2022 – 23 (CBSE)

SUBJECT:- CHEMISTRY.
CLASS 12 (SCIENCE).
SUBMITTED BY
SUBHRAJIT ROY
CLASS 12TH SCIENCE
ROLL NO.:-
UNDER THE SUPERVISION OF DR. RUPAK BANIK

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 CERTIFICATE

This is here to certify that, the original and genuine investigation work on the content of the
Project entitled, "STUDY OF THE QUANTITY OF CASEIN IN VARIOUS SAMPLE OF MILK" of
the subject "CHEMISTRY" has been successfully carried out by SUBHRAJIT ROY of class 12
(Science) ROLL NO.:-…………….. under the supervision of the Subject teacher Dr. RUPAK
BANIK as per the guidelines given by CENTRAL BOARD OF THE SECONDARY EDUCATION
(CBSE) for the consideration in partial fulfillment of the requirement for the ALL INDIA
SENIOR SECONDARY CERTIFICATE EXAMINATION (AISSE) 2022-23.

INTERNAL SIGNATURE SCHOOL STAMP

EXTERNAL SIGNATURE PRINCIPAL SIGNATURE

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 ACKNOWLEDGEMENT

I would like to express my sincere thanks to DR. RUPAK BANIK sir for his valuable
guidance and support in completing my project.

I would also like to express my gratitude towards our principal MR. ANIMESH ACHARYA
for giving me this great opportunity to do a project on “STUDY OF THE QUANTITY OF
CASEIN IN VARIOUS SAMPLE OF MILK”. Without their support and suggestions, this
project would not have been completed.

And, I would also thanks to my PARENTS who provided me sufficient encouragement

and support in making f this project. And I thanks to FRIENDS who really showered
constructive feedbacks and suggestions without which the project would not have
been in present form

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 INDEX

SL. Topic Page No.

NO.
1 AIM OF PROJECT 5

2 ABSTRACT 6

3 OBJECTIVE 8

4 INTRODUCTION 8-10

5 APPLICATION 11-15

6 EXPERIMENT 16-18

7 CONCLUSION&DISCUSSION 19

8 BIBLIOGRAPHY 20

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 AIM OF THE PROJECT

STUDY THE QUANTITY OF CASEIN PRESENT IN DIFFERENT SAMPLE OF MILK.

FIG: CASEIN PRODUCT

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 ABSTRACT

The objective is to isolate it in order to perform hydrolysis to break its components

and color reaction for its characterization. Acetic acid was added to isolate casein by
the formation of a solid particle called curd. Then to break down its amino acid
hydrolysis was performed by using 6M HCI.

Color reaction was performing to characterize the protein and its functional group
plus the amino acids. Thus this White solid particle that participate after the addition
of acetic acid is confirmed to be casein.

FIG: CASEIN SOURCE

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 OBJECTIVE

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.

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 Introduction

What is Casein?

Casein is the protein found in all mammals' milk. Mammals include cow, goat,
sheep, yak, buffalo, camel and humans.

Milk is a complete diet as it contains minerals, vitamins, proteins, Carbohydrates, Fats

and Water.

Casein in the most predominant protein in milk and is a mixed phosphor protein.
Casein has a isoelectric pH of about 4.7 can be easily separated around this
isoelectric pH. It readily dissolves in dilute acids and alkalis.

Natural milk is an opaque white fluid Secreted by the mammary glands of Female
mammal .The main constituents of natural milk are Protein, Carbohydrate. However,
when it is kept for long time at a temperature of 5 degree it become sour because of
bacteria present in air. These bacteria convert lactose of milk into lactic acid which is
sour in taste. In acidic conditions casein of milk separate out as precipitate. When the
acidity in milk is sufficient and temperature is around 36 degree, it forms curd.

FIG: COW’S MILK

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 Composition of Casein:

Casein contains a high number of proline amino acids which hinder the formation
of common secondary structural motifs of proteins. There are also no disulfide
bridges. As a result, it has relatively little tertiary structure. lt is relatively
hydrophobic, making it poorly soluble in water. It is found in milk as a suspension
of particles, called casein micelles, which show only limited resemblance with
surfactant-type micelles in a sense that the hydrophilic parts reside at the
surface and they are spherical. However, in sharp contrast to surfactant micelles,
the interior of a casein micelle is highly hydrated. The caseins in the micelles are
held together by calcium ions and hydrophobic interactions. Any of several
molecular models could account for the special conformation of casein in the
micelles. One of them proposes the micellar nucleus is formed by several
submicelles, the periphery consisting of microvellosities of K-casein. Another
model suggests the nucleus is formed by casein-interlinked fibrils. Finally, the
most recent model proposes a double link among the caseins for gelling to take
place. All three models consider micelles as colloidal particles formed by casein
aggregates wrapped up in soluble x-casein molecules. The isoelectric point of
casein is 4.6. Since milk's pH is 6.6, casein has a negative charge in milk. 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
aqueous sodium oxalate and sodium acetate.

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 The caseins in the micelles are held together by calcium ions and hydrophobic
interactions. Any of several molecular models could account for the special conformation of
casein in the micelles . The enzyme trypsin can hydrolyze a phosphate-containing peptone. It
is used to form a type of organic adhesive.

