CHEMISTRY

INVESTIGATORY
PROJECT

Aastha Malhotra
XII-B
Apeejay School, Pitampura
APEEJAY SCHOOL PITAMPURA
Department of Chemistry

Certificate
This is to certify that Aastha Malhotra XII – B, a student of Apeejay School,
Pitampura has completed her research on the topic – ‘Study of Quantity
of Casein in Different Samples of Milk’ under the guidance of Mrs.
Bharti Rattan (subject teacher) during the year 2022-23 in practical
fulfillment of chemistry investigatory project.

Signature

Acknowledgement

I am greatly indebted towards the principal for giving me an

opportunity in elaborating my knowledge towards the subject
(Chemistry) by completing this project work.

I express my heartiest gratitude to my beloved school for the guidance

 . I would also like to thank my parents,sister and my chemistry
teachers (Mrs. Bharti Rattan and Mrs. Anuradha Batra) for giving me
their cooperation in completing this project.

INDEX

1. Certificate

2. Acknowledgement

3. Aim
4. Apparatus

5. Theory

6. Experiment

7. Conclusion

8. Precaution

9. Bibliography

AIM

To Study the Quantity of Casein Present in Different Sample of

Milk
 APPARATUS

○ 250 mL beakers
○ Funnel
○ Glass rod
○ Chemical Balances
○ Test tubes
 ○ Filtration flask
○ Bunsen burner
○ Different samples of Milk
○ 1% acetic acid
○ Saturated ammonium sulfate solution

THEORY

Milk is a multinutrient fluid and it is the primary source of

nutrition for humans. It consists of 80% of proteins. The protein
in the milk is classified into casein and whey protein. Milk
protein consists of 80% of casein and 20% whey protein. The
function of casein is to provide energy to the human body. The
name of casein is related to the family of phosphoproteins. These
proteins are commonly found in mammalian milk. This study
deals with the precipitation of casein from the various milk
samples such as cow milk, goat milk, buffalo milk and also the
samples that availed from the market. The technique of
precipitation of casein is used to predict the protein content in
the milk samples.

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 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 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.

APPLICATIONS
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 (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 non-dairy cheese substitutes to improve consistency
especially when melted.

PROCEDURE

1. Wash the beaker (250 ml) with the distilled water and dry it.
2. Take 20 ml of buffalo’s milk in a 250 ml beaker and find its weight.
3. Add 20 ml saturated solution of ammonium sulfate 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 x100
 Weight of Milk

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

Milk Milk taken Milk (W1 g) Casein of 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

RESULT

Different samples of milk contain different percentages 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.caesine-pro.com
www.sciencejournals.com

www.icar.nic.in

www.zetascience.com

www.scribd.com