CHEMISTRY PROJECT

INTRODUCTION
Casein contains 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 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.
Casein belongs to proteins family which found in milk.
Casein is a white or creamy-coloured powder that is odourless and
tasteless. It has a fine, granular texture and is typically insoluble in
water. It includes distinct proteins: alpha-casein, beta-casein, gamma-
casein, and delta casein. Structure of casein depends upon specific
type of casein. Casein proteins are complex and consists of a
combination of amino acid. In general casein proteins are composed
of long chains of amino acid folded into a globular shape.
1
DESCRIPTION OF THE EXPERIMENT
AIM:
To extract casein from different types of milk.
APPARATUS:
1. Conical flask
2. Beaker
3. Weighing balance
4. HCI
5. Milk samples (as stated above)
6. Petri dish
7. Stirrer
8. Filter
PROCEDURE:
Acid casein is warmed to produce skimmed milk which is acidified
with dilute acid in which whey is separated and curd is washed
several times for drying and then pulverized.
Rennet casein is skimmed milk which is treated with enzyme, the
rennet product is separated and purified.
The above process takes place in the following steps:

* Three different samples of milk are taken in three different
beakers of 250 ml and the samples are heated at 35degree Celsius.
* Then hydrochloric acid is added with constant stirring in the

beakers containing the milk sample in the ratio of 10% of
hydrochloric acid for 100% milk.
2
* By doing so the pH of the milk will decrease and the casein will get
coagulated.
* Once the milk gets coagulated it is passed through the filter paper to
separate the curd and whey. The curd is the part of the milk which we
need for the experiment as it contains the casein.
* The curd which is separated remains in the filter paper. It is then

washed to remove the acid and the whey proteins present in it.
* Then the curd is dried to remove the water content present in it.
* After drying we get the precipitate of casein which we require.
We could perform the test for the presence of casein using

following methods:
*The confirmation test for presence of casein protein is the

xanthoproteic test.
*Biuret test is the second test from which we can confirm the
presence of casein.
3
EXPERIMENT
XANTHPROTEIC TEST
MATERIALS:
1. Milk sample
2. Concentrated nitric acid (Caution: Nitric acid is corrosive and
should be handled with care)
3. Test tubes
4. Test tube rack
5. Dropper or pipette
6. Water bath or hot plate
4
PROCEDURE:
Pour a small amount of milk into a test tube.
Add an equal volume of concentrated nitric acid to the milk in
the test tube using a dropper or pipette. Be cautious while handling
the nitric acid.
Mix the contents of the test tube gently by swirling.
Place the test tube in a water bath or on a hot plate and heat gently.
Do not allow the mixture to boil.
Observe any color change in the solution. A yellow coloration
indicates the presence of aromatic amino acids like tyrosine and
tryptophan, which are characteristic of proteins like casein.
After heating, allow the test tube to cool down to room temperature.
Compare the color of the solution with a control test tube containing
only milk (without nitric acid). The presence of a yellow color in the
test tube containing the milk and nitric acid indicates a positive result
for the presence of casein.
OBSERVATION:
1) Volume of milk taken in each case = 20 ml
2) Weight of milk taken = W1g
3) Weight of casein isolated = W2g
4) Percentage of casein = Weight of casein X 100
5
Sl. Types of Milk Volume of Weight of Weight % of
No Milk Milk of Casein
W1gm Casein
W2gm.
1 Arokya Milk 20 ml 14.2 1.19 8.38%
2 Nandhini milk 20 ml 18.2 1.088 5.78%
3 Cow milk 20 ml 18.17 0.62 3.1%
4 Buffalo milk 20 ml 18.1 0.66 3.3%
5 Goat milk 20 ml 17.86 0.56 3.67%
RESULT:
The xanthoproteic test for the presence of casein in milk would be
indicated by a yellow coloration in the solution after heating with
concentrated nitric acid. If the solution turns yellow, it suggests the
presence of aromatic amino acids like tyrosine and tryptophan, which
are characteristic of proteins such as casein. This color change
confirms the presence of casein in the milk sample.
PRECAUTIONS:
1. Handle concentrated nitric acid with extreme caution.
Wear appropriate protective equipment such as gloves and
goggles.
2. Work in a well-ventilated area to avoid inhaling any fumes.
3. Avoid skin contact with the nitric acid. If it comes into
contact with the skin, wash the affected area immediately with
water.
4. Dispose of the waste properly according to laboratory safety
guidelines
6
USES OF CAESIN:
Casein, a principal protein found in milk, plays a crucial role in
numerous industries due to its versatile properties. In the food
industry, it serves as a key ingredient in cheese production, where it
coagulates with rennet to form curd, the basis for various cheese
varieties. Additionally, it functions as an emulsifier, stabilizer, and
thickening agent in processed foods like yogurt, ice cream, and
sauces, enhancing their texture and consistency.
Beyond food, casein finds applications in nutritional supplements,

particularly in protein powders favored by athletes and bodybuilders.
Its slow-release nature provides sustained amino acid delivery, aiding
in muscle recovery and growth. In pharmaceuticals, casein serves as a
carrier for drug delivery systems, owing to its biocompatibility and
ability to form micelles, facilitating controlled release of medications.
Furthermore, casein-based adhesives are utilized in woodworking,

bookbinding, and paper manufacturing for their strong binding
properties. In the realm of paints and coatings, casein formulations
offer durability, adhesion, and a desirable matte finish, making
them popular choices in art and interior decoration.
Moreover, casein finds utility in textiles as a sizing and finishing

agent, enhancing fabric stiffness, drape, and crease resistance. It
also features in personal care products such as shampoos,
conditioners, and creams. where it functions as a moisturizing and
conditioning agent, promoting healthier hair and skin.
7
CONCLUSION:
This study clearly indicated that the amount of casein precipitated
from the cow milk was higher than that of the other milk samples. The
quantitative analysis of casein precipitated from the various milk
samples provide the ample scope to the cottage cheese manufacture.
Thus, the cow milk is suitable for the best muscle growth and basic
body building achievements. “Different samples of milk contain
different percentage of casein.”
In summary, casein's multifaceted attributes render it indispensable
across a spectrum of industries, from food and pharmaceuticals to
textiles and personal care, contributing to the formulation of diverse
products that meet various consumer needs.
8
BIBLIOGRAPHY:
https://en.wikipedia.org/wiki/Wikipedia:Complete_diff_and_link_gui
de https://takshlaksh.weebly.com/uploads/4/8/1/1/48115631/version_-
_taksh.pd
https://www.scribd.com/document/339107979/Chemistry-Board-
Project-
CLASS-12-CBSE-PAINTS-PIGMENTS-POSTER-COLOURS
https://takshlaksh.weebly.com › version_-_taksh
https://www.slideshare.net/slideshow/hirday-gupta-poster-paintspptx/

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INTRODUCTION

Casein contains high number of proline residues, which do

The above process takes place in the following steps:

* Then hydrochloric acid is added with constant stirring in the

* The curd which is separated remains in the filter paper. It is then

* After drying we get the precipitate of casein which we require.

We could perform the test for the presence of casein using

*The confirmation test for presence of casein protein is the

Beyond food, casein finds applications in nutritional supplements,

Furthermore, casein-based adhesives are utilized in woodworking,

Moreover, casein finds utility in textiles as a sizing and finishing

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