ACKNOWLEDGEMENT

I would like to thank Ms. Poonam Gupta

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 high number of proline
residues, which do not interact. There are
also no disulfide 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 replaced by synthetic resins,
casein-based glues till 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 cond in
Phe105-Met106 of K-casein and is
considered to be the most efficient
protease for the cheese making industry
(Raoet al., 1968).
British terminology, on the other hand,
uses the term ‘caseinogen’ for the
uncoagulated protein and casein for the
coagulated protein. As it exists in milk, it
is a salt of calcium.
Plastics & 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. Lanital, 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 can provide a
sustained slow release of amino acids
into the blood stream, sometimes lasting
for several hours.
Medical & 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
Guernseys, 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”. Studies supporting these
claims have had significant flaws, and
the data are inadequate to guide autism
treatment recommendations.
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 suggests
another milk protein, when protein, may
play a protective role against colon
tumours in rats. According to 21 a study
from the Australian Dairy Council,
casein has antimutagenic effects.
 AIM

To Determine the
Amount of CASEIN
Present in Different
Samples of Milk.
 REQUIREMENTS
APPARATUS CHEMICALS
 250ML BEAKERS  DIFFERENT
 FUNNEL, GLASS SAMPLES OF
ROD MILK
 PORCELAIN DISH  1% OF ACETIC
 CHEMICAL ACID SOLUTION
BALANCES  SATURATED
 TEST TUBES AMMONIUM
 FILTRATION FLASK SULPHATE
SOLUTION
 BURNER
AL

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 25 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 degrees, 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 dis- 27 solves
in water forming milky solution leaving
fat undissolved.
3. The milky solution was heated to
about 40° C and 1% acetic acid solution
dropwise, 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 of Milk Weight of
No. .
Casein
Present

1. Cow

2. Buffalo

3. Goat

4. Sheep
OBSERVATION
TAB
 CONCLUSION

“Different
samples of
milk contain
different
percentage
of Casein.”
 BIBLIOGRAPHY
1. Wikipedia.com
2. Chemiprojects.blogspot.in
3. Scribd.com