Amount of Casein in Milk Chemistry Project Cbse Class 12

2024 - 2025
CHEMISTRY INVESTIGATORY PROJECT
Sri Thillai
Hari XII – A
ROLL NO. -
ACKNOWLEGEMENT
I would like to express my immense gratitude to

my chemistry teacher Mrs. Poonam Taneja , for
the help and guidance she provided for completing
the investigatory project.
I also thank my parents who gave their ideas and
inputs in making this Project. Most of all I thank
our school management, for providing us the
facilities and opportunity to do this project.
Lastly, I would like to thank my school mates who
have rendered and done this project along with
me. Their support made this project fruitful.
- SRI THILLI HARI

CERTIFICATE
This is to certify that Mr. Sri Thillai Hari (Roll No. -

) , student of class XII – ‘A’, Green field
International School has successfully completed
research in the below given project under the
heading ‘Study of amount of casein in different
milk samples’ during the academic session 2024-
2045 under the guidance of Mr. Muneeshwaran.
School Stamp
Signature of Principal
Signature of external examiner
Signature of chemistry teacher

OBJECTIVE –
To study the quantity of Casein

present in different samples of
milk.
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 WATE MINERAL PROTEINS FATS CARBO-HYDRATES
OF MILK R S
(%) (%) (
(%) (%) %
)
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 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 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 + 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 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 of
amino 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.
AIM –
To study quantity of casein in different samples of milk.
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 –
(i) Different samples of milk.
(ii) Saturated ammonium sulphate solution.
(iii) 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 Volume Weig Weight Percentage of

. milk of milk ht of of casein
taken milk Casein
(ml) (W₁ (W₂ g)
g)
1. Buffalo 2 23.09 0.63 2.73
’s 0 2 %
milk
2. Cow’s 2 35.66 0.55 1.64
milk 0 %
3. Goat’s 2 23.09 0.77 3.67
milk 0 %
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.co
m www.caesine-
pro.com
www.sciencejournals.
com www.icar.nic.in
www.zetascience.com
www.scribd.com

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2024 - 2025

CHEMISTRY INVESTIGATORY PROJECT

I would like to express my immense gratitude to

- SRI THILLI HARI

This is to certify that Mr. Sri Thillai Hari (Roll No. -

Signature of external examiner

Signature of chemistry teacher

To study the quantity of Casein

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

Ca2+ - Caesinate + 2CH3COOH(aq)  Casein+

The isoelectric point of casein is 4.7. The

In addition to being consumed in milk, casein

(ii) Saturated ammonium sulphate solution.

(iii) 1 % acetic acid solution.

2. Take 20 ml of buffalo’s milk in 250 ml beaker and find

3. Add 20 ml saturated solution of ammonium

4. Filter the above solution and transfer the

5. Treat the above precipitate with 30 ml

6.Warm the above contents of the beaker to 40 -

7. Filter the precipitated casein and wash with

8.Find the weight of dry precipitate.

9.Repeat the whole experiment with cow’s milk,

ml Weight of milk taken = W₁ g

Weight of Casein isolated = W₂ g

Percentage of casein = Weight of Casein x 100

S.no Type of Volume Weig Weight Percentage of

Different Samples of milk contains different

Highest percentage of casein is present in Goat’s

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