CHEMISTRY INVESTIGATORY

PROJECT

Academic Session: 2023-2024

Name: Jaymit Nayak

Class: 12B
Roll.no:
 Certificate
Thisis to certify that Ma. Jaymit Nayak of class XII B has
successfully completed this Chemistry project on the topic
“Study of amount of casein in different milk samples”
prescribed by prescribed by Mr. Hitesh Velari during
academic session 2023-24 as per the guidelines issues by
Central Board of Secondary Education.

Internal Examiner Principal External Examiner

 ACKNOWLEGEMENT

I would like to express my special thanks of gratitude to my teacher Mr.

Hitesh Velari as well as our Principal Mrs. Nirmal Tondon who gave
me the golden opportunity to do this wonderful project of subject
Chemistry on the topic “Study of amount of casein in different milk
samples” which also helped me in doing a lot of Research and I came
to know about so many new things I am really thankful to them.

Secondly, I would also like to thank my parents and friends who helped
me a lot in finalizing this project within the limited time frame.

Date: Jaymit Nayak

 INTRODUCTION –

Milk is a complete diet as it contains proteins, carbohydrates,

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

SOURCE WATER MINERALS PROTEINS FATS CARBOHYDRATES

OFMILK
(%) (%) (%) (%) (%)

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 phosphoprote is found in milk

an 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 proteolytic enzyme typicallyobtained 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 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 milk the negative charges are neutralized.

Ca2+ Caesinate + 2 CH3COOH(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 in salt
solutions such as sodium oxalate and sodium acetate.
Applications:
In addition to being consumed in milk, casein in 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 ofamino acids as
opposed to the fast-digesting whey protein, and also as an
extremely high source of glutamine (post workout). Another
reason it is used in bodybuilding, is because of its anti-catabolic
effect, meaning that casein consumption inhibits protein
breakdown in the body. Casein is frequently found in otherwise
nondairy cheese substitutes to improve consistency especially
when melted.
Theory
Milk contains 3 to 4% casein suspended in water in the colloidal
form. It is precipitated in a weakly acidic medium.

APPARATUS REQUIRED
Funnel, funnel stand , glass rod , filter paper, weight box , test
tubes, pestle and mortar.

CHEMICALS REQUIRED
1) Different samples of milk.
2) Saturated ammonium sulphate solution.
3) 1 % acetic acid solution.
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 - 45°C 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 isolated = W₂ g

Percentage of casein = Weight of Casein x 100

Weight of milk

S.no. Type of milk Volume of Weight Weight of Percentage of

milk taken of milk Casein casein
(ml) (W₁ g) (W₂ g)

1. Buffalo’s 20 23.09 0.632 2.73%

milk

2. Cow’s milk 20 35.66 0.55 1.64%

3. Goat’s milk 20 23.09 0.77 3.67%

RESULT
Different Samples of milk contains different percentage 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.
BIBLIOGRAPHY
www.wikipedia.com
www.encyclopedia.com
www.sciencejournals.com
www.icar.nic.in
www.zetascience.com