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Chemistry Investigatory project

Analysis on Presence of Proteins in


Different Food Items
SUBMITTED TO
Mrs. DIVYA JYOTI
NAGOTRA

SUBMITTED BY
DEVENDRA YADAV
CLASS 12 A

Chemistry Investigatory Project

CERTIFICATE
This is to certify that DEVENDRA YADAV a
student of class XII has successfully
completed the research analysis project
on
the topic Analysis of Food Stuff for the
presence of Proteins under the guidance of
Mrs. DIVYA JYOTI NAGOTRA (Subject
teacher).
This project is absolutely genuine and does not
indulge in plagiarism of any kind.
The references taken in making this project
has been declared in bibliography.
(Subject Teacher)
Mrs.DIVYA JYOTI
NAGOTRA

(Principal)

Mrs.NEELAM
MALVIYA

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ACKNOWLEDGEMENT
Success is the progressive realization of a
worthy goal, says our respected Principal, I wish my
deep gratitude to my Principal Mrs. NEELAM
MALVIYA & respected teachers Mrs. DIVYA JYOTI
NAGOTRA, whose eloquent guidance and valuable
suggestions have been indispensable in bringing out
this assigned project successfully. It is through
there practical knowledge, there suggestion and help
offered by them from time to time that brought
great confidence in taking up this work and
synchronizing my efforts in accomplishment of the
project work.
I also express my gratitude to the Laboratory
Assistant Mr.Ramnarayan Sir, who has greatly
helped me in completion of
experiments and this
project.

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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
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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
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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

replication, responding

to

reactions, DNA

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.

linear

chain

of

amino

acid

residues

is

called

a polypeptide. A protein contains at least one long


polypeptide. Short polypeptides, containing less than 20
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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 andin

certain archaeapyrrolysine. 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

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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 12 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

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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- (-),
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beta- (-), gamma- (-) or delta- (-) 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 PROTIENS
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 -helix, -sheet and turns.
Because secondary structures are local, many regions of

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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
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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.

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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,

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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 nonessential 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
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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
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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
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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
- Millions 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.

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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.

Chemistry Investigatory Project

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.
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Note the observation. The appearance of deep yellow


colour confirms the presence of proteins.
Ninhydrins 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.

Millons Test:

Take 2ml meshed sample of taken food in a test tube.

Add 2 drops of Millons Reagent and boil the


content.
Note the observation. The white ppt changes to
brick red on boiling.
OBSERVATIONS:
Sn. Test
performed
1. Buiret Test
2.
3.

4.

Xanthoprotein
test
Ninhydrin
Test
Millions Test

Soyabean
Violet
colour
Yellow
ppt
Intense
blue
colour
Brick red
ppt

Egg
white
Violet
colour
Yellow
ppt
Intense
blue
colour
Brick
red ppt

Bread

Nuts

Inference

Violet
colour
Yellow
ppt
Intense
blue
colour
Brick
red ppt

Violet
colour
Yellow
ppt
Intense
blue
colour
Brick
red ppt

Protein
Present
Protein
Present
Protein
Present

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Protein
Present

RESULTS & CONCLUSION :During

the

analysis

experiment,

the

given

sample

of

Soybeans, Nuts, Bread, Egg white the contain the


Proteins

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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

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