A COMPARATIVE

STUDY OF
PROTEIN
CONTENT IN EGGS
AND SOY CHUNKS
INTRODUCTION
Ever wondered about proteins, which are the building blocks of life
importance in day to day basis? It’s one of the most important topics
when it comes to your physique and making improvements to it.
So what is protein? Proteins are biopolymer made up of building blocks
of amino acids. These amino acids are joined together by chemical
bonds and then folded in different ways to create three-dimensional
structures that are important to our body’s functioning.

Plants can synthesize all of the amino acids; animals cannot, even
though all of them are essential for life. Plants can grow in a medium
containing inorganic nutrients that provide nitrogen, potassium, and
other substances essential for growth. They utilize the carbon dioxide in
the air during the process of photosynthesis to form
organic compounds such as carbohydrates. Animals, however, must
obtain organic nutrients from outside sources. Because the protein
content of most plants is low, very large amounts of plant material are
required by animals, such as ruminants (e.g., cows), that eat only plant

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material to meet their amino acid requirements. Nonruminant animals,
including humans, obtain proteins principally from animals and their
products—e.g., meat, milk, and eggs. The seeds of legumes are
increasingly being used to prepare inexpensive protein-rich food .
The protein content of animal organs is usually much higher than that
of the blood plasma. Muscles, for example, contain about 30 percent
protein, the liver 20 to 30 percent, and red blood cells 30 percent.
Higher percentages of protein are found in hair, bones, and other
organs and tissues with low water content. The quantity of free amino
acids and peptides in animals is much smaller than the amount of
protein; protein molecules are produced in cells by the stepwise
alignment of amino acids and are released into the body fluids only
after synthesis is complete.
The high protein content of some organs does not mean that the
importance of proteins is related to their amount in an organism
or tissue; on the contrary, some of the most important proteins, such
as enzymes and hormones, occur in extremely small amounts. The
importance of proteins is related principally to their function. All
enzymes identified thus far are proteins. Enzymes, which are
the catalysts of all metabolic reactions, enable an organism to build up
the chemical substances necessary for life—proteins, nucleic acids,
carbohydrates, and lipids—to convert them into other substances, and
to degrade them. Life without enzymes is not possible. There are
several protein hormones with important regulatory functions. In all
vertebrates, the respiratory protein hemoglobin acts as oxygen carrier
in the blood, transporting oxygen from the lung to body organs and
tissues. A large group of structural proteins maintains and protects the
structure of the animal body.
There are two main categories of amino acids in the body. First, we’ve
got essential amino acids – those that the body can’t manufacture, and
thus we must consume in our diets.
Some amino acids are conditionally essential, which means that our
bodies can’t always make as much as we need.

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 Next, we’ve got nonessential amino acids – those that the body can
usually make for itself.

Essential amino acids Conditionally essential amino acids Nonessential

amino acids
 Histidine
 Isoleucine
 Alanine
 Leucine
 Arginine  Asparagine
 Lysine
 Cysteine  Aspartic acid
 Methionine
 Glutamine  Glutamic acid
 Phenylalanine
 Tyrosine  Proline
 Threonine
 Serine
 Tryptophan
 Valine

Why is it important to get enough protein?

During digestion, the body breaks down the protein we eat into
individual amino acids, which contribute to the plasma pool of amino
acids. This pool is a storage reserve of amino acids that circulate in the
blood.
The amino acid pool in the bloodstream readily trades with the amino
acids and proteins in our cells, provides a supply of amino acids as
needed, and is continuously replenished.
Since our bodies need proteins and amino acids to produce important
molecules in our body – like enzymes, hormones, neurotransmitters,
and antibodies – without an adequate protein intake, our bodies can’t
function well at all.
Protein helps replace worn out cells, transports various substances
throughout the body, and aids in growth and repair.
Consuming protein can also increase levels of the hormone glucagon,
and glucagon can help to control body fat. Glucagon is released when

3
blood sugar levels go down. This causes the liver to break down stored
glycogen into glucose for the body.
It can also help to liberate free fatty acids from adipose tissue – another
way to get fuel for cells.

