INTRODUCTION

MILK
Milk is a nutrient-rich, white liquid food produced by
the mammary glands of mammals. It is the primary
source of nutrition for infant mammals (including
humans who are breastfed) before they are able to
digest other types of food. Early-lactation milk
contains colostrum, which carries the mother's
antibodies to its young and can reduce the risk of
many diseases. It contains many other
nutrients including protein and lactose. Interspecies
consumption of milk is not uncommon, particularly
among humans, many of whom consume the milk of
other mammals. As an agricultural product, milk, also
called dairy milk, is extracted from farm animals
during or soon after pregnancy.

Average composition of milk from different sources is

given ahead.
 CASEIN
Casein (from Latin caseus "cheese") is a family of
related phosphoproteins (αS1, αS2, β, κ). These
proteins are commonly found in mammalian milk,
comprising c. 80% of the proteins in cow's milk and
between 20% and 45% of the proteins in human milk.
The j Casein has a wide variety of uses, from being a
major component of cheese, to use as a food additive.
The most common form of casein is sodium
caseinate.
As a food source, casein supplies amino acids,
carbohydrates, and two essential elements, calcium
and phosphorus.
Casein contains a high number of proline
residues, which do not interact. There are also no
disulfide bridges. As a result, it has relatively little
tertiary structure. It is relatively hydrophobic, making it
poorly soluble in water. It is found in milk as a
suspension of particles, called casein micelles, which
show only limited resemblance with surfactant-type
micelles in a sense that the hydrophilic parts reside at
the surface and they are spherical. However, in sharp
contrast to surfactant micelles, the interior of a casein
micelle is highly hydrated. The caseins in the micelles
are held together by calcium ions and hydrophobic
interactions. Any of several molecular models could
account for the special conformation of casein in
the micelles. One of them proposes the micellar
 nucleus is formed by several submicelles, the
periphery consisting of
microvellosities of κ-casein. Another model suggests
the nucleus is formed by casein-interlinked fibrils.
Finally, the most recent model proposes a double link
among the caseins for gelling to take place. All three
models consider micelles as colloidal particles formed
by casein aggregates wrapped up in soluble κ-casein
molecules. The isoelectric point of casein is 4.6.
Since milk's pH is 6.6, casein has a negative charge in
milk. The purified protein is water-insoluble. While it is
also insoluble in neutral salt solutions, it is readily
dispersible in dilute alkalis and in salt solutions such
as aqueous sodium oxalate and sodium acetate.

The enzyme trypsin can hydrolyze a phosphate

containing peptone. It is used to form a type of
organic adhesive.
Ca2+-Caseinate + 2CH3COOH(aq.) Casein(s)+
(CH3 COOH)2Ca
Structure of Casein:
 Uses of Casein
Casein is used in prepared foods, in medicines
and dietary supplements, and in cosmetics. Minor
industrial applications include the seasoning and
dressing of leather, cleaners and polishes for shoes,
textile printing and sizing, insecticide sprays,
soapmaking, and many uses in which casein serves as a
protective colloid, emulsifying agent, or binder. Major
applications of casein are paper coatings, glues, paints,
plastics, and man-made fibres.

Glues
Wood joints made with casein glue withstand dampness
for some time. Prepared casein glue is a powder
composed of naturally soured or acid casein, lime,
suitable sodium salts, and a fungicide. The powder is
dissolved in water shortly before the glue is used,
whereupon the sodium salts precipitate part of the lime,
release sodium hydroxide, and dissolve the casein as
sodium caseinate; later the rest of the lime slowly
changes the sodium caseinate to insoluble calcium
caseinate.
 Plastics
Molded plastics of casein resemble horn, ivory, ebony,
and marble in appearance. The principal use is for
buttons for clothing. Rennet casein is granulated,
moistened with water, and kneaded thoroughly. Dyes or
pigments may be added. The granules absorb the water
and are softened. The material is then passed through a
heated cylinder press with rotating screw from which
soft plastic is extruded under pressure in rods or tubes.
The soft plastic may then be molded in the desired
shape. The shaped plastic is hardened by long soaking in
formaldehyde solution after which it is slowly dried.

