PELJORLING HIGHER SECONDARY SCHOOL

TASHICHOELING SAMTSE: BHUTAN

Year 2023

TOPIC: Quantity of Casein in different milk

Submitted by: Submitted To:

Tenzin Jigme
Index No:012230460010 Bola Nath Kafley
Date:19/11/2022 (Subject Teacher)
 PELJORLING HIGHER SECONDARY SCHOOL
TASHICHOELING
SAMTSE: BHUTAN

CERTIFICATE OF COMPLETION

This is to certify that the project work on

Quantity of Casein in different milk

Is completed and submitted by Tenzin Jigme to the Department of Science,
Peljorling Higher Secondary School in partial fulfillment of requirements of
BCSEA of (Chemistry) curriculum.

Mr. Bola Nath Kafley. Signature of

(Subject teacher/supervisor). Principal

HOD
 Acknowledgment
First of all, I would like to thank my chemistry teacher Mr. Bola Nath Kafley for giving me the
opportunity to work on this project. While I was working on this project I have gain so many
skills and methods to use MS words efficiently. And also I would like to thank my friend
Jamyang Doya for helping me with the formats.
Lastly, I would like to thank my brother for supporting me financially and motivating me day
and night to keep going forward.
 Table of Contents

Page no. Topic

1 Introduction
2 Composition of milk
3 Hypothesis
4 Procedures
5 Background Information
6 Observation and Results
7 Bibliography
 Introduction

Humans first learned to consume the milk of other mammals regularly following the
domestication of animals during the Neolithic Revolution or the development of agriculture.
This development occurred independently in several global locations from as early as 9000–
7000 BC
in Mesopotamia to 3500–3000 BC in the Americas. People first domesticated the most important
dairy animals – cattle, sheep and goats – in Southwest Asia, although domestic cattle had been
independently derived from wild aurochs populations several times since. Initially animals were
kept for meat, and archaeologist Andrew Sherratt has suggested that dairying, along with the
exploitation of domestic animals for hair and labor, began much later in a separate secondary
products revolution in the fourth millennium BC. Sherratt’s model is not supported by recent
findings, based on the analysis of lipid residue in prehistoric pottery, that shows that dairying
was practiced in the early phases of agriculture in Southwest Asia, by at least the seventh
millennium BC.
From Southwest Asia domestic dairy animals spread to Europe (beginning around 7000 BC but
did not reach Britain and Scandinavia until after 4000 BC), and South Asia (7000–5500 BC).
The first farmers in central Europe and Britain milked their animals. Pastoral and pastoral
nomadic economies, which rely predominantly or exclusively on domestic animals and their
products rather than crop farming, were developed as European farmers moved into the Pontic–
Caspian steppe in the fourth millennium BC, and subsequently spread across much of the
Eurasian steppe. Sheep and goats were introduced to Africa from Southwest Asia, but African
cattle may have been independently domesticated around 7000–6000 BC. Camels, domesticated
in central Arabia in the fourth millennium BC, have also been used as dairy animals in North
Africa and the Arabian Peninsula. The earliest Egyptian records of burn treatments describe burn
dressings using milk from mothers of male babies. In the rest of the world (i.e., East and
Southeast Asia, the Americas and Australia), milk and dairy products were historically not a
large part of the diet, either because they remained populated by hunter-gatherers who did not
keep animals or the local agricultural economies did not include domesticated dairy species.
Milk consumption became common in these regions comparatively recently, as a consequence of
European colonialism and political domination over much of the world in the last 500 years.

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 Composition of Milk

Lipid: Initially milk fat is secreted in the form of a fat globule surrounded by
a membrane. Each fat globule is composed almost entirely of triacylglycerols and is surrounded
by a membrane consisting of complex lipids such as phospholipids, along with proteins. These
act as emulsifiers which keep the individual globules from coalescing and protect the contents of
these globules from various enzymes in the fluid portion of the milk. Although 97–98% of lipids
are triacylglycerols, small amounts of di- and monoacylglycerols, free cholesterol and
cholesterol esters, free fatty acids, and phospholipids are also present. Unlike protein and
carbohydrates, fat composition in milk varies widely due to genetic, lactational, and nutritional
factor difference between different species.

Protein: Normal bovine milk contains 30–35 grams of protein per liter, of which about 80% is
arranged in casein micelles. Total proteins in milk represent 3.2% of its composition.

Casein: The largest structures in the fluid portion of the milk are "casein micelles": aggregates of
several thousand protein molecules with superficial resemblance to a surfactant micelle, bonded
with the help of nanometer-scale particles of calcium phosphate. Each casein micelle is roughly
spherical and about a tenth of a micrometer across. There are four different types of casein
proteins: αs1-, αs2-, β-, and κ-caseins. Most of the casein proteins are bound into the micelles.
There are several competing theories regarding the precise structure of the micelles, but they
share one important feature: the outermost layer consists of strands of one type of protein,
kcasein, reaching out from the body of the micelle into the surrounding fluid. These kappa-casein
molecules all have a negative electrical charge and therefore repel each other, keeping the
micelles separated under normal conditions and in a stable colloidal suspension in the
waterbased surrounding fluid.

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 Hypothesis

Milk contains 3% to4% casein suspended in water in colloidal form.It is precipatated in weakly
acidic medium but quantity of Casein in different source of milk is not same.

Materials Required: ❖
Funnel
❖ Funnel stand
❖ Glass rod
❖ Paper filter
❖ Weight box
❖ Test tubes
❖ Pestle and mortar

Chemical Required:
➢ Different sample of milk
➢ Saturated ammonium sulphate solution
➢ 1% acetic acid

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 Procedures

1. Wash the beaker(250 ml) with the distilled water and dry it.
2. Take 20 ml of Buffalo’s milk in the beaker and finds its weight
3. Add 20 ml of saturated solution of ammonium sulphate slowly with stirring, fats 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 fats remain as such
6. Warm the above contents of the beaker to 40-50°C on a low flame. Then, 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 precipitated.
9. Repeat the whole experiment with cow’s milk and goat’ milk.

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 Background Information

Casein contains a high number of proline amino acids which hinder the formation of
common secondary structural motifs of proteins. 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
microvillosities 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.

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 Observation and Results

✓ Volume of milk taken in each case = 20 ml

✓ Weight of milk taken = W×g

✓ Weight of Casein isolated = w×g

✓ Percentage of Casein = ( Wt. of Casein/ Wt. of milk) × 100

SL. No Type of milk Volume of Weight of Weight of Percentage of

milk (g) milk (g) Casein (g) Casein (%)
1 Buffalo 20 23.09 0.632 2.73

2 Cow 20 35.66 0.55 1.64

3 Goat 20 23.09 0.77 3.67

Results:
✓ Different sample of milk contains different amount of casein.
✓ Highest amount of casein is present in goat’s milk.

Page 6
 Bibliography

1. www.wikipedia.com
2. www.scribd.com

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