting property.
Milk contains a factor, which affect the loaf volume of bread when milk is added Thermal Processing of
Milk
during bread making. As a result volume of bread is depressed and slackens dough
is produced. This defect can be overcome by heating milk. This is supported by the
role of added skim milk powder to dough during bread making, which contain heat
denatured whey proteins. Heat denaturation of whey proteins in skim milk powder
is thus used as an index of baking quality.

There is loss of creaming property and increase in whitening of milk due to denauration
of whey protein. Loss of creaming property has been attributed to the interactions
between whey proteins notably immunoglobulins which interact with proteins of fat
globules. This interaction affect the creaming ability. Cream layer formed in such
milk is shallow and indistinct from normal milk. Reflectance or improvement in
whitening has been attributed to a heat denatured state of milk proteins just before
browning. At this stage flocculation of whey protein occur, along with aggregation
of casein and conversion of soluble calcium to insoluble salt.
c) Destabilization of caseinate system: Caseinate-phosphate particles in milk
exist in a precarious equilibrium with soluble Ca++ and Mg++, dissolved salts and
whey proteins. Slight changes occurring as a result of heating or changes in
ionic environment through pH will alter this equilibrium. Casein binds Ca++ and
Mg++ ions very strongly. Casein is stabilized in the system by charge it carries.
Heating causes pH changes which affect this process. The caseinate particles
are very sensitive to changes in pH. Casein start precipitating below pH 6.0
and micelles precipitation starts at pH 5.2 to 5.3 where they still contain Ca++
and Mg++ attached to them. The manufacture of cottage cheese is based on
the phenomenon of caseinate system by heat and acidity. During this process
the destabilization of the caseinate particles leads to the formations of a smooth
gel occupying the entire volume originally occupied by the milk. In this system
a three-dimensional type network is formed that entraps the liquid along with
gel structure formation or a network and a semi-solid system is formed. On
applying heat to this system at cooking stage of the process, the caseinate
particles become more closely knit together, water is expelled, and the clot
shrinks. A desirable product is obtained by judicious use of pH and proper heat
treatment.

The calcium caseinate phosphate micelles are readily precipitable by addition of

various salts such as ammonium sulphate and urea. Heating hastens the process.
This is the basis of producing various fractions of casein. The effects of heat and
divalent cations are important from the view point of rennet action and heat. In this
phenomenon ionic concentration and heat play an important role in the stability of
casein micelles. Phosphate and citrate ordinarily exert an opposite effect over Ca++
and Mg++ because they form undissociated complexes with Ca++ and Mg++.

Some milk apparently are stabilized by added calcium and destabilized by ions such
as phosphate and citrate that sequester calcium. Observations of this type are the
basis of the well-known salt balance theory first suggested by Sommer and Hart
(1926). This theory holds that optimum stability depends on a certain ratio of
calcium and magnesium ions to those of phosphate and citrate. The concept has
been of great practical utility in developing practical procedures for controlling the
stability of evaporated milk during heat sterilization. In practice evaporated milk to
be sterilized is treated, as a series of samples on a pilot scale with graded level of
phosphate or Ca the later being rarely if ever necessary. The samples are then
sterilized and after cooling the minimum level of added salt that imparted satisfactory
stability is noted and used to stabilize the lot of milk to be sterilized.
IV. Forewarming process and heat stability: Before sterilization in the preparation
of evaporated milk forewarming of milk provides heat stability to milk. Generally,
heating milk at 950C for 10 minutes provide heat stability to milk. It has been
shown that a high temperature short time process of heat treatment provides
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Fundamentals of Dairy a better heat stability. However, it may be stated that this phenomenon of heat
Chemistry
stability is complex and depends upon other factors such as quality of milk,
storage temperature of milk, etc.
V. Browning of milk: Browning reactions in milk and milk products are the
manifestation of heat induced processing of milk. Browning reaction occur due
to changes related with pH, storage conditions, moisture content, relative humidity
and temperature of processing and storage of milk and milk products. Browning
reaction is absent in pasteurized milk but is evident in highly heated sterilized
milk on storage. Browning reaction occurs in two forms on heating. The two
types of browning in relation to heating are (a) amino sugar or Maillard browning
and (b) non-amino browning or caramelization.
a) Amino Sugar or Maillard browning: Two components are responsible
for this browning reaction. They are milk protein particularly casein and
lactose present in milk and milk products. Phosphate salts and whey proteins
make minor contribution in browning reaction. Browning reaction is complex.
The reaction occurs between aldehyde groups (-CHO) of sugars and amino
groups (-NH2) of amino acids. They together start the browning reaction
which ultimately lead to the formation of brown pigment melanoidin.

