Certificate

This is to certify that ‘Harsh Pratap Singh’ of

class 12th ‘C’ has successfully completed the
project work on ‘Determine the amount of
casein in different sample of milk’ for class
XII practical examination of chemistry
conducted by CBSE, New Delhi in year 2018‐
19.

Sign of internal Sign of external

examiner: examiner:

Sign of Principal:
Acknowledgem
ent
I would like to sincerely and profusely
thank Mr. Devendra Sir for the
valuable guidance, advice and for
giving useful suggestions and relevant
ideas that facilitate an easy and early
completion of this project.
And would also like to thank my
parents and my friends for helping me
with my project with every possible
help they could get me.
INDEX
1. Introduction
2. Aim
3. Requirements
4. Theory
5. Procedure
6. Observations
7. Conclusion
8. Bibliography
Introduction
Casein is the name of related phosphor
proteins. These proteins are commonly
found in mammalian milk, making up
80%of the proteins in cow milk and
between 20% and 45% of the proteins in
human milk. Casein has a wide variety of
uses, from being a major component of
cheese, to use as a food additive, to a
binder for safety matches. As a food
source, casein supplies for amino acids,
carbohydrates and two inorganic

elements, calcium and phosphorus.

Composition of Casein:
Casein contains a fairly high number
of proline residues, which do not
interact. There are also no
disulphide bridges. As a result,
hydrophobic, making it poorly
soluble in water. It is found in milk
as a suspension of particles called
“casein micelles” which slow only
limited resemblance with surfactant-
type micellae 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. Several
models account for the special
conformation of casein in the
micelles. One of them proposes the
micellar nucleus is formed by
several sub micelles, the periphery
consisting of microvellosites of K-
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 K-casein
molecules.
Uses: -

Paint- Casein paint is a fast

drying, water soluble medium used
by artists. Casein paint has been
used since ancient Egyptian times as
a form of tempera paint, and was
widely used by commercial
illustrators as the material of choice
until the late 1960s when, with the
advent of acrylic paint, casein
became less popular. It is still
widely used by scene painters,
although acrylic has made inroads in
that field as well.
Glue- Casein- based glues were
popular for woodworking, including
for aircraft, as late as the de
Havilland Mosquito. Casein glue is
also used in transformer
manufacturing (specially
transformer board) due to its oil
permeability. While largely replaced
by synthetic resins, casein-based
glues still have a use in certain niche
applications, such as laminating
fireproof doors and the labelling of
bottles.

Cheese making- Cheese

consists of proteins and fat from
milk, usually the milk of cows,
buffalo, goats or sheep. It is
produced by coagulation of casein.
Typically, the milk is acidified and
then coagulated by the addition of
rennet, containing a proteolytic
enzyme, typically obtained from the
stomachs of calves. The solids are
separated and pressed into final
form. Unlike many proteins, casein
is not coagulated by heat. During the
process of clotting, milk-clotting
proteases act on the soluble portion
of the caseins, K-casein, thus
originating an unstable micellar state
that results in clot formation. When
coagulated with chymosin (EC
3.4.23.4) is an aspartic protease that
specially hydrolyses the peptide
bond in Phe105-Met106 of K-
casein, and is considered to be the
most efficient protease for the
cheese-making industry (Rao et
al.,1968). British terminology, on
the other hand, uses the term
caseinogens for the uncoagulated
protein and casein for the coagulated
protein. As it exists in milk, it is a
salt of calcium.

Plastics and fibre- Some of

the earliest plastics were based on
casein. In particular, galalith was
well known for use in buttons.
Fibre can be made from extruded
casein. Limital, a fabric made from
casein fibre (known as Aralac in the
United States), was particularly
popular in Italy during the 1930s.
Recent innovations such as QMilch
are offering a more refined use of
the fibre for modern fabrics.

Protein Supplements An
attractive property of the casein
molecule is its ability to form a gel
or clot in the stomach, which makes
it very efficient in nutrient supply.
The clot is able to provide a
sustained slow release of amino
acids into the blood stream,
sometimes lasting for several hours.

Medical and dental uses-

Casein-derived compounds are used
in tooth
remineralization products to
stabilize amorphous calcium
phosphate(ACP) and release the
ACP onto tooth surfaces, where it
can facilitate remineralization.