Structures of common amino acids

The amino acids present in proteins differ from each other in the
structure of their side (R) chains. The simplest amino acid is Glycine, in
which R is a hydrogen atom. In a number of amino acids, R represents
straight or branched carbon chains. One of these amino acids is alanine,
in which R is the methyl group (−CH3). Valine, leucine, and isoleucine,
with longer R groups, complete the alkyl side-chain series. The alkyl side
chains (R groups) of these amino acids are nonpolar; this means that
they have no affinity for water but some affinity for each other.
Although plants can form all of the alkyl amino acids, animals can
synthesize only alanine and Glycine; thus valine, leucine, and isoleucine
must be supplied in the diet.
Two amino acids, each containing three carbon atoms, are derived from
alanine; they are serine and cysteine. Serine contains an alcohol group
(−CH2OH) instead of the methyl group of alanine, and cysteine contains
a mercapto group (−CH2SH). Animals can synthesize serine but not
cysteine or cysteine. Cysteine occurs in proteins predominantly in its
oxidized form (oxidation in this sense meaning the removal of hydrogen
atoms), called cysteine. Cysteine consists of two cysteine molecules
linked by the disulfide bond (−S−S−) that results when a hydrogen atom
is removed from the mercapto group of each of the cysteine. Disulfide
bonds are important in protein structure because they allow the linkage
of two different parts of a protein molecule to—and thus the formation
of loops in—the otherwise straight chains. Some proteins contain small

4
amounts of cysteine with free sulfhydryl (−SH) groups.

Four amino acids, each consisting of four carbon atoms, occur in

proteins; they are aspartic acid, threonine, and methionine. Aspartic
acid and asparagines, which occur in large amounts, can be synthesized
by animals. Threonine and methionine cannot be synthesized and thus
are essential amino acids; i.e., they must be supplied in the diet. Most
proteins contain only small amounts of methionine.
Proteins also contain an amino acid with five carbon atoms (glutamic
acid) and a secondary amine (in proline), which is a structure with the
amino group (−NH2) bonded to the alkyl side chain, forming a
ring. Glutamic acid and aspartic acid are dicarboxylic acids; that is, they
have two carboxyl groups (−COOH).
Proteins usually are almost neutral molecules; that is, they have neither
acidic nor basic properties. This means that the acidic carboxyl ( −COO−)
groups of aspartic and glutamic acid are about equal in number to the
amino acids with basic side chains. Three such basic amino acids, each
containing six carbon atoms, occur in proteins. The one with the
simplest structure, lysine, is synthesized by plants but not by animals.
Even some plants have low lysine content. Arginine is found in all
proteins; it occurs in particularly high amounts in the strongly basic
protamines (simple proteins composed of relatively few amino acids) of
fish sperm. The third basic amino acid is histidine. Both arginine and
histidine can be synthesized by animals. Histidine is a weaker base than

5
either lysine or arginine. The imidazole ring, a five-membered ring
structure containing two nitrogen atoms in the side chain of histidine,
acts as a buffer (i.e., a stabilizer of hydrogen ion concentration) by
binding hydrogen ions (H+) to the nitrogen atoms of the imidazole ring.

The remaining amino acids—phenylalanine, tyrosine, and tryptophan—

have in common an aromatic structure; i.e., a benzene ring is present.
These three amino acids are essential, and, while animals cannot
synthesize the benzene ring itself, they can convert phenylalanine to

6
tyrosine.

Because these amino acids contain benzene rings, they can

absorb ultraviolet light at wavelengths between 270 and 290
nanometers Phenylalanine absorbs very little ultraviolet light; tyrosine
and tryptophan, however, absorb it strongly and are responsible for the
absorption band most proteins exhibit at 280–290 nanometers. This
absorption is often used to determine the quantity of protein present in
protein samples.

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PROTEIN CONTENT IN EGGS:
Eggs are high in protein content and it is
due to this fact that manufacturers of
protein powder often base their
products on egg protein. Egg protein
contains all the essential amino acids
that the human body requires. The egg
white and yolk proteins are high in
nutrients and it can be said that one large egg contains about 6.5 grams
of proteins, out of which egg white protein content is about 3.6 grams.
But yolk contains fats and owing to this fact many people avoid eating
the yolk part. Though chicken eggs are extremely popular as a source of
protein, there are other eggs which are consumed by people from all
parts of the world. Eggs from duck, quails, goose also impart their equal
share in providing protein.