Human-made fibres
Wool-like textile fibres are made from casein by
extruding an alkaline solution of casein through
spinnerets of the kind used in making rayon and then
hardening the fibres in an acid bath containing
formaldehyde. First marketed in the 1930s under the
name Lanital in Italy and Aralac in the United
States, human-made casein fibres saw use during World
War II due to wool shortages.
 Potential health issues and
adverse effects
A1/A2 beta caseins in milk
A1 and A2 beta-casein are genetic variants of the beta
casein milk protein that differ by one amino acid;
a proline occurs at position 67 in the chain of amino
acids that make up the A2 beta-casein, while in A1 beta
casein a histidine occurs at that position. Due to the way
that beta-casein interacts with enzymes found in the
digestive system, A1 and A2 are processed differently
by digestive enzymes, and a seven-amino peptide, beta
casomorphin

Casein allergy
A small fraction of the population is allergic to
casein. Casein intolerance, also known as "milk protein
intolerance" is experienced when the body cannot break
down the proteins of casein.. The prevalence of casein
allergy or intolerance ranges from 0.25 to 4.9% of young
children. Numbers for older children and adults are not
known. Breast milk has not typically been shown to
cause an allergic reaction, but should be administered to
an infant with caution each time in case of adverse
reaction from something the breastfeeding parent
consumed that contained casein
 EXPERIMENT

AIM:
To study the quantity of casein present in
different samples of milk .

MATERIAL REQUIRED:
➢1. 250 ml beaker
➢2. Funnel and Glass road
➢3. Chemical Balances
➢4. Test tube
➢5. Filtration flask
➢6. Burner
➢7. Porcelain dish
 CHEMICALS :

➢ Different samples of milk

➢ 1% of acetic acid solution

➢ Saturated ammonium sulphate solution

THEORY :
Natural milk is an opaque white fluid secreted by
the memory gland of females. The main
constituents of natural Milk are protein,
carbohydrates, minerals, vitamin, fats and water
are a complete balanced diet .
Fresh milk is sweetish in taste however when it is
kept for a long time at a temperature of 5° it
become sore because of bacteria present in air.
These bacteria convert lactose of milk into lactic
acid which is soar in taste in acidic condition
cousing of milk start separating out as a specific
date when the acidity in milk is sufficient and
temperature is around 36°C it forms semisolid
mass called curd .
 PROCEDURE:
➢ Clean dry beaker has been taken, followed by putting
20 ML of cow milk in it and adding 20 ML of saturated
ammonium sulphate slowly which stirring fat along
with casein was precipitated out.

➢ The solution was filtered and precipitates were

tranfered to another beaker, 30 ML of water was
added to precipitate. Only casein is dissolved in water
forming milky solution leaving fat undissolved.

➢ The milky solution was heated to about 40°C and 1%

acetic acid solution drop twice when Casein got
precipitated.

➢ Filter the precipitate, wash it with water and the

precipitate is allowed to dry.

➢ Weight the dry mass in previously weighted watch-

glass.

➢ The experiment was repeated with other samples

which were given.
 OBSERVATION:

RESULT :
According to our analysis of various samples of
milk, we conclude that:
Cow milk contains 3% casein.
Goat milk contains 3.25% casein.
Buffalo milk contains 4.2% casein.
Amul milk contains 3.88% casein.
So various samples of milk contain different quantities of
milk.
Precaution :
• During filtration, press the casein formed.
• Use only the right amount of acid for precipitation
• Use only fresh milk.
• Use same amount of each sample for the experiment.
 Conclusion

❖ Milk is a complete diet as it contains minerals

vitamins proteins carbohydrates and fats.

❖ Casein is major protein constituent in milk and

is mixed as phosphor protein.

❖ Casein is present in milk as calcium casinate in

form of miscelle these miscelles have negative
charge on adding acid to milk, the negative
charge are neutralised.

❖When the acidity of milk is sufficient and

temperature is around 40 degrees then casein in
milk is separated out as a precipitate that is it
becomes insoluble in water and this temperature
at pH.

❖ It is found from this experimental study that

the goat milk contains maximum casein.