INTRODUCTION

4 - 2015

Chemistry Investigatory Project

Arpit Ranka

XII – a

Roll No. - 18

2014-201ACKNOWLEGEMENT

I would like to express my immense gratitude to my

chemistry teacher Mrs. Poonam Taneja , for the help and

guidance she 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.

- Arpit Ranka
Certificate

This is to certify that Mr. Arpit Ranka (Roll No. - 18) ,

student of class XII – ‘A’, S.D Jain Modern School Surat 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 2014-2015 under

the guidance of Mrs. Poonam Taneja.

School Stamp

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 OF

MILK

WATER

MINERALS

(%)

(%)

PROTEINS

FATS
(%)

(%)

CARBO-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.

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 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 + 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 nondairy cheese substitutes

to improve consistency especially when melted.

Aim –

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.

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 20 ml of buffalo’s 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. 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 ml

Weight of milk taken = W₁ g

Weight of Casein isolated = W₂ g

Percen