EGGS ALSO CONTAIN ESSENTIAL NUTRIENTS:

 Choline-It is the precursor to acetylcholine, an important brain

chemical (neurotransmitter) for nerve and muscle function.
 Selenium-It plays vital role in DNA synthesis, thyroid hormone
metabolism, reproduction and protection against oxidative
damage and infection.
 Biotin (Vitamin B7)-It commonly benefits hairs and nail, but it also
supports your digestive tract, skin, nerves and metabolism.
 Vitamin A-Vitamin A has many important functions for health,
including cell growth, vision support and immune system support.
 Vitamin B12-(Cobalamin)-It the only vitamin containing a metal
element, cobalt. Among other functions it facilitates the

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 successful transport of oxygen through your blood. It also aid in
DNA production and regulates energy metabolism.
 Vitamin B5 (Pantothenic acid)-It is vital for energy metabolism. It
is also a essential component of Coenzyme A(CoA),an essential
chemical for sustaining life.Carbohydrates,proteins and fats are
broken down and burned into fuel with the help of Coenzyme A.
 Vitamin B2 (Riboflavin)-Riboflavin gives vital support to iron
metabolism, antioxidants and energy production.
 Vitamin D-It helps to keep bone healthy, sugar levels under
control and immune system in great shape.
 Molybdenum (Mo)-Dietary intake of Mo helps sulfur in body in
control.
 Iodine-It supports your thyroid gland and is a fundamental
component of hormone production.
 Phosphorus- It is a key component in making sure that bone stay
healthy and strong and other crucial bodily functions.

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BROWN EGGS VS WHITE EGGS: WHAT'S THE DIFFERENCE?

When it comes to food, the golden

rule is that brown is better. Brown
bread, wheat, pasta, etc. Same is
felt with regard to egg. The only
real difference between brown and
white eggs is that former is
expensive. In nutritional aspect
there is no real difference and difference in Omega-3 fatty acids is
almost negligible.

White eggs are laid by white feathered chickens with white coloured
earlobes while brown ones are laid by brown feathered chicken with
red earlobes. The reason brown eggs cost more is because they come
from chickens that have a big appetite and are expensive to keep.
While their counterparts are cheaper and feed less. There’s another
misconception that brown eggs have harder shells. But there’s no co-
relation between its colour. Eggs laid by younger hens are harder
compared to older ones. This is true for both white and brown eggs.

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PROTEIN CONTENT IN SOYABEANS :
Soybeans are among the best sources of
plant-based protein, making them ideal
for vegan diets. The protein content of
soybeans ranges from 36 to 56% of the
dry weight. One cup of boiled soybeans
(172 g) contains around 29 grams of
protein. The nutritional value of soy
protein is good, although the quality is not quite as high as animal
protein. The main types of protein in soybeans are glycinin and
conglycinin, which make up approximately 80% of the total protein
content. These proteins may trigger allergic reactions in some people.
Consumption of soy protein has been linked with a modest decrease in
cholesterol levels. Soybeans also contain bioactive proteins, such as
lectin and lunasin, which may have anti-cancer properties.

SOYBEANS ALSO CONTAIN ESSENTIAL NUTRIENTS:

Soybeans are a good source of various vitamins and minerals.

 Molybdenum: Soybeans are rich in molybdenum, an essential

trace element, primarily found in seeds, grains and legumes.
 Vitamin K1: The form of vitamin K found in legumes is known as
phylloquinone. It plays an important role in blood clotting.
 Folate: One of the B-vitamins, also known as vitamin B9 or folic
acid. It has various different functions in the body and is
considered to be particularly important during pregnancy.

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 Copper: Dietary intake of copper is often low in Western
populations. Copper deficiency may have adverse effects on heart
health.
 Manganese: A trace element found in most foods and drinking
water. Manganese is poorly absorbed from soybeans because of
their high phytic acid content.
 Phosphorus: Soybeans are a good source of phosphorus, an
essential mineral that is abundant in the Western diet.
 Thiamin: Also known as vitamin B1, thiamin plays an important
role in many body functions.
 Soy fat: Soybeans are rich in fat. In fact, soybeans are classified as
oilseeds and are often used to make soybean oil. The fat content
is approximately 18% of the dry weight, mainly polyunsaturated
and monounsaturated fatty acids, with small amounts of
saturated fat. The predominant type of fat in soybeans is linoleic
acid, accounting for approximately 50% of the total fat content.

