ANALYSIS ON PRESENCE OF

PROTEINS IN DIFFERENT
FOOD ITEMS
A PROJECT REPORT IN CHEMISTRY (043) SUBMITTED IN PARTIAL
FULFILLMENT OF THE REQUIREMENT FOR THE COMPLETIOM OF

AISSCE 2024-2025
BY
K.BARANI
AISSCE Roll No: ……………………………..

Under the supervision of

Miss. A.DHANALAKSHMI
PGT Chemistry
JAIRAM PUBLIC SCHOOL
Chinnathirupathi (Po),
Salem, Tamilnadu.

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 JAIRAM PUBLIC SCHOOL
CBSE-SENIOR SECONDARY,
Chinnathirupathi (Po), Salem-636008

CERTIFICATION

This project entitled ANALYSIS ON PRESENCE OF

PROTEINS IN DIFFERENT FOOD ITEMS is the investigatory
project workin chemistry (043), successfully completed by master,
K.BARANI student of class XII, Jairam Public School, Salem,
with AISSCE Roll NO. …………….under the supervision of Miss.
A.DHANALAKSHMI (PGT Chemistry), for the partial fulfillment
ofrequirements for the course completion in pursuance of AISSCE
2024-2025.

…………………… ..…..………………
Teacher In-charge Principal

……………………
Practical Examiner School Stamp

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 ACKNOWLEDGEMENT

I have taken effect in this project. However it would not have

been possible without the kind support and help of many individual.

I would like Principal sir, Mr. Paul Francis Xavier and school
for providing me with facilities required to do my project.

I am highly indebted to my chemistry teacher,

Miss.A.Dhanalakshmi, for her invaluable guidance which has
sustained my efforts in all these stages of this project work.

I would also like to thanks my parents for their continuous

support and encouragement.

My thanks and appreciation also goes to my fellow classmates

and to the people who have willingly helped me out with their
abilities.

K.BARANI

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 INDEX

1:- What are Proteins?

2:- What are Amino Acids?

3:- Structures of Proteins.

3.1 :-Primary Structure.

3.2 :- Secondary Structure.
3.3 :- Tertiary Structure.
3.4 :- Quaternary Structure.

4:-Types of Amino Acids.

4.1 :-Essential Amino Acids

4.2 :-Semi Essential Amino Acids
4.3 :-Non Essential Amino Acids

5:– Diseases caused by deficiency of Proteins.

5.1 :- Marasmus
5.2 :- Kwashiorkor
5.3 :- Deficiencies of Protein C and Protein S
5.4 :- Cachexia
6:- Tests for Proteins.

7:-Sources of Proteins.

7.1 :-Seafood
7.2 :-White-Meat Poultry
7.3 :-Milk, Cheese & Yogurt
7.4 :-Egg
7.5 :-Beans
7.6 :-Pork Tenderloin
 PROTEINS

1-What are protiens?

Proteins large biomolecules, or macromolecules, consisting of one or more

long chains of amino acidresidues. Proteins perform a vast array of functions
within organisms, including catalysing metabolic reactions, DNA
replication, responding to stimuli, and transporting molecules from one
location to another. Proteins differ from one another primarily in their
sequence of amino acids, which is dictated by the nucleotide sequence of
their genes, and which usually results in protein folding into a specific three-
dimensional structure that determines its activity.

A linear chain of amino acid residues is called a polypeptide. A protein

contains at least one long polypeptide. Short polypeptides, containing less
than 20–30 residues, are rarely considered to be proteins and are commonly
called peptides, or sometimes oligopeptides. The individual amino acid
residues are bonded together by peptide bonds and adjacent amino acid
residues. The sequence of amino acid residues in a protein is defined by
the sequence of a gene, which is encoded in the genetic code. In general, the
genetic code specifies 20 standard amino acids; however, in certain
organisms the genetic code can include selenocysteine and—in
certain archaea—pyrrolysine. Shortly after or even during synthesis, the
residues in a protein are often chemically modified by post-translational
modification, which alters the physical and chemical properties, folding,
stability, activity, and ultimately, the function of the proteins. Sometimes
proteins have non-peptide groups attached, which can be called prosthetic
groups or cofactors. Proteins can also work together to achieve a particular
function, and they often associate to form stable protein complexes.

