CENTRAL MODEL SCHOOL

BARRACKPORE
AISSCE

CBSE
NAME: SHUBHRODEEP MUKHERJEE

CLASS: XII SCIENCE D

BOARD ROLL NO.:

SUBJECT: CHEMISTRY

INVESTIGATORY PROJECT FILE

 CERTIFICATE

This is to certify that Shubhrodeep Mukherjee, student

of class 12 SCIENCE D, has successfully completed
the research on the project
“Study the Faraday law of Electromagnetic induction”
under the guidance of our chemistry teacher Mr.
Tamal Banerjee and Vice Principal Mr. Sanjay Dubey
in partial fulfillment of the curriculum of Central Board
of Secondary Education leading to the award of
annual examination of the year 2022-23.

SUBJECT TEACHER EXTERNAL EXAMINER VICE PRINCIPAL

 ACKNOWLEDGEMENTS
I would like to express my special gratitude to my
chemistry teacher as well as our principal who gave
me the golden opportunity to do this wonderful
project of the topic “AMOUNT OF CASEIN IN MILK”
which also helped me in doing a lot of research and I
came to know about so many new things and I am
really thankful to them.
Secondly, I would also like to thank my parents and
friends who helped me a lot in finalizing the project
within the limited time frame.
 AIM

To study the amount of casein in milk.

 INTRODUCTION

Milk is a complete diet as it contain proteins,

carbohydrates, fats, minerals, vitamins and water. The
average composition of milk from different sources is
given below:

SOURCES WATER MINERALS PROTEINS FATS CARBOHY-

DRATES
OF MILK (%) (%) (%) (%)
(%)
Cow 87.1 0.7 3.4 3.9 4.9
Human 87.4 0.2 1.4 4.0 4.9
Goat 87 0.7 3.3 4.2 4.8
Sheep 82.6 0.9 5.5 6.5 4.5

Casein is the most predominant phosphoprotein found in milk and cheese.

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 proteolyptic enzyme typically obtained from the stomach 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 which
show some resemblance with surfactant-type micellae 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 the milk, the negative charges
are neutralized.
Ca2+-Caseinate+2CH3COOH(aq) Casein+(CH3COO)2Ca(aq)
The isoelectric 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 salt
solutions such as sodium oxalate and acetate.

Structure of Casein
 APPARATUS REQUIRED

Funnel with Glass Rod Filter Paper

funnel stand

Weight Box Test Tubes Pestle & Mortar

 CHEMICALS REQUIRED

Different sources of milk.

Saturated (NH4)2SO4 CH3COOH

 PROCEDURE

1. Wash the beaker (250 ml) with the distilled water

and dry it.
2. Take 20 ml of buffalo’s milk in 250 ml beaker and
find its weight.
3. Add 20 ml saturated solution of ammonium sulphate
slowly with stirring fat and casein will separate out
as precipitate.
4. Filter the above solution and transfer the precipitate
in another beaker.
5. Treat the above precipitate with 30 ml distilled
water. Casein dissolves forming milky solution
whereas fat remains as such.
6. Warm the above contents of the beaker to 40 – 45oc
on a low flame. Now, add 1% acetic acid solution
drop wise with stirring when casein gets
precipitated.
7. Filter the precipitated casein and wash with distilled
water and dry it.
8. Find the weight of dry precipitate.
9. Repeat the whole experiment with cow’s milk,
goat’s milk and sheep’s milk.
 OBSERVATIONS

Volume of milk taken in each case = 20 ml

Weight of milk taken = W1 g
Weight of casein taken = W2 g
Percentage of casein = Weight of casein x 100
Weight of milk

S.no. Type of Volume Weight Weight Percentage

Milk of milk of milk of of casein
taken (W1 g) casein
(ml) (W2 g)
1. Buffalo’s 20 23.09 0.632 2.73%
milk
2. Cow’s 20 35.66 0.55 1.64%
milk
3. Goat’s 20 23.09 0.77 3.67%
milk
 RESULTS
Different samples of milk contains different precentages of
casein.
Highest percentage of casein is present in goat’s milk.
 PRECAUTIONS

1. Handle apparatus and chemicals carefully.

2. Add ammonium sulphate solution very slowly.
3. Stir milk while adding chemicals.
4. Do not disturb milk after adding ammonium
sulphate solution and wait some time for fat and
casein to precipitate out.
5. Take the amount readings carefully with digital
weighing machine only.
 CONCLUSION
This study clearly indicates that the amount of casein
precipitated from the Goat’s milk was higher than that of the
other milk samples. The quantitative analysis of casein
precipitated from the various milk samples provide the ample
scope to the cottage cheese industries.
It was found that cow’s milk contains the smallest amount of
casein protein. Although the mineral content in goat’s and
cow’s milk are same, goat’s milk contains more calcium,
potassium, iron, magnesium and sodium. All milk has lots of
caseins but there are different types of caseins and for
someone who has casein sensitivity, goat milk may provide an
alternative to which they do not react.
 BIBLIOGRAPHY
1. www.wikipedia.com
2. www.encyclopedia.com
3. www.caseinepro.com
4. www.sciencejournals.com
5. www.icar.nic.in
6. www.zetascience.com
7. www.scribd.com