FIG: CASEIN SOURCE

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 APPLICATIONS:

In addition to being consumed in milk casein is used in the manufacture of adhesives,

binders, protective coatings, plastics (such as knife handles and knitting needles), fabrics,
food additives, and many other products. It is commonly used by body builders as slow
digesting whey proteins 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 non dairy substitutes to improve consistency especially when melted.

Paints:-
Casein paint is a fast-drying, water-soluble medium used by artists. Casein paint has
been used since ancient Egyptian times as a form of tempera paint, and was widely
used by commercial illustrators as the material of choice until the late 1960s when,
with the advent of acrylic paint, casein became less popular. It is still widely used by
scene painters, although acrylic has made inroads in that field as well.

FIG: CASEIN PRODUCT(PAINT)

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GLUE:-
Casein-based glues. formulated from casein, water, hydrated lime and m hydroxide
were popular for woodworking, including for aircraft, as latc as the de Havilland
Albatross airliner in 1939 Casein glue is also used in transformer manutacturing
(specifically transformer board) due to its oil 1ermeability. While largely replaced with
synthetic resins, casein-based olues stil1 have a use in certain niche applications,
such as laminating fireproof doors and the labeling of bottles. Elmer's Glue-All,
Elmer's School Glue and many other Borden adhesives were originally made from
casein. While one reason was its non-toxic nature, a primary factor was that it was
economical to use. Towards the end of the 20th century, Borden replaced casein in all
of its popular adhesives with synthetics like PVA.

FIG: CASEIN PRODUCT(GLUE)

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Cheese making:-
Cheese consists of proteins and fat from milk, usually the milk of cows, buffalo,
goat or sleep. It is produced by coagulation that is caused by destabilization of
the casein micelle, which begins the processes of fractionation and selective
concentration. Typically, the milk is acidified and then coagulated by the
addition of rennet, traditionally obtained from the stomachs of calves, but
currently produced more often from genetically modified microorganisms. The
solids are then separated and pressed into final form.

FIG: CHEESE MAKING IN FACTORY

Unlike many proteins casein is not coagulated by heat. During the process of
clotting, milk-clotting proteases act on the soluble portion of the caseins, k-
casein, thus originating an unstable micellar state that results in clot
formation. When coagulated with chymosin, casein is sometimes called par
casein. Chymosin is an aspartic protease that specifically hydrolyzes the
peptide bond in Phe105-Met106 of k-casein, and is considered to be the most
efficient protease for the cheese-making industry. British terminology, on the
other hand, uses the term caseinogens for the un-coagulated protein.
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Medical & dental uses:-
Casein-derived compounds are used in tooth re-mineralization products to
stabilize amorphous calcium phosphate (APC) and release the ACP onto tooth
surfaces, where it can facilitate demineralization.

Casein and gluten exclusion diets are sometimes used in alternative medicine
for children with autism. As of 2015 the evidence the such diets have any
impact on behavior or cognitive and social functioning in autistic children was
limited and weak.

FIG: CASEIN PRODUCT USED IN MEDICAL

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Protein Supplements:-
An attractive property of the casein molecule is its ability to form a gel or clot
in the stomach, which makes it release of amino acids into the blood stream
sometimes lasting for several hours. Often casein is available as hydrolyzed
casein, whereby it is hydrolyzed by a protease such as trypsin. Hydrolyzed
forms are noted to taste bitter and such supplements are often refused by
infants and lab animals in favor of intact casein.

FIG: CASEIN PRODUCT(PROTEIN SUPPLEMENTS)

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 Objective- To study of quantity of casein present in different sample of milk.

 Requirement –
1. 250ml of beaker.
2. Glass Rod.
3. Porcelain dish.
4. Chemical balances.
5. Buchner funnel
6. Test tubes
7. Burner.
8. Different samples of milk.
9. 1% of acetic acid solution.
10. Saturated ammonium sulphate solution
 Procedure-
1. Wash the beaker (250ml) with the distilled water and dry it.
2. Take 20ml of buffalo’s milk in 250ml beaker and find its weight.
3. Add20ml 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 30ml 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.
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 Observations:-
Volume of milk taken in each case = 20ml
Weight of milk taken = W1g
Weight of Casein isolated = W2g
 Percentage of casein =

SL. Types of Vol. of milk Weight of Weight of Percentage of

NO. milk taken(ml) Milk(g) casein Casein

1. Buffalo’s 20 23.09 0.632 2.37%

milk
2. Cow’s milk 20 35.66 0.55 1.64%
3. Goat’s milk 20 23.09 0.77 3.67%

 Result:-
i. Different samples of milk contains different percentage of casein.
ii. 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 waitsometime
for fat and casein to precipitate out.
5. Take the amount reading carefully with digital weighting machine only.
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 Conclusion and discussion
According to above brief analysis of casein milk we are to conclude that:
Amount of casein in cow’s milk is 5%
Amount of casein in goat’s milk is 3.25%
Amount of casein in Buffalo’s milk is 4.20%
Amount of casein in Amul milk is 5%
So, according to above analysis we can finally conclude that cow’s milk is the best
milk or beneficial milk for human beings.

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 Bibliography
To complete this project I took help from the following sources:-

 NCERT class 12 chemistry books part i, ii.

 Evergreen laboratory manual class 12 Chemistry
 Arihant laboratory manual class 12 Chemistry.
 www.google.co.in
 www.wikipedia.org
 www.ncert.nic.in
 www.wikipedia.com
 www.enclopedia.com
 www.caesine-pro.com
 www.sciencsjournals.com

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