Once formed, proteins only exist for a certain period of time and are
then degraded and recycled by the cell's machinery through the process
of protein turnover. A protein's lifespan is measured in terms of its half-
life and covers a wide range. They can exist for minutes or years with an
average lifespan of 1–2 days in mammalian cells. Abnormal and or
misfolded proteins are degraded more rapidly either due to being targeted for
destruction or due to being unstable.

Like other biological macromolecules such as polysaccharides and nucleic

acids, proteins are essential parts of organisms and participate in virtually
every process within cells. Many proteins
are enzymes that catalyse biochemical reactions and are vital to metabolism.
Proteins also have structural or mechanical functions, such
as actin and myosin in muscle and the proteins in the cytoskeleton, which
form a system of scaffolding that maintains cell shape. Other proteins are
important in cell signaling, immune responses, cell adhesion, and the cell
cycle. In animals, proteins are needed in the diet to provide the essential
amino acids that cannot be synthesized. Digestion breaks the proteins down
for use in the metabolism.

2 -What are amino amino acids?

Amino acids are biologically important organic

compounds containing amine (-NH2) and carboxyl (-COOH) functional
groups, along with a side-chain (R group) specific to each amino acid.[ The
key elements of an amino acid are carbon, hydrogen, oxygen, and nitrogen,
though other elements are found in the side-chains of certain amino acids.
About 500 amino acids are known (though only 20 appear in the genetic
code) and can be classified in many ways. They can be classified according
to the core structural functional groups' locations as alpha- (α-), beta- (β-),
gamma- (γ-) or delta- (δ-) amino acids; other categories relate
to polarity, pH level, and side-chain group type (aliphatic, acyclic, aromatic,
containing hydroxyl or sulfur, etc.). In the form of proteins, amino acids
comprise the second-largest component (water is the largest) of
human muscles, cells and other tissues. Outside proteins, amino acids
perform critical roles in processes such as neurotransmitter transport
and biosynthesis.
 3 – Structure of proteins

Most proteins fold into unique 3-dimensional structures. The shape into
which a protein naturally folds is known as its native
conformation. Although many proteins can fold unassisted, simply through
the chemical properties of their amino acids, others require the aid of
molecular chaperones to fold into their native states. Biochemists often refer
to four distinct aspects of a protein's structure:

3.1:-Primary structure:- The amino acid sequence. A protein is

a polyamide.

3.2:- Secondary structure :- Regularly repeating local structures stabilized

by hydrogen bonds. The most common examples are the α-helix, β-
sheet and turns. Because secondary structures are local, many regions of
different secondary structure can be present in the same protein molecule.

3.3:- Tertiary structure :- The overall shape of a single protein molecule;

the spatial relationship of the secondary structures to one another.
Tertiary structure is generally stabilized by nonlocal interactions, most
commonly the formation of a hydrophobic core, but also through salt
bridges, hydrogen bonds, disulfide bonds, and even posttranslational
modifications. The term "tertiary structure" is often used as synonymous
with the term fold. The tertiary structure is what controls the basic
function of the protein.

3.4:- Quaternary structure:- The structure formed by several protein

molecules (polypeptide chains), usually called protein subunits in this
context, which function as a single protein complex.
Proteins are not entirely rigid molecules. In addition to these levels of
structure, proteins may shift between several related structures while they
perform their functions. In the context of these functional rearrangements,
these tertiary or quaternary structures are usually referred to as
"conformations", and transitions between them are called conformational
changes. Such changes are often induced by the binding of
a substrate molecule to an enzyme's active site, or the physical region of the
protein that participates in chemical catalysis. In solution proteins also
undergo variation in structure through thermal vibration and the collision
with other molecules.
Proteins can be informally divided into three main classes, which correlate
with typical tertiary structures: globular proteins, fibrous proteins,
and membrane proteins. Almost all globular proteins are soluble and many
are enzymes. Fibrous proteins are often structural, such as collagen, the
major component of connective tissue, or keratin, the protein component of
hair and nails. Membrane proteins often serve as receptors or provide
channels for polar or charged molecules to pass through the cell membrane.
A special case of intramolecular hydrogen bonds within proteins, poorly
shielded from water attack and hence promoting their own dehydration, are
called dehydrons.
 4 – Types of amino acids