 Fibers: Soybeans contain a fair amount of both soluble and

insoluble fibers. The insoluble fibers are mainly alpha-
galactosides, such as stachyose and raffinose. These fibers may
cause flatulence and diarrhea in sensitive individuals. Alpha-
galactosides belong to a class of fibers called FODMAPs, which
may exacerbate the symptoms of irritable bowel syndrome (IBS) .
Despite unpleasant side effects in some people, soluble fibers in
soybeans are generally considered to be healthy. They are
fermented by bacteria in the colon, leading to the formation of
short-chain fatty acids, such as butyrate, which may improve
colon health and cut the risk of colon cancer.

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  Carbohydrates: Being low
in carbohydrates , whole
soybeans are very low on the
glycemic index, which is a
measure of how foods affect
the rise in blood sugar after a
meal. The low glycemic index
makes soybeans particularly
suitable for people with
diabetes.

Other soy bean products include:

 Soy milk: Grinding, soaking and straining soybeans create a

mild-tasting liquid known as soy milk. Soy milk is usually a
suitable replacement for dairy milk. Vanilla and chocolate
soy milk are often sold alongside unflavored soy milk, which
are all typically packaged in aseptic containers. A 1-cup
serving of soy milk has 104 calories, 6 grams of protein and
3.5 grams of fat, on average. Fortified soy milk is a good
source of calcium, iron, vitamin B-12 and vitamin D.

 Tofu: Soybean curd -- or tofu -- is created by curdling soy

with a coagulant. Tofu, which has minimal flavor, can absorb
seasonings and flavorings easily. Firm tofu is dense and
useful in stir fries or soups. Soft tofu is mushier and works in
place of yogurt in smoothies. A 1/2-cup serving of firm tofu
has 88 calories, over 10 grams of protein and 5 grams of fat.
Creamy desserts using tofu are common in grocery stores, as
are plain blocks of tofu with varying firmness. Most Asian
markets carry fresh tofu, which has a smoother texture and
flavor.

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 Soy sauces: Soy sauce is one of the most common soy
products available. This dark brown liquid with a salty taste
is made by fermenting soybeans. Shoyu and tamari are
common varieties of soy sauce and are typically available in
different levels of darkness. A 1-teaspoon serving of tamari
has 4 calories and 335 milligrams of sodium. Vegetable,
meat and tofu dishes often call for soy sauce, but it is even
used in some cookie recipes.

 Soy bean oil: According to The United Soybean Board, most

margarines, shortenings and salad dressings contain
soybean oil. In addition, most of the “vegetable oil” you see
in the grocery store is pure soybean oil. The American Heart
Association lists soybean oil as a safe fat for maintaining
health and longevity. A 1-teaspoon serving of soybean oil
has 40 calories, 4.5 grams of fat and less than 1 gram of
saturated fat. Soybean oil is mostly flavorless, making it a
non-intrusive ingredient in most dishes.

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DETERMINATION OF PROTEIN CONTENT:
Proteins are the fundamental constituents of the body. They are the
major organic constituents of protoplasm and extra-cellular materials.
Different kinds of proteins are specific for different functions. Proteins
may function as enzyme, hormone, receptor; etc.All proteins are
constructed from the same ubiquitous set of 20 amino acids, and
covalently linked with linear sequences which folds, form a 3-D
structure and are modified to attain the active conformation.

The overall protein concentration can be done by following methods:

 Kjeldahl method

The Kjeldahl method was developed in 1883 by a brewer called Johann

Kjeldahl. The food is digested with a strong acid so that is digested so
that it releases nitrogen which can be determined by a suitable titration
technique. The amount of protein present is then calculated from the
nitrogen concentration of the food.

Kjeldahl method is widely used for its high precision and good
reproducibility has made it the major method for the estimation of
protein in food. One of the disadvantages is that it does not give a
measure of the true protein, since all nitrogen in foods is not in the
form of protein. The use of concentrated sulfuric acid at high
temperatures poses a considerable hazard as does the use of some of
the possible catalysts.

 Enhanced Dumas method

Recently, an automated instrumental technique has been developed

which is capable of rapidly measuring the protein concentration of food

15
samples. It was beginning to compete with Kjeldahl due its rapidness. It
doesn’t need toxic chemicals or catalysts and is easy to use. One of the
disadvantages is that it’s expensive and the small sample size makes it
difficult to obtain a representative samples.

A sample of known mass is combusted in a high temperature chamber.

