CHEMISTRY INVESTIGATORY PROJECT
Academic Session: 2023-2024
Name: Jaymit Nayak
Class: 12B
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Certificate
This is to certify that Ma. Jaymit Nayak of class XII B has successfully completed this Chemistry project
on the topic “Study of amount of casein in different milk samples” prescribed by prescribed by Mr.
Hitesh Velari during academic session 2023-24 as per the guidelines issues by Central Board of Secondary
Education.
Internal Examiner Principal External Examiner
ACKNOWLEGEMENT
I would like to express my special thanks of gratitude to my teacher Mr. Hitesh Velari as well as our
Principal Mrs. Nirmal Tondon who gave me the golden opportunity to do this wonderful project of subject
Chemistry on the topic “Study of amount of casein in different milk samples” which also helped me in
doing a lot of Research and I came to know about so many new things I am really thankful to them.
Secondly, I would also like to thank my parents and friends who helped me a lot in finalizing this project
within the limited time frame.
Date: Jaymit Nayak
Index
Content Page Number
Introduction 4-5
Applications 6
Theory 7
Apparatus Required 7
Chemicals Required 7
Procedure 8
Observations 9
Result 10
Precautions 10
Bibliography 11
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 givenbelow:-
SOURCE
OF MILK Water (%) Minerals (%) Protiens (%) Fats (%) Carbohydrates (%)
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
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 typicallyobtained 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 isfound in milk as a suspension of particles called casein micelles which show some
resemblance with surfactant-typemicellae 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 + 2 CH3COOH(aq) Casein+(CH3COO)2Ca(aq)
The isoelectric point of casein is 4.7. The purified proteinis 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 ofamino 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.
Theory
Milk contains 3 to 4% casein suspended in water in the colloidal form. It is precipitated in a
weakly acidic medium.
APPARATUS REQUIRED
Funnel, funnel stand , glass rod , filter paper, weight box ,test tubes, pestle and mortar.
CHEMICALS REQUIRED
1) Different samples of milk.
2) Saturated ammonium sulphate solution.
3) 1 % acetic acid solution.
PROCEDURE
1. Wash the beaker (250 ml) with the distilled water and dry it.
2. Take 20 ml of buffalo’s milk in 250 ml beaker and find its weight.
3. Add 20 ml saturated solution of ammonium sulphate slowly withstirring. Fat and casein will separateout as
precipitate.
4. Filter the above solution andtransfer the precipitatein anotherbeaker.
5. Treat the above precipitate with 30 ml distilled water. Caseindissolves 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 waterand 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.
OBSERVATIONS
Volume of milk taken in each case = 20 mlWeight of milk taken
= W₁ g
Weight of Casein isolated = W₂ g
Percentage of casein = Weight of Casein x 100
Weight of milk
[Link]. Type of milk Volume of milk Weightof milk Weight ofCasein Percentage ofcasein
taken(ml) (W₁ g) (W₂ g)
1. Buffalo’smilk 20 23.09 0.632 2.73%
2. Cow’s milk 20 35.66 0.55 1.64%
3. Goat’s milk 20 23.09 0.77 3.67%
RESULT
Different Samples of milk contains different percentage of casein.
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 wait some
time for fat andcasein to precipitate out.
5. Take the amount readings carefully with digital weighing machine only.
BIBLIOGRAPHY
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