Amino acids are organic compounds which contain at least one amino group
(-NH2) and a carboxy (-COOH) group. In the human genome, 20 amino
acids are created to build proteins and therefore termed proteinogen. Besides
this, there are approximately 250 amino acids which do not form proteins.
These are used to form sugar for example.

The 20 proteinogen amino acids are also called standard amino acids, which
can be divided into three groups: essential, semi-essential and non-essential.

4.1 :- ESSENTIAL AMINO ACIDS:- Eight amino acids are essential for
humans, as the body cannot produce them by themselves, and they have to
be supplied externally. These are: isoleucine, leucine, lysine, methionine,
phenylalanine, threonine, tryptophan and valine.

4.2 :- SEMI ESSENTIAL AMINO ACIDS:-Arginine and histidine form the

group of so-called semi-essential amino acids. They have to be consumed in
the diet under certain circumstances.

4.3 :- NON ESSENTIAL AMINO ACIDS:- The ten non-essential amino

acids are able to be produced in the body. The following amino acids fall
into this category: alanine, asparagine, aspartic acid, cysteine, glutamine,
glutamic acid, glycine, proline, serin and tyrosine.
It should be noted that the grouping ‘essential’ and ‘non-essential’ does not
mean that one group more important is that the other. This is because the
division of the two does not assess whether the body has sufficient supply of
the amino acids in question at its disposal. The protein requirement can
differ greatly from person to person. The amount of semi-essential and non-
essential amino acids produced by the body itself depends on many different
factors, such as age, mental and/or physical stress or distress situations.
These determine the various amino acid levels required to stay fit and
healthy.
 5 – Diseases caused by deficiency of proteins
5.1:- Marasmus

Marasmus is a disease caused by a severe deficiency of protein and calories

that affect infants and very young children, often resulting in weight loss
and dehydration. Marasmus can develop into starvation and cause fatality
caused by a lack of essential nutrients. People with marasmus appear bony
with little muscle tissue, according to Food4Africa.

5.2:- Kwashiorkor

Kwashiorkor is a disease caused by a severe deficiency of protein in diets

that contain calories mostly from carbohydrates such as yams, rice and
bananas. It usually affects older children. People with kwashiorkor appear
puffy in the abdomen area from retention of fluid, according to the
University of Maryland Medical Center. Common symptoms of both
marasmus and kwashiorkor include fatigue, irritability, diarrhea, stunted
growth and impairment of cognition and mental health.

5.3:- Deficiencies of Protein C and Protein S

Deficiencies of protein C and protein S are inherited conditions that cause

abnormal blood clotting, according to Medline Plus. Deficiency of protein C
occurs in about 1 out of 300 people. Deficiency of protein S affects 1 in
20,000 people. Symptoms for these deficiencies include redness, pain,
tenderness or swelling in the affected area. People with these protein
deficiencies need to be careful about activities that increase risk of blood
clots, such as prolonged sitting, bed rest, and long-time travel in cars and
airplanes. Research by A. Hooda published in the "Annals of Indian
Academy of Neurology" in 2009 discovered that protein S deficiency causes
ischemic stroke.

5.4:- Cachexia
Cachexia is a condition that involves protein deficiency, depletion of skeletal
muscle and an increased rate of protein degradation, according to research by
D.P. Kotler published in the "Annals of Internal Medicine" in 2000.
Cachexia causes weight loss and mortality and is associated with cancer,
AIDS, chronic kidney failure, heat disease, chronic obstructive pulmonary
disease and rheumatoid arthritis, according to J.E. Morley in the "American
Journal of Clinical Nutrition." Patients with malignant cancer of the
stomach, colon, liver, billiary tract and pancreas experience under nutrition
from reduced intake of protein, calories and micronutrients, and have fatigue
and a negative nitrogen balance as a result of loss of muscle mass from
cachexia, according to J. Ockenga in "Alimentary Pharmacology and
Therapeutics" in 2005.

