AISSCE 2020

COMPARATIVE STUDY OF
CAESIN IN DIFFERENT
BRANDS OF MILK PROJECT
IN BIOLOGY

REGISTRATION NUMBER:
NAME: L.PRAGADI
BATCH: 2019-2020
 TO STUDY THE
QUANTITY OF CASEIN
PRESENT IN
DIFFERENT SAMPLES
OF MILK
 INDEX
 AKNOWLEDEMENT – 1
 OBJECTIVE-2
 INTRODUCTION-3,4
 APPLICATIONS-5
 APPARATUS REUIRED-6
 CHEMICALS REQUIRED-6
 PROCEDURE-7
 OBSERVATIONS-8
 RESULT-9
 PRECAUTIONS-10
 BIBLIOGRAPHY-11
 PHOTOS
 ACKNOWLEGEMENT
I would like to express my immense gratitude to my

Principal Mrs.RADHA SUBRAMANIAN, M.Sc., B.Ed. and

my Biology teacher Mrs.NIRMALA SURESH, M.Sc.,

B.Ed., M.Phil. For the help and guidance she provided for

completing this 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, lab attenders 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.

- L.PRAGADI
OBJECTIVE

To study the quantity of Casein present in different

samples of milk.
 INTRODUCTION
SOURCE WATER MINERALS PROTEINS FATS CARBO-
OF MILK HYDRATES
(%) (%) (%) (%)
(%)

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

Milk contains two types of proteins -- casein and whey. Casein is

80% of the milk protein, while whey is 20%.Casein protein is
digested slowly, while whey protein digested quickly. This is an
important difference between these two popular dairy proteins.

Like other animal proteins, casein is a complete protein source.

That means it provides all the essential amino acids your body
needs for growth and repair .

It also contains various unique proteins and bioactive

compounds, some of which have health benefits.

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
micelle 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 non dairy cheese substitutes to improve
consistency especially when melted.
 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 50 ml of sample 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. Remove the fat by using a suitable organic solvent like
alcohol.
9. Find the weight of dry precipitate.
10. Repeat the whole experiment with milk from
different brands available in the market.
 OBSERVATIONS
Volume of milk taken in each case = 50 ml
Weight of Casein isolated = W g
Percentage of casein = Weight of Casein x 100
WEIGHT OF MILK

Sl. Type of Volume of Weight of

No. milk milk taken Casein
(ml)
(W g)

1. Amul 50

2. Thirumala 50

3. Heritage 50

4. Aavin 50 1.95
blue

5. Nestlé 50 0.34
milk
powder

6. Aarokya 50 1.32
 RESULT
According to our analysis of various samples of milk, we
conclude that: Cow milk contains 5% casein.
milk powder contains 3.25% casein.
Tirumala milk contains 4.2% casein.
Amul milk contains 3.88% casein.
Aavin milk contains

According to above results, we conclude that Amul’s milk

is most beneficial for human beings
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
www.icbse.com
PHOTOS