2021 -2022

ACKNOWLEDGEMENT

I would like to express my immense gratitude to my

chemistry teacher MR.RAVI KANT DWIVEDI,for the help
and guidance he 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.

-ABHINAV NARAYAN
 CERtifiCAte

This is to certify that Mr.ABHINAV NARAYAN (RollNo.01),

student of class XII -PCM B1 St.Xaviers High School Hardoi
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 2021-
2022 under the guidance of Mr.Ravi Kant Dwivedi.

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-
OF R S HYDRATES
MILK (%) (%)
(%) (%) (%
Cow 87.1 0.7 3.4 3.9 4.9

Human 87.4 1.4 4.0 4.9

0.2
Goat 87 0.7 3.3 4.2 4.8

Sheep 0.9 5.5 6.5 4.5

82.6

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 + 2CH3C00H(aq)

■^Casein+(CH3C00)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.
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.
APPARATUSREQUIRED—
Funnel, funnel stand, glass rod, filter paper, weight box
test tubes, pestle and mortar.

CHEMICAI SREQUIRED—
(i) Different samples ofmilk.

(ii) Saturated ammonium sulphatesolution.

(iii) 1 % acetic acidsolution.

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I PROCEDURe— i
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1. Wash the beaker (250ml) with the distilled water and dryit.
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2. Take20mlofbuffalo'smilkin250mlbeakerandfinditsweight. i
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3. Add20mlsaturatedsolutionofammoniumsulphateslowlywith \
stirring.Fatandcaseinwillseparateoutasprecipitate.
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4. Filtertheabovesolutionandtransfertheprecipitateinanother
 beaker.

5. Treattheaboveprecipitatewith30mldistilledwater.Casein
dissolvesformingmilkysolutionwhereasfatremainsassuch.
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6. Warm the above contents of the beaker to 40 -
45°Cona low flame. Now, add 1 % acetic acid solution i
drop wise with stirring when casein getsprecipitated. i
7. Filter the precipitated casein and wash with
distilledwater and dryit.

8. Find the weight of dryprecipitate.

9. Repeat the whole experiment with cow's milk, goat's

milk and sheep'smilk. \
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i OBSERVAtionS— i
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! Volumeofmilktaken ineach case=20ml !

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Weight ofmilktaken =\N^g
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i Weight of Casein isolated = W2 g i
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i Percentage of casein = Weight of Caseinxl 00 i
| Weight of milk \
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S.n Type of Volume Weight Percentage
o. milk of milk Weigh t of of casein
taken of milk Casei
(ml) (W, g) n
1. Buffalo's 20 23.09 0.63 2.73
milk 2 %

Cow's 35.66 0.55 1.64

2. milk 20 %
3. Goat's 23.09 0.77 3.67
milk 20 %
Result—

Different Samples of milk contains different percentage of casein.

Highest percentage of casein is present in Goat': milk.

PRECAUtionS —

1. Handle apparatus and chemicalscarefully.

2. Add ammonium sulphate solution veryslowly.
3. Stir milk while addingchemicals.
4. Do not disturb milk after adding ammonium sulphate solution
and wait some time for fat and casein to precipitateout.
5. Take the amount readings carefully with digital weighing
machineonly.
BIBLIOGRAPHY
www.wikipedia.com

www.encyclopedia.com
www.caesine-
pro.comwww.sciencejou
rnals.comwww.icar.nic.i
nwww.zetascience.com
www.scribd.com