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CHEMISTRY INVESTIGATORY PROJECT

2019 - 2020

SUBMITTED TO: SUBMITTED BY:


MR.ASHUTOSH JHA VARUN CHAUDHARY
CLASS:12TH B
ROLL NO.42

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ACKNOWLEGEMENT

I would like to express my immense gratitude to my


chemistry teacher Mr.Ashutosh Jha , for thehelp andguidance she
provided for completing theinvestigatoryproject.
I also thank my parents who gave their ideasand inputs in
making this Project. Most of all I thank ourschoolmanagement,
for providing us the facilitiesand opportunityto do this project.
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Lastly, I would like to thank my school mateswho haverenderedand
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done this project along withme. Their supportmade thisproject
1.fruitful.
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v
- arun chaudhary

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Certificate

This is to certify that Mr. VARUN CHAUDHARY (Roll No. - 42


) , student of class XII – ‘B’, Gayatri Public School Agra 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 2019-
2020 under the guidance of Mr.Ashutosh Jha.
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Signature of Principal

Signature of external examiner

Signature of chemistry teacher

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Objective –

To study the quantity of Casein present


in different samples of milk.

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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 WATER MINERALS PROTEINS FATS CARBO-HYDRATES


MILK
(%) (%) (%) (%) (%)

Cow 87.1 0.7 3.4 3.9 4.9


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Human 87.4
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4.0 4.9
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Goat 87 0.7 3.3 4.2 4.8

Sheep 82.6
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Casein is the most predominant phosphoprote


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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.

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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
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at the surface. The
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caseins for registered user:
in the micelles
are held together by calcium ions and hydrophobic
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interactions.
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the output have negative charge and on
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adding
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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
Thistoisthe fast-digesting
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extremely
high source of glutamine (post
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workout). Another reason it is used in bodybuilding, is
because
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anti-catabolic effect, meaning that casein
consumption
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the outputprotein breakdown in the body. Casein is
documents.

frequently found in otherwise nondairy cheese substitutes to


improve consistency especially when melted. Remove it Now

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Aim –
To study quantity of casein in different samples of milk.

Theory –
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Milk contains 3 to 4% casein suspended in water in the
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colloidal form. It is precipitated in a weakly acidic medium.
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Apparatus Required –
Funnel, funnel stand , glass rod , filter paper, weight box ,
test tubes, pestle and mortar.

Chemicals Required –
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(i) Different samples of milk.
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(ii) Saturated ammonium sulphate solution.
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(iii) 1 % acetic acid solution.

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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.
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4. Filter
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registered solution and transfer the precipitate in another
beaker.
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output documents.
dissolves forming milky solution whereas fat remains as such.
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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.

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Observations –
Volume of milk taken in each case = 20 ml

Weight of milk taken = W₁ g

Weight of Casein isolated = W₂ g

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S.no. Type of milk Volume of Weight Weight of itPercentage


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milk taken of milk Casein casein
(ml) (W₁ g) (W₂ g)

1. Buffalo’s 20 23.09 0.632 2.73%


milk

2. Cow’s milk 20 35.66 0.55 1.64%

3. Goat’s milk 20 23.09 0.77 3.67%

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Result –

Different Samples of milk contains different percentage


of casein.
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Highest percentage of casein is present in Goat’s milk.
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Precautions – Remove it Now

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 and
casein to precipitate out.
5. Take the amount readings carefully with digital
weighing machine only.

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Bibliography –
www.wikipedia.com

www.encyclopedia.com
www.caesine-pro.com
www.sciencejournals.com
www.icar.nic.in
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www.zetascience.com
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