This leads to release of CO2,H2O andN2.These gases are removed by
passing them over columns that absorbs them. The nitrogen content is
then measured by passing the remaining gasses through a column that
has a thermal conductivity detector at the end. Thus the signals from
thermal conductivity detector can be converted to nitrogen content.

 Methods using UV- visible spectroscopy

A number of methods have been devised to measure protein

concentration, which are based on UV- visible spectroscopy. These
methods use either the natural ability of proteins to absorb light or
scatter in the UV.First of all a calibration curve of absorbance (or
turbidity) versus protein concentration is prepared using a series of
protein solution of known concentration. The absorbance of the
solution being analyzed is then measured at the same wavelength
and its protein concentration determined from the calibration curve.
A number of the most commonly used UV- visible spectroscopy
methods for determining the protein
content of foods are listed below:

 Biuret Method

A violet-purplish colour is produced

when cupric ions(Cu2+)interact with
peptide bonds under alkaline conditions.

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The Biuret reagent, which contains all the chemicals required to
carry out the analysis, can be purchased commercially. The Biuret
reagent is made of sodium hydroxide and hydrated copper sulfate,
together with potassium sodium tartarate (added to stabilize the
cupric ions).In the presence of alkaline medium, cupric ions given by
CuSO4 reacts with peptide linkage to form the bluish-violet coloured
complex. The peptide nitrogen atoms form a coordination complex
with the cupric ions. The intensity of colour depends upon the
amounts of protein present in the solution. The Biuret reaction can
be used to assess the concentration of proteins because of peptide
bonds occur with same frequency per amino acid in the peptide. The
intensity of the colour is directly proportional to the protein
concentration, according to the Beer-Lambert law.Dipeptides and
amino acids do not answer this test. Despite its name, the reagent
does not in fact contain Biuret ((H2N-CO-)2NH).The test is named so
because it also gives a positive reaction to the peptide-like bonds in
the Biuret molecule. Biuret reagent mixed with a protein and then
absorbance is read at 540nm.If the solution turns purple, protein is
present and about 5-160mg/mL can be determined. The major
advantage of this technique is that there is no interference from
materials of this technique is that there is no interference from
materials that absorb at lower wavelengths and the technique is less
sensitive to protein type because it utilizes absorption involving
peptide bonds that are common to all proteins rather than specific
side groups. However it has a relatively low sensitivity compared to
other used UV- visible methods.

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  Lowry Method

The Lowry method combines the Biuret reagent with another

reagent (the Folin-Ciocalteau phenol reagent) which reacts tyrosine
and tryptophan residues in proteins. This gives a bluish colour which
can be read somewhere between 500-750nm depending on the
sensitivity required. The reaction combines the reaction of copper
ions with peptide bonds under alkaline conditions with oxidation of
aromatic protein residues. The Lowry method is based on the
reaction of Cu+,
produced by
the oxidation of
peptide bonds,
with Folin-
Ciocalteau
reagent (a
mixture of
phosphotungsti
c acid and
phosphomolybd
ic acid) The
reaction mechanism is still not understood well, but involves
reduction of the Folin-Ciocalteau reagent and oxidation of aromatic
residues (mainly tryptophan, also tyrosine).The total protein
concentration is measured using colorimetric techniques. This test
was devised by Oliver H Lowry in 1940.This method is more sensitive
to low concentrations of proteins than the Biuret methods.

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METHODOLOGY
 Preparation of Reagent: Biuret method requires Biuret reagent
which is made by dissolving 3g of copper sulphate in 9g of
sodium potassium tartarate in500ml of 0.2N NaOH solution. To
this 5g of potassium iodide is added and made upto 100ml in
0.2N NaOH.
 Preparation of BSA Standard solution: Bovine serum albumin
is used as standard A BSA stock is prepared with a
concentration of 10mg/ml by dissolving 1000mg of BSA in
100ml of distilled water

Preparation sample solutions-

1. Preparation of Egg white solution: Approximately 5gm of egg

white of both brown and white shelled egg is separated and
weighed.0.1N of NaOH is prepared for (both white & brown
shelled egg) and the above weighed egg white is dissolved in it.
About 1ml each is drawn from the stock for experimental
purpose.
2. Preparation of solution of boiled egg: About 32gm of boiled egg
white is ground to get homogenized mixture. Then it is filtered
using water. The filtrate is used for protein estimation.
3. Preparation of solution of Soy chunks: For experiment purpose
Soy chunks are used since they are lack other components which
may interfere with the experiment. Approximately 50gms of Soy
chunks are initially boiled with water and allowed to cool. Then it
is homogenized. From the mixture about 1g is taken and filtered
using water. The filtrate is used for experimental purpose.

