Unit I Structure and Function of Biomolecules Nep 2020

ZOOLOGY
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UNIT I
STRUCTURE & FUNCTION OF BIOMOLECULES
CONTENTS
 Carbohydrates
 Amino Acids
 Proteins
 Lipids
 Fatty Acids
 Enzymes
DR. WKB’S ZOOLOGY STUDY MATERIAL
UG SEMESTER-I UNDER NEP-2020 (ZOOLOGY)

AUTHORED BY: DR. WAHIED KHAWAR BALWAN
M.Sc., Ph.D., D.Litt., D.Sc., PDF-H, FZSI, FSLSc., FAELS, FBPS, FSASS, FABRF, FGESA, FC-ISCA, FIARA, FGT, FIIOR, FIOASD
Senior Asstt. Professor Zoology, Higher Education Department, Jammu and Kashmir
E-Mail: wahied_kb@yahoo.co.in
Mob. No.: +91-94193-69557
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ZOOLOGY SEMESTER-I NEP-2020 (UNIT-I : STRUCTURE & FUNCTION OF BIOMOLECULES) BY DR. WAHIED KHAWAR BALWAN
Biomolecule is any molecule that is of carbohydrates are potatoes, maize, milk,
produced by a living organism, including popcorn and bread etc.
large molecules such as protein, Classification of Carbohydrates
polysaccharides, lipids and nucleic acids as Carbohydrates are classified into two
well as small molecules such as primary types namely small (monosaccharides and
metabolites, secondary metabolites and oligosaccharides) and complex
natural products. A more general name for (polysaccharides).
this class of molecule is biogenic substance. Monosaccharides
Biomolecules which are larger in size, They are simple sugars. They cannot
have complex structures and high be hydrolysed into simple sugars. They are
molecular weight (usually 10,000 Daltons) sweet in taste and soluble in water. For
are called macromolecules like Example, Glucose, Fructose, Galactose etc.
carbohydrates, proteins, lipids, nucleic Oligosaccharides
acids etc. Biomolecules which are smaller in They are sugars which yield 2 to 10
size, having low molecular weight (18-1800 monosaccharides on hydrolysis. They are
Daltons) are called micromolecules. They sweet in taste and soluble in water e.g.,
include water, gases, minerals, amino Maltose (formed of two molecules of
acids, simple sugars, nucleotides etc. glucose), Lactose (formed of galactose and
CARBOHYDRATES glucose), Sucrose (formed of glucose and
fructose) etc. Depending upon the number
Carbohydrates are defined as
of sugars, oligosaccharides are classified
optically active polyhydroxy aldehydes or
into disaccharides (having two
ketones or substances giving polyhydroxy
monosaccharide unit), trisaccharide
aldehydes or ketones on hydrolysis.
(having three monosaccharide units and so
Carbohydrates are hydrates of carbon.
on.
They contain carbon, hydrogen and oxygen
Polysaccharides
in the ratio of 1:2:1. Carbohydrates are
They have large number of
represented by the general formula
monosaccharides joined together by
Cn(H2O)n. They are also called saccharides
glycosidic bond. Polysaccharides are of two
as their basic component is sugar.
types namely Homopolysaccharide and
SOURCES OF CARBOHYDRATES
Hetropolysaccharide.
Carbohydrates are an important part
 Homopolysaccharide: It is formed by the
of any human‟s diet. Some common sources
linking of a single type of monosaccharides.
By Dr. Wahied Khawar Balwan, Senior Assistant Professor in Zoology, Higher Education Department, Jammu & Kashmir, India WKB 1

On hydrolysis, they yield only one type of  Glucose is named as D (+)-glucose, D
monosaccharide e.g. Starch, Glycogen, represents the configuration whereas
Inulin, cellulose, pectin, chitin etc. (+) represents the dextrorotatory nature
 Heteropolysaccharides: It is composed of of the molecule.
a mixture of monosaccharides. On  The ring structure of glucose can explain
hydrolysis, they yield a mixture of many properties of glucose which
monosaccharides e.g. Hyaluronic acid, cannot be figured by open-chain
Chondroitin, Heparin, Agar agar etc. structure.
STRUCTURE OF CARBOHYDRATES  The two cyclic structures differ in the
Glucose configuration of the hydroxyl group at

C1 called anomeric carbon. Such
One of the most important
isomers i.e. α and β form are known as
monosaccharides is glucose. The two
anomers.
commonly used methods for the
 The cyclic structure is also called
preparation of glucose are
1. From Sucrose: If sucrose is boiled pyranose structure due to its analogy
with pyran.
with dilute acid in an alcoholic
The cyclic structure of glucose is given
solution then we obtain glucose and
below:
fructose.
2. From Starch: We can obtain glucose
by hydrolysis of starch and by
boiling it with dilute H2SO4 at 393K
under elevated pressure.
Fig.: Structure of Monosaccharides