CHO RNH
l l
H–C–OH + H2N – R D H–C–OH
l l
Sugar Amino Complex ultimately
(Lactose) group of leading to the formation of
with alde- amino acid melanoidin
hyde group of the protein

b) Caramelization or non-amino browning: Caramelization or browning

may be defined as the heat decomposition of sugar as a function of pH and
buffers in the absence of amino compounds. It requires a relatively high
order of heat energy. On the other hand, Maillard type browning requires
a relatively low order of energy for its initiation and exhibit autocatalytic
qualities once it has started. Caramelization is desirable in milk based
products such as caramelized flavour which is desirable and liked.
c) Changes related to browning: Along with browning many complex
reactions also occur with the formation of various compounds. In addition,
fluorescent and reducing substances, various sugar fragments and flavour
compounds are formed. Many of these are detected before browning starts.
These changes have great practical utility. Notable amongst these is the
development of flavour especially caramelized flavour. Following changes
related to browning can occur:
 Compound formation: A large number of lactose degradation
compounds are formed. These include furfuryl alcohol, furfuryl aldehyde,
maltol, acetol, acetaldehyde, acetic, formic and pyruvic acid, NH3, H2S
and CO2
 Reducing substances: Heated and dried milk contain’s a complex
reducing system involving –SH compounds, ascorbic acid and substances
associated with browning reaction. Heating concentrated milk for a
similar period has a significant effect on browning reaction.
d) Factors affecting browning of milk: The principle factors responsible for
browning in milk are:
i) pH: A pH above 6.8 favours browning reaction. This defect is
predominant in evaporated milk where pH of milk plays an important
role. Due to variations in pH and protein concentration in different
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 milks browning is affected due to these variations. This is due to Thermal Processing of
Milk
release of protons during heating. As the pH is raised above pH 6.6
browning reaction occurs at a faster rate.
ii) Storage and temperature: Higher temperature and prolonged storage
period favours browning. These changes are favoured in the presence
of increased humidity and moisture. Colour intensity increases with
storage time and is highest at a storage temperature of 400C.
iii) Total solids concentration: During concentration of milk total solids
concentration increases. As the total solids concentration in milk
increases the browning reaction also gains momentum. Lactose plays
a major part of total solids concentration along with casein. The
interaction results in increased browning.
iv) Heat treatment: Heating milk as a pre-heat treatment between 85-
1000C for 30 minutes or more favours browning. It is one of the most
important factors of browning. Reducing the heating time such as with
HTST process will reduce the browning of milk products.
v) Oxygen: Oxygen favours browning as it reacts with –SH groups
released during heating. Presence of oxygen destroys these reducing
groups. Problem can be reduced by replacing O2 with N2 while storing
heated and dried milk products.
e) Prevention of Browning: Browning can be prevented to a great extent
by storing milk and milk products at low temperatures and short period of
storage. In dried products moisture should be below 5%. Also N2 packing
helps in reducing browning due to replacement of oxygen. Strong and long
duration heating should be avoided.

10.4 FREEZE PROCESSING OF MILK

Freezing has been suggested as a means for tansporting frozen concentrated milk.
This is to co-ordinate supply to those areas, which are not adequately covered to
supply liquid milk. The objective of freezing is to prepare frozen concentrated milk
to replace liquid milk supply to distant areas, which are not well connected.

Freezing of milk and its effect on milk system: To manufacture frozen milk,
the milk is first concentrated and then frozen stored. During frozen storage of milk
and its subsequent thawing very fine milk particles called flocculates are formed.
Initially flocculates are readily dispersible but prolonged storage period makes them
difficult to disperse.

Effect of freezing on lactose and caseinate system: Lactose is the first component
of milk which is affected during frozen storage. Frozen storage results in crystallization
of lactose especially at very low temperatures. Lactose is present in milk in a highly
supersaturated state which readily crystallize on storage. Lactose binds calcium
from milk but calcium is released on crystallization. In the dissolved state lactose
binds calcium but releases calcium upon crystallization. No change in protein
denaturation occurs on storage even though flocculation occurs. The reason for
destabilization is calcium. It has been seen that frozen stored casein remains
unchanged in terms of solubility. Casein isolated from frozen stored milk has the
same sensitivity to calcium precipitation as casein isolated from fresh milk. Although
casein flocculates on frozen storage but protein seems to be unchanged.
Check Your Progress 1
1. Define denaturation of protein. Name some of the major proteins affected by
denaturation.
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Fundamentals of Dairy ....................................................................................................................
Chemistry
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2. What is the reason for development of cooked flavour during heating?
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3. Name the agents of browning reaction.
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4. Discuss the role of ions during heating.
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5. How lactose affect frozen storage of milk?
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10.5 ENZYMES IN RELATION TO PROCESSING

Enzymes are organic catalytst, which are found in plant and animal cells. The
enzymes bring about metabolic reactions but they don’t undergo any chemical
change. They are colloidal and proteinous in nature and are classified as per the
reaction performed e.g., lipase, the fat splitting enzyme. The activity is affected by
pH, heat, light etc. Enzyme in milk gain entry via udder or externally.