6:-Tests for Proteins in food items :

The presence of Proteins in food stuffs can be detected by

performing following tests :
- Xanthoprotein test
- Biuret test
- Million’s test
- Ninhydrin test
 7:-Sources of Proteins.
7.1 :-Seafood
Seafood is an excellent source of protein because it's usually low in fat. Fish
such as salmon is a little higher in fat, but it is the heart-healthy kind: it has
omega-3 fatty acids.

7.2 :-White-Meat Poultry

Stick to the white meat of poultry for excellent, lean protein. Dark meat is a
little higher in fat. The skin is loaded with saturated fat, so remove skin
before cooking.

7.3 :-Milk, Cheese, and Yogurt

Not only are dairy foods like milk, cheese, and yogurt excellent sources of
protein, but they also contain valuable calcium, and many are fortified
with vitamin D. Choose skim or low-fat dairy to keep bones and teeth strong
and help prevent osteoporosis.

7.4 :-Eggs
Eggs are one of the least expensive forms of protein. The
American Heart Association says normal healthy adults can safely enjoy an
egg a day.

7.5 :-Beans
One-half cup of beans contains as much protein as an ounce of broiled steak.
Plus, these nutritious nuggets are loaded with fiber to keep you feeling full
for hours.

7.6 :-Pork Tenderloin

This great and versatile white meat is 31% leaner than it was 20 years ago.
 EXPERIMENT

AIM:-
To analyze the presence of proteins in a sample of Soybeans, Egg white,
Nuts, Bread.

APPARATUS REQUIRED:-
 Test tubes
 Test tube stand

CHEMICALS REQUIRED:-
 Reagents as required for testing and analysis of proteins for various test.
 A sample of taken food in crushed with water.

PROCEDURE:-
Biuret Test :
 Take 2ml meshed sample of taken food in a test tube.
 Add few drops of sodium hydroxide solution.
Add very dilute solution of copper sulphate drop--wise.
 Note the observation. The appearance of violet colour confirms the
presence of proteins.
Xanthoprotein Test :
 Take 2ml meshed sample of taken food in a test tube.
 Add few drops of 2ml of conc. Nitric acid. Shake for some time and
keep aside.
 Note the observation. The appearance of deep yellow colour confirms
the presence of proteins.
Ninhydrin’s Test:-
 Take 2ml meshed sample of taken food in a test tube.
 Add 2 few drops of Ninhydrin Solution and boil the content.
  Note the observation. The appearance of intense blue colour confirms
the presence of proteins.
Millon’s Test:-
 Take 2ml meshed sample of taken food in a test tube.
 Add 2 drops of Millon’s Reagent and boil the content.
 Note the observation. The white ppt changes to brick red on boiling.
OBSERVATIONS:

Sn. Test Soyabean Egg Bread Nuts Inference

performed white
1. Buiret Test Violet Violet Violet Violet Protein
colour colour colour colour Present
2. Xanthoprotein Yellow Yellow Yellow Yellow Protein
test ppt ppt ppt ppt Present
3. Ninhydrin Test Intense Intense Intense Intense Protein
blue blue blue blue Present
colour colour colour colour
4. Million’s Test Brick red Brick red Brick Brick Protein
ppt ppt red ppt red ppt Present

RESULTS & CONCLUSION :-

During the analysis experiment, the given sample of Soybeans, Nuts,
Bread, Egg white the contain the Proteins
 BIBILIOGRAPHY

 NCERT Text book on Chemistry

 Together with Lab Manual Chemistry - Class – XII

 Arya Publications on Chemistry laboratory Manual

 Dictionary of Science

 www.Wikipedia.com
 www.google.com
 www.scribd.com
 www.amrita.olabs.edu.in