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PROCEDURE

1) Standard protein solution is prepared by pipetting 0.2,0.4,0.6,0.8

and so on of BSA and then distilled water about 3.8,3.6,3.4,3.2
and 3.0 is added to make the volume upto 4ml.To 1ml of test
samples, 3ml of distilled water is added.

2) To all the test tubes 6ml each of Biuret reagents is added.

3) The contents are mixed well with help of Vortex mixer.

4) The test tubes are incubated in incubator for 10mins.

5) The absorbance or optical density is measured at 520nm.

6) The values of O.D are plotted on graph and the unknown protein
concentration is found out.

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OBSERVATION AND CALCULATION

TABULAR COLUMN:

Volume of Concentration Volume Volume of Optical

Standard of of Biuret Density
protein(ml) protein(mg/ml) water(ml) reagent(ml) in nm

1 0.0 - 4 6 0.0
2 0.2 2 3.8 6 0.04
3 0.4 4 3.6 6 0.10

Incubate at 37ᴼC for 10 mins

4 0.6 6 3.4 6 0.15
5 0.8 8 3.2 6 0.20
6 1.0 10 3.0 6 0.25
7 1.2 12 2.8 6 0.35
8 1.4 14 2.6 6 0.40
9 1.6 16 2.4 6 0.63
10 1.8 18 2.2 6 0.66
T1 1 W 3.0 6 0.54
T2 1 x 3.0 6 0.43
T3 1 Y 3.0 6 0.33
T4 1 z 3.0 6 0.36
T1- Test (Soya Chunks)

T2- Test (Boiled Egg)

T3- Test (Raw egg white of Brown shelled egg)

T4- Test (Raw egg white of White shelled egg)

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22
1) Sample Z (white part of white shelled egg)

From the graph, Protein concentration is found out to be 14.3 mg/ml

4 ml solution=14.3 mg of protein

1ml of test solution =14.3/4=3.575 mg of protein

100ml of the original solution contains 5g of egg white

Therefore, 1 ml of solution is drawn, therefore the amount of egg white in it

=5 x 1 /100=0.05g of egg white

Therefore 0.05g of egg white contains 3.575mg of protein

OR

So, 32gms of egg white contains

= 32 x 0.003575/0.05g =2.288~ 2.29g of proteins

2) Sample Y (white part of brown shelled egg)

From the graph the protein concentration is found out to be 13.3 mg/ml

4 ml of test solution =13.3 mg of proteins

1ml of the test solution = 13.3/4 =3.325 mg of proteins

100 ml of the original solution contains 5g of egg white

Therefore 1ml of solution is drawn therefore the amount of egg white in it

= 5x 1 /100 = 0.05g of egg white

Therefore 0.05g of egg white contains 3.325 mg of proteins

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100 ml of the original solution contains 5 g of egg white.

Therefore 1 ml of solution is drawn therefore the amount of egg white in it.

= 5 x 1 /100 = 0.05g of egg white.

Therefore 0.05g of egg white contains 3.325 mg of proteins

OR

0.05g of egg white contains 0.00325g of proteins

Therefore 32 g of egg white contains

32 x 0.00325/0.05 = 2.128g~ 2.19 g of proteins

3) Sample W (extract of Soya chunks)

From the graph, the protein concentration is found to be 21.2 mg/ml.

4 ml of test solution =21.2 mg of proteins

1 ml of test solution =21.2/4=5.3 mg of proteins

100 ml of original solution contains 1 g of homogenized soya chunks.

Therefore 1 ml of test solution is drawn from the original solution, therefore

the amount of homogenized soya chunks in it.

1 x 1 /100 = 0.01 g of homogenized soya chunks

Therefore 0.01 g of homogenized soya chunks contains 5.3mg of proteins or

0.0053g of proteins

Therefore 50 of soya chunks contains

50 x 0.0053/0.01 = 26.5g ~27g of proteins

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4) Sample x (Boiled egg white)

From the graph the protein concentration is found out to be 17.2 mg/ml

4ml of test solution = 17.2 mg of proteins

1ml of test solution = 17.2 /4 =4.3 mg of proteins

32 g of egg white was homogenized and 26 ml of filtrate was obtained.