Milk enzymes are technologically important. They are related with flavour (e.g.,
lipase). Study and knowledge of these enzymes is essential to understand their
role.
Functions of enzymes
The following functions are related to enzymes.
 Oxidising enzymes (e.g., peroxidase)
 Lipolytic enzyme hydrolyzing fat (e.g., lipase)
 Decomposing H2O2 (e.g., catalase)
 Decomposes phosphorous esters.(e.g., phosphatase)
 Lactose hydrolyzing enzyme (e.g., lactase)
 Reductase as reducing enzyme (e.g., MBR test)
 Proteolytic enzymes hydrolyzing protein (e.g., protease)
 Hydrolysing aldehyde (e.g., xanthine oxidase)
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 Peroxidase, lipase, catalase, reductase, phosphatase, xanthine oxidase, lactase are Thermal Processing of
Milk
all present in freshly drawn milk. Other enzymes enter via bacterial contamination.
i) Peroxidase: Peroxidase is present in milk as lactoperoxidase enzyme. The
enzyme is destroyed between 70-800C. Lactoperoxidase enzyme act on H2O2
in the presence of thiocyanate ions, forming hypothiocyanate ions (OSCN-) are
lethal to microbes. This enzyme has been used in milk to improve shelf life
during transportation of milk from distant places to milk plant. The enzyme is
also used as an index of detecting proper heating of milk as it is destroyed at
700C, especially for detecting high temperature heat treatment of milk.
ii) Phosphatase: Phosphatase catalyse the hydrolysis of phosphate esters. Alkaline
phosphatase is the most important milk enzyme. It is destroyed by pasteurization
of milk. At the temperature of pasteurization of milk tubercle bacili bacteria
present in milk are also destroyed. The inactivation of this enzyme is thus taken
as the process of destruction of TB organisms. Under health consideration
pasteurization of milk is mandatory in various countries. Phosphatase test has
been developed to ascertain if the milk has been properly pasteurized. So as
to ensure the destruction of Micobacterium tuberculosis which is destroyed at
a temperature wherein alkaline phosphatase is inactivated.
iii) Lipases: Lipases hydrolyse milk fat into corresponding fatty acids and glycerol.
In milk they are linked with hydrolytic rancidity of milk fat releasing butyric
acid. Excessive presence of butyric acid in milk causes rancid flavour defect.
This defect may also be present in butter. They are destroyed at 630C when
heated for 20 minutes.
iv) Proteases: Proteins are hydrolysed by proteases to simple compounds such as
proteose, peptone, amino acid and other compounds. They are inactivated in the
presence of salt or preservative. Proteases are destroyed by heating milk
between 70-800C. Proteolytic enzymes have been employed externally for
preparing different varieties of cheese. These enzymes primarily hydrolyze
⎯⎯ ⎯⎯→ casein.
Catalase
v) Reductase: Reductase are enzymes of bacterial origin. These enzymes are
capable of reducing certain dyes to their colourless leuco-compounds. It has
been shown that generally speaking the reduction time at 380 C is approximately
proportional to the number of bacteria.. They are used as measure of microbial
population and determine the extent of contamination of milk by bacteria. This
is possible through methylene blue reduction test (MBRT). The blue dye is
reduced to a colourless compound in the presence of reductase. The earlier the
dye lost its blue colour greater is the contamination.
vi) Catalase: Catalase catalyses the decomposes hydrogen peroxide as per the
following reaction

2H 2O 2 2H 2O+O2
Catalase content varies in milk from different animals and within the same
species. It is also affected by feed given to the animal. Catalase content is high
in colostrum, mastitis milk and milk contaminated with mastitis or colostrum
milk or bacterial contamination. It tends to parallel leucocyte count. It increases
with multiplication of bacteria in milk. It is destroyed when milk is heated to
about 650C or over.
vii) Xanthine oxidase: A variety of substances are oxidized by this enzyme including
xanthine, hypoxanthine, aldehyde, oxypurines, etc. Thus in the presence of O2
and an aldehyde following reaction takes place:
Xanthine oxidase
RCHO +H2O+O2 ⎯⎯ ⎯ ⎯ ⎯ ⎯⎯→ RCOOH+H2O2
Xanthine oxidase is a prominent enzyme of milk and was discovered as early
as 1902.
57
Fundamentals of Dairy Xanthine oxidase content varies from cow to cow and increases with stage of
Chemistry
lactation. It is associated with fat globules. It can be isolated from cream or
buttermilk. The following table gives the data for inactivation of the enzymes
in milk.