Controversies:-
Autism Although research has
shown high rates of use of
complementary and alternative
therapies for children with autism,
including gluten and/or casein
exclusion diets, as of 2008 there is a
lack of evidence for the efficacy of
these diets. A 2006 review of seven
studies indicated that, although all
reported benefits of exclusive diets
in reducing autism symptoms, all
suffered design flaws, and there was
not enough evidence overall to
justify recommending exclusion
diets to patients.

A1/A2 beta caseins in milk-

According to Food Standards
Australia New Zealand(FSANZ),
“Milk contains many types of
proteins can be quite different in the
milk from different breeds of cows
and in the milk from other animals.
Of the six major protein types in
cow’s milk, four are casein proteins
and the other two are whey proteins.
The caseins usually make up about
80% of the protein in cow’s milk.
One of the major caseins is beta-
casein. There are different beta
casein types, but the most common
are beta casein A1(milk high in this
type is known as A2 milk).
Certain breeds of cows, such as
Friesians, produce mostly A1 milk,
whereas other breeds, such as
Guernsey’s, as well as sheep and
goat, produce mostly A2 milk. Milk
produced in Australia and New
Zealand is normally a mix of A1
and A2 milks. The European Food
Safety Authority carried out a
literature review in 2009
concluding “a cause and effect
relationship is not established
between the dietary intake BCM7,
related peptides or their possible
protein precursors and non-
communicable diseases”.
Cancer- T. Colin Campbell’s The
China Study (2005), a book,
describes a direct correlation
between casein administered to rats
and the promotion of cancer cell
growth when exposed to
carcinogens. Aflatoxin (a potent
carcinogen) was administered to
these rats over a 2-week dosing
period. The rats were given a 1 week
postdosing period before beginning
the test (promotion period). During
the promotion period, one group of
rats was put on a 5% casein protein
diet and another group on a 20%
casein protein diet. None of the rats
on 5% casein protein developed
foci, precursors to cancerous cell
growth, and every rat on 20% casein
protein developed the precancer
foci. It should be noted that all test
groups were fed a 20% casein diet
for a total of 5 weeks (2-wk
acclimation, 2-wk dosing, 1-wk
post-dosing) prior to the 12 week
promotion period in order to survive
the initial aflatoxin B1(AFB1)
dosing, regardless of whether they
were in the 5% or 20% test groups.
Campbell has performed additional
studies using a range of different
carcinogens and other experimental
animals, and claims to have found a
consistent correlation between
cancer growth and the amount of
casein protein in diet. A 2001 study
suggest another milk protein, when
protein, may play a protective role
against colon tumours in rats.
According to a study from the
Australian
Dairy Council, casein has
antimutagenic effects.
To study the quantity
Of CASEIN (milk
protein) present in
different samples Of
milk.
Requirements-
APPARATUS-
• 250ML BEAKERS
• FUNNEL, GLASS ROD
• PORCELAIN DISH
• CHEMICAL BALANCES
• TEST TUBES

• FILTRATION FLASK
• BURNER

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 mammary glands of
female mammal. The main constituents
of natural milk are protein,
carbohydrate, mineral vitamins, fats and
water and are a complete balanced diet.
Fresh milk is sweetish in taste.
However, when it is kept for long time
at a temperature of 5 degree it become
sour because of bacteria present in air.
These bacteria convert lactose of milk
into lactic acid which is sour in taste. In
acidic condition casein of milk starts
separating out as a precipitate. When
the acidity in milk is sufficient and
temperature is around 36 degree, it
forms semi-solid mass, called curd.

Procedure
1. A clean dry beaker has been
taken, followed by putting 20 ml
of cow’s milk into it and adding 20
ml of saturated ammonium
sulphate slowly and with stirring.
Fat along with casein was
precipitate out.

2. The solution was filtered and

transferred the precipitates in
another beaker. Added about 30
ml of water to the precipitate.
 Only casein dissolves in water
forming milky solution leaving fat
undissolved.

3. The milky solution was heated

to about 40° C and 1% acetic acid
solution drop-wise, when casein
got precipitated.

4. Filtered the precipitate,

washed with water and the
precipitate was allowed to dry.

5. Weighed the dry solid mass in a

previously weighed watch glass.
 6. The experiment was repeated
with other samples of milk.

Serial Name Weight of

no. of Casein (in 20
Milk ml milk)
1. Cow

2. Buffalo

3. Goat

4. Sheep
“Different samples of
milk contain different
percentage of Casein.”
BIBLIOGRAPHY

1. Wikipedia.com
2. Chemiprojects.blogs
pot.in
3. Scribd.com
 REMARKS

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