1ml of test solution contained 4.3 mg of protein or 0.0043g of proteins.

Therefore 26 ml of test solution contains

0.0043 X 26 =0.1118 g of proteins

Therefore 32 g of egg white contains

32 X 0.1118 =3.5 ~ 4g of proteins.

25
RESULTS

The amount of protein content or concentration in the

following food items are:
a. White part of white shelled egg =2.29g
b. White part of brown shelled egg =2.19 g
c. White part of boiled egg =4g
d. Soya chunks =27g

According to the tests that were performed, it was found that

soy chunks had the highest protein content compared to the
brown or white shelled eggs.
It was concluded that there was not much difference between
the white and brown shelled eggs.
On the contrary, the whites of the boiled eggs showed high
protein concentration as compared to the raw eggs.

26
DISCUSSION
Eggs are high in protein content and it is due to this fact that
manufacturers of protein powders often base their products on egg
protein. Egg protein contains all the essential amino acids that the
human body requires. The egg white and yolk proteins are high in
nutrients and it can be said that one large egg contains about 6.5 grams
of protein, out of which egg white protein content is about 3.6 grams.
Many people tend to avoid eating egg yolk as it also contains fats along
with protein.

In terms of intake, the digestibility and absorption of egg protein is much

greater in cooked eggs than in raw. One study, published in The Journal
of Nutrition, found that the availability of egg protein is 91% with cooked
eggs and only 50% with raw eggs. This means a raw egg would only
provide 3 grams of digestible protein compared to eating a whole cooked
egg, which contains almost 6 grams of protein.

The higher digestibility of protein in cooked eggs is likely due to

structural changes caused by cooking. Another reason for the difference
in digestibility may be Trypsin Inhibitors. Trypsin is an enzyme that
breaks down proteins and may be blocked by enzymes in raw eggs. Heat

27
will destroy some of the functional properties of protein, such as
inhibiting Trypsin, so that the protein is more readily digested.

Cooking your eggs can also help prevent food borne illness. A small
percentage of unpasteurized eggs may contain salmonella. Cooking eggs
to temperatures of 160 degrees or above (or until the yolk is firm or fully
cooked) will kill salmonella, and reduce risk of food poisoning.

There are mainly two types of eggs found in the market; White eggs, and
brown eggs. White eggs are laid by white-feathered chickens with white
or light coloured earlobes while the brown ones are laid by brown-
feathered chickens with red earlobes. It has been observed that there are
more white eggs in the market than brown ones as breeding and raising
white-feathered chickens is much cheaper. Brown chickens are bigger in
size and have a big appetite. Hence, they are expensive to keep.
It has been said that there is no real difference in nutritional value
between brown and white eggs. The only real difference is that brown
eggs are more expensive than the white ones. Their nutritional profile,
quality and type is undetermined. Brown eggs may have more Omega-3
fatty acids but the difference is almost negligible.

Brown and white eggs do taste different. But that has nothing to do with
quality or nutritional profile of the egg but more with the diet of the
chicken that laid it. The chickens are fed a different kind of diet which
impacts the quality and taste of the egg. So if a brown chicken and a
white chicken were fed with the same kind of food, the difference in taste
would go unnoticed.

Soy chunks are exceptional sources of essential nutrients providing in a

100gms serving high contents of the Daily Value (DV) especially for
Protein (36%DV), dietary fiber (37%), including several minerals and
vitamins like iron, manganese, phosphorous, potassium, zinc and several
vitamin B complexes including vitamin K.For human consumption,

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soybeans must be cooked with wet heat to destroy the Trypsin
inhibitors. Soy protein are essentially identical to the protein of other
legume seeds and pulses.

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GALLERY

Fig1: 4 Samples: Solutions of soya chunks, egg white of raw egg and white
part of boiled egg

Fig3: Test tubes containing test samples.

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Fig 4: Standard protein solutions

Fig 5& 6: Colorimetric estimation

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BIBLIOGRAPHY
 www.iloveindia.com
 www.healtyeating.sfgate.com
 www.eggnutritioncenter.org
 www.bodybuilding.com
 www.food.ndtv.com
 www.scribd.com
 www.wikipedia.org
 www.augusta.edu
 shinaebiochem.blogspot.in
 elte.prompt.hu

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