It

Chemistry project
On
Quantity of casein
In milk

Project supervisor:. Submitted by:.

Mr B K SINGH JYOTSHNA BHAINSAL
PGT, CHEMISTRY XII SCIENCE
DAV PUBLIC SCHOOL ROLL NO.
MCL, BANDHABAHAL
 ACKNOWLEDGEMENT
In the accomplishment of this project successfully,
many people have bestowed their blessings upon
me and the heart pledged support. I want to thank
my subject teacher Mr B K Singh whose valuable
guidance helped me to complete this project.

I can’t forget to offer my sincere thanks to my

parents and also to my classmates who helped me
to carry out this project work successfully.

Jyotshna Bhainsal
 BONAFIDE CERTIFICATE
It is to certify that JYOTSHNA BHAINSAL of class XII
SCIENCE has successfully completed research in the
below given project under the heading 'Quantity of
casein in milk' during the academic session 2019-20
under the guidance of Mr B K Singh.

Signature of internal examiner

Signature of external examiner

 PREFACE
For the practical fulfillment of the subject
chemistry, I hereby submit a project on
'Quantity of casein in milk’ for the session
2019-20.
INDEX
 Objective
 Introduction
 Requirements
 Theory
 Procedure
 Observations
 Conclusion
 Bibliography
 OBJECTIVE
To study the quantity of casein in different samples of
milk.

INTRODUCTION
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. The major milk protein casein is found
only in milk and nowhere in the world. The composition
of milk from different sources is given below:-
 APPARATUS REQUIRED
 Beakers(250ml)
 Filter-paper
 Glass rod
 Weight box
 Filteration flask
 Buchner funnel
 Test tubes
 Porcelain dish

CHEMICALS REQUIRED
 Different samples of milk
 1% acetic acid
 Saturated Ammonium sulphate solution

THEORY
Casein is a major protein constituent in milk and is
a mixed phosphor-protein. When coagulated with
rennet, casein is sometimes called paracasein.
British terminology, on the other hand, uses the
term caseinogen for the uncoagulated protein and
casein for coagulated protein. As it exists in milk,
it is a salt of calcium.
Casein is not coagulated by heat. It is precipitated
by acids and by rennet enzymes, a proteolytic
enzyme, typically obtained from the stomachs of
calves. The enzyme trypsin can hydrolyze off a
phosphate-containing peptone.
Casein consists of a fairly high number of praline
peptides, which do not interact. There are also no
disulphide bridges. As a result, it has relatively
little secondary structure or tertiary structure.
Because of this, it cannot denature. It is relatively
hydrophobic, making it poorly soluble in water. It
is found in milk as a suspension of particles called
casein micelles in a sense that the hydrophilic parts
reside at the surface. The caseins in the micelles
are held together by calcium ions and hydrophobic
interactions. These micelles have negative charge
and on adding acid to milk, the negative charges
are neutralized.
The isoelectronic point of casein is 4.7. 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 sodium oxalate and sodium acetate.

PROCEDURE
o A clean dry beaker with 20ml of cow's milk
was taken. 20ml of saturated ammonium
sulphate solution was added slowly with
stirring. Fat along with casein was precipitated
out.
o The solution was filtered and the precipitates
were transferred to another beaker. 30ml of
distilled water was added to the precipitate.
Only casein dissolved in water forming milky
solution leaving fat undissolved.
o The milky solution was heated to about 40°C
and 1% acetic acid solution was added drop-
wise, when casein got precipitated.
o The precipitate was filtered, washed with
water and the precipitate was allowed to dry.
o The dry solid mass was weighed in a previously
weighed watch glass.
o The experiment was repeated with other
samples of milk.

OBSERVATIONS
 CONCLUSION
Different samples of milk contain different
percentages of casein. In addition to being consumed
in milk, casein is used in the manufacture of
adhesives, binders, protective coatings, plastics(such
as for knife handles and knitting needles), fabrics,
food additives and many other products. It is
commonly used by bodybuilders as a slow-digestive
source of amino acids as opposed to the fast-digesting
whey protein, and also as an extremely high source of
glutamine. Another reason it is used in body-building,
is because of its anti-catabolic effect, meaning that
casein consumption inhibits protein breakdown in the
body. Casein is frequently found in otherwise non-
dairy cheese substitutes to improve consistency
especially when melted.

BIBLIOGRAPHY
 www.scribd.com
 www.wikipedia.com
 www.encyclopedia.com
 www.caesine.pro.com
 Magazine