ARMY PUBLIC SCHOOL

KUNRAGHAT

A project submitted to department of

Submitted to: submitted by:

Mr.k.s pandey shruti kumari

xii-b
 INDEX
1. Certificate
2. Acknowledgement
3. Objective
4. Milk
5. Casein
6. Materials required
7. Procedure
8. Observations
9. Result
10. Precautions
11. Bibliography
TO STUDY THE QUANTITY OF
CASEIN PRESENT IN
DIFFERENT SAMPLES OF
MILK
 MILK
Milk is a nutrient-rich, white liquid food
produced by the mammary glands of mammals.
It is the primary source of nutrition for infant
mammals (including humans who are breastfed)
before they are able to digest other types of
food. Early-lactation milk contains colostrums,
which carries the mother's antibodies to its
young and can reduce the risk of many
diseases. It contains many other nutrients
including protein and lactose. Interspecies
consumption of milk is not uncommon,
particularly among humans, many of whom
consume the milk of other mammals. As an
agricultural product, milk, also called dairy milk,
is extracted from farm animals during or soon
after pregnancy. Dairy farms produced about
730 million tones of milk in 2011, from 260
million dairy cows. India is the world's largest
producer of milk, and is the leading exporter of
skimmed milk powder, yet it exports few other
milk products.
 CASEIN
Casein (from Latin caseus "cheese") is a family
of related phosphoproteins (αS1, αS2, β, κ).
These proteins are commonly found in
mammalian milk, comprising c. 80% of the
proteins in cow's milk and between 20% and
45% of the proteins in human milk. The j Casein
has a wide variety of uses, from being a major
component of cheese, to use as a food additive.
The most common form of casein is sodium
caseinate. As a food source, casein supplies
amino acids, carbohydrates, and two essential
elements, calcium and phosphorus. Casein
contains a high number of proline residues,
which do not interact. There are also no
disulfide bridges. As a result, it has relatively
little tertiary structure. 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 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 κ-
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 κ-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. The enzyme trypsin can
hydrolyze a phosphate-containing peptone. It is
used to form a type of organic adhesive.

 REACTION INVOLVED

Ca2+ -Caseinate + 2CH3COOH(aq.) Casein(s)+ (CH3COOH)2Ca

 STRUCTURE OF CASEIN
OBJECTIVE:-
To study the quantity of casein present in
different samples of milk.

MATERIALS REQUIRED:-

• Conical flask
• Beakers
• Funnel
• Measuring cylinder(100 mL)
• Watch glass
• Filter paper
• 1% acetic acid
• Different samples of milk
• Glass rod
PROCEDURE:-
•Take 200 mL of each sample of milk in separate
beakers (500 mL).
• Heat the beakers containing milk sample upto
50- 60oC.
• Now, add a few drops of 1% acetic acid
solution slowly with constant stirring with a
glass rod for 5-10 minutes.
• After adding acetic acid, casein coagulates as
amorphous substance.
• Filter the precipitate with the help of the
funnel and wash the precipitates several times
with tap water.
• Remove the fat by using a suitable organic
solvent like alcohol.
• Now, wash the casein again with water and dry
it.
• Weigh a dried casein in a watch glass.
• Repeat this process with all samples of milk.
OBSERVATIONS:-
S.no Type of Amount of % of
milk Casein casein
present present
RESULT
According to our analysis of various
samples of milk, we conclude that:
PRECAUTIONS
• During filtration, press the casein formed.
• Use only the required amount of acid for
complete precipitation.
• Use only fresh milk.
• Use same amount of each sample for the
experiment.
 BIBLIOGRAPHY

• https://arihantbooks.com/laboratory-
manualchemistry-class-xii
• https://en.wikipedia.org/wiki/Casein
• https://en.wikipedia.org/wiki/Milk
• https://www.slideshare.net/dineshpol/amount-
ofcasein-in-milk
• https://www.slideshare.net/Neelanjyan/study-
ofquantity-of-caesin-present-in-different-
samples-ofmilk-54726663
 Certificate
This is to certify that Shruti Kumari, student of
class XII-B ,ARMY PUBLIC SCHOOL,has
completed the project titled “TO STUDY THE
QUANTITY OF CASEIN PRESENT IN DIFFERENT
SAMPLES OF MILK” during the academic year
2019-2020 towards partial fulfillment of credit
for the Chemistry practical evaluation of CBSE
2019-2020,and submitted satisfactory report ,as
compiled in the following pages,under my
supervision.

Department of Chemistry
ARMY PUBLIC SCHOOL
 Acknowledgement
I would like to express my sincere gratitude to
my Chemistry mentor for his vital support,
guidance and encouragement, without which
this project would not have come forth.
I would also like to express my gratitude to the
Staff Department of Chemistry at ARMY
PUBLIC SCHOOL for their support during the
making of this project.

Shruti kumari
________________