Table 10.1: Inactivation temperature of enzymes

S.No. Enzymes Inactivation temperature (0C)

1. Lipase 800C (weakend at 600C)
2 Peroxidase 720C (for 30 minutes)
3 Reductase Above 800C
4 Catalase 65 to 700C(for 30 minutes)
5 Phosphatase 62.50C (for 20 minutes)
6 Lactase 75 to 800C

Check Your Progress 2

1. What are enzymes?
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2. Name some of the enzymes present in milk.
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3. Name the enzyme responsible for hydrolytic rancidity and cause for rancid
flavour.
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10.6 LET US SUM UP

Thermal processing of milk is an important aspect. The milk industry will come to
a standstill if heat is not applied. This is because milk is a highly perishable
commodity. Also heat is necessary to evaporate water to prepare dried milk and
related products. Preservation of milk and milk products is the primary objective of
heat.

Heat treatment consists of several processes such as pasteurization, sterilization,

forewarming, condensing, drying and UHT processing. Heat treatment causes
changes in milk in terms of denaturation of proteins including whey proteins, altering
of salt balance, browning reaction, caramelization, development of flavour and
compounds formed from lactose. Heating also results in changes in various other
properties including development of cooked flavour, anti-oxygenic property, clotting
and soft curd characteristics and baking quality of milk.
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Freezing of milk results in lactose crystallization, Ca++ binding and flocculation of Thermal Processing of
Milk
milk particles. Various enzymes are present in milk. They have been involved in
processing of milk such as pasteurization e.g., phosphatase and lactopeoxidase,
catalase as index of mastitis or leucocytes, lactoperoxide system for milk preservation.

10.7 KEY WORDS

Enzyme : Organic proteinous catalyst involved in
metabolic raction
Pasteurization : A process of heating milk to kill pathogenic
organisms
Amino group : A group present in amino acid
Denaturation : A process by which structure is changed
e.g.,enzyme or protein
Cations : Positively charged ions e.g., Ca++
Anions : Negatively charged ions e.g., Cl–
Melanoidin : A brown coloured pigment
Reducing sugar : Sugar with free aldehyde or ketonic group

10.8 SOME USEFUL BOOKS

Jenness, R and Patton, S. (1959). Principles of Dairy Chemistry, John Wiley and
Sons. Inc. New York
Webb, H.H., Johnson, A. and Alford, J.A. (1978). Fundamentals of Dairy Chemistry.
The AVI Pub, Co. Inc. West Port, Connecticut.
Ling, E.R. (1956). A Textbook of Dairy Chemistry, Vol. 1& 2, Chapman and Hall,
London, UK

10.9 ANSWER TO CHECK YOUR PROGRESS

Your answers should include following points
Check Your Progress 1
1) i. Denaturation may be defined as the change in the original native three-
dimensional structure of protein. It consists of non-proteolytic structural
changes of protein. The major proteins responsible for denaturation are
whey proteins such as immunoglobulin, beta – lactoglobulin, alpha –
lactalbumin and serum albumin.
2) i. The reason for cooked flavour development in milk is release of H2S. It is
liberated from sulphur containing amino acid cysteine.
3) i. The two reactants of browning reaction are – CHO or aldehyde group of
reducing sugar lactose and -NH2 or amino group of basic amino acids such
as lysine.
4) i. Frozen storage results in crystallization of lactose at low temperature.
Lactose binds to Ca++ and release calcium upon crystallization
Check Your Progress 2
1) i. Enzymes are organic catalysts which are found in plant and animal cells.
The enzymes bring about metabolic changes but they do not undergo any
chemical change.
59
Fundamentals of Dairy 2) i. The enzymes present in milk are -
Chemistry
 Peroxidase
 Lipase
 Phosphatase
 Lactase
 Reductase
 Protease
 Xanthine oxidase
3) i. Lipase is responsible for hydrolytic rancidity in milk by releasing butyric
acid from milk fat.

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