Fructose
It is an important ketohexose. The
Fig.: Glucose
molecular formula of fructose is C6H12O6
 Glucose is also called aldohexose and
and contains a ketonic functional group at
dextrose and is abundant on earth.

carbon number 2 and has six carbon atoms Lactose
in a straight chain. The ring member of Commonly it is called milk sugar as
fructose is in analogy to the compound this disaccharide is found in milk. It is made
furan and is named furanose. The cyclic up of Beta-D-galactose and β -D-glucose.
structure of fructose is shown below: The bond is between the first carbon of
galactose and the fourth carbon of glucose.
This is also a reducing sugar.
Fig.: Structure of Monosaccharides

Sucrose
Sucrose being dextrorotatory in
nature gives dextrorotatory glucose as well
as laevorotatory fructose on hydrolysis. The
overall mixture is laevorotatory and this is
because the laevorotation of fructose (-92.4)
is more than the dextrorotation of glucose
(+52.5).
Maltose
Fig.: Structure of Disaccharides
Maltose is also one of the
Starch
disaccharides which have two α -D-glucose
units which are connected by the first Starch is a polymer consisting of D-
carbon of the glucose and also linked to the glucose units. Starches (and other glucose
fourth carbon of another glucose unit. In the polymers) are usually insoluble in water
solution, a free aldehyde can be produced because of the high molecular weight, but
at the first carbon of the second glucose of they can form thick colloidal suspensions
the solution and it is a reducing sugar as it with water.
shows reducing properties. Starch is a storage compound in

plants, and made of glucose units. It is a

homopolysaccharide made up of two broken down by glycolysis/ Kreb‟s
components: amylose and amylopectin. cycle to yield ATP.
Most starch is 10-30% amylose and 70-90% 2. Glucose is the source of storage of
amylopectin. Amylose – a straight chain energy. It is stored as glycogen in
structure formed by 1, 4 glycosidic bonds animals and starch in plants.
between α-D-glucose molecules. 3. Stored carbohydrates act as energy
source instead of proteins.
4. Carbohydrates are intermediates in
biosynthesis of fats and proteins.
The amylose chain forms a helix. This 5. Carbohydrates aid in regulation of
causes the blue colour change on reaction nerve tissue and are the energy
with iodine. Amylose is poorly soluble in source for brain.
water, but forms micellar suspensions. 6. Carbohydrates get associated with
Amylopectin-a glucose polymer with lipids and proteins to form surface
mainly α - (1→4) linkages, but it also has antigens, receptor molecules,
branches formed by α -(1→6) linkages. vitamins and antibiotics.

7. They form structural and protective
components, like in cell wall of plants
and microorganisms.
8. In animals they are important
constituent of connective tissues.
9. They participate in biological
Amylopectin causes a red-violet transport, cell-cell communication
colour change on reaction with iodine. This and activation of growth factors.
change is usually masked by the much 10. Carbohydrates that are rich in fibre
darker reaction of amylose to iodine. content help to prevent constipation.
BIOLOGICAL IMPORTANCE OF 11. Also they help in modulation of

immune system.
CARBOHYDRATES
1. Carbohydrates are chief energy
AMINO ACIDS
source, in many animals, they are Amino Acids are the organic
instant source of energy. Glucose is compounds that combine to form proteins,
hence they are referred to as the building

components of proteins. These 3. In taste, few Amino acids are sweet,
biomolecules are involved in several tasteless, and bitter.
biological and chemical functions in the 4. Most of the amino acids are soluble
human body and are the necessary in water and are insoluble in
ingredients for the growth and organic solvents.
development of human beings. There are Sources of Amino Acids
about 300 amino acids that occur in nature. Amino acids play an important role in
Amino acids are organic compounds performing several biological and chemical
containing the basic amino groups (-NH2) functions in different parts of our body,
and carboxyl groups (-COOH). The including building and repairing the
ingredients present in proteins are amino tissues, the formation and function
acids. Both peptides and proteins are long of enzymes, food digestion, the
chains of amino acids. Altogether, there are transportation of molecules, etc. Our body
twenty amino acids, which are involved in can synthesize only certain amino acids and
the construction of proteins. the rest of the amino acids which are called
essential amino acids should be supplied
through protein-rich foods in our daily diet.
Foods rich in amino acids include
plant-based products like broccoli, beans,
beetroots, pumpkin, cabbage, nuts, dry
fruits, chia seeds, oats, peas, carrots,
cucumber, green leafy vegetables, onions,
soybeans, whole grain, peanuts legumes,
lentils, etc. Fruits rich in amino acids are
apples, bananas, berries, figs, grapes,
melons, oranges, papaya, pineapple, and
pomegranates. Other animal products
General properties of Amino acids include dairy products, eggs, seafood,
1. They have a very high melting and chicken, meat, pork etc.
boiling point. Structure of amino Acids
2. Amino acids are white crystalline The general structure of Amino acids is
solid substances. H2NCH RCOOH, and it can be written as:

COOH aspartic acid, glutamic acid, cysteine,
| glutamine, proline, glycine, serine, and
H2N – –C – – H tyrosine.
| Apart from these, there are other nine
R amino acids, which are very much essential
There are 20 naturally occurring amino as they cannot be synthesized by our body.
acids and all have common structural They are called essential amino acids, and
features – an amino group (-NH3+), a they include Isoleucine, Histidine, Lysine,
carboxylate (-COO-) group and a Leucine, Phenylalanine, Tryptophan,
hydrogen-bonded to the same carbon atom. Methionine, Threonine and Valine.
They differ from each other in their side- Functions of Amino Acids
chain called the R group. Each amino acid Functions of Essential Amino acids
has 4 different groups attached to α- carbon.
1. Phenylalanine helps in maintaining
These 4 groups are amino group,
a healthy nervous system and in
COOH group, Hydrogen atom and Side
boosting memory power.
chain (R).
2. Valine acts as an important
component in promoting muscle
growth.
3. Threonine helps in promoting the
functions of the immune system.
4. Tryptophan is involved in the
production of vitamin B3 and
serotonin hormones. This serotonin
hormone plays a vital role in
maintaining our appetite, regulating
Fig.: Structure of Twenty Amino Acids
sleep and boosting our moods.
Essential and Non-essential Amino
5. Isoleucine plays a vital role in the
acids formation of haemoglobin,
Out of 20 amino acids, our body can stimulating the pancreas to
easily synthesize a few on its own, which synthesize insulin, and transporting
are called non-essential amino acids. These oxygen from the lungs to the various
include alanine, asparagine, arginine, parts.

6. Methionine is used in the treatment synthesis of nucleic acids – DNA and
of kidney stones, maintaining RNA.
healthy skin and also used in 4. Glycine is helpful in maintaining the
controlling invade of pathogenic proper cell growth, and its function,
bacteria. and it also plays a vital role in
7. Leucine is involved in promoting healing wounds. It acts as a
protein synthesis and growth neurotransmitter.
hormones. 5. Glutamic acid acts as a
8. Lysine is necessary for promoting neurotransmitter and is mainly
the formation of antibodies, involved in the development and
hormones, and enzymes and in the functioning of the human brain.
development and fixation of calcium 6. Arginine helps in promoting the
in bones. synthesis of proteins and hormones,
9. Histidine is involved in many detoxification in the kidneys,
enzymatic processes and in the healing wounds, and maintaining a
synthesizing of both red blood cells healthy immune system.
(erythrocytes) and white blood cells 7. Tyrosine plays a vital role in the
(leukocytes). production of the thyroid hormones
Functions of Non-Essential Amino -T3 and T4, in synthesizing a class of
acids neurotransmitters and melanin,

which are natural pigments found in
1. Alanine functions by removing
our eyes, hair, and skin.
toxins from our body and in the
8. Serine helps in promoting muscle
production of glucose and other
growth and in the synthesis of
amino acids.
immune system proteins.
2. Cysteine acts as an antioxidant and
9. Asparagine is mainly involved in the
provides resistance to our body; it is
transportation of nitrogen into our
important for making collagen. It
body cells, formations of purines
affects the texture and elasticity of
and pyrimidine for the synthesis of
the skin
DNA, the development of the
3. Glutamine promotes a healthy brain
nervous system and improving our
function and is necessary for the
body stamina.

10. Aspartic acid plays a major role in PROTEINS
metabolism and in promoting the
Proteins are macromolecules
synthesis of other amino acids.
composed of one or more polypeptide
11. Proline is mainly involved in the
chains possessing a characteristic amino
repairing of the tissues in the
acid sequence. It is a polymer of amino
formation of collagen, preventing
acids. In proteins one amino acid is binded
the thickening and hardening of the
to the other amino acid by peptide (-CO-
walls of the arteries
NH-) bond which is formed between amino
(arteriosclerosis) and in the
group of one amino acid and carboxyl
regeneration of new skin.
group of other amino acid. The term protein
DEFICIENCY OF AMINO ACIDS
was coined by Jons Jacob Berzelius in 1838.
Amino acids are the building blocks
SOURCES OF PROTEINS
of proteins and proteins play a fundamental
Proteins are obtained from animal
role in almost all life processes. Therefore,
and plant source. The animal sources of
it is necessary to include all nine essential
proteins include milk, egg, meat, fish, liver
amino acids in our daily diet to maintain a
etc. Plant sources of proteins are pulses,
healthy and proper function of our body.
nuts and cereals.
The deficiency of amino acids may include
CLASSIFICATION OF PROTEINS
different pathological disorders, including:
On the basis of solubility and shape,
 Edema
proteins are classified into two types
 Anemia
namely Globular and Fibrous Proteins:
 Insomnia
 Globular Proteins: They are spherical in
 Diarrhea
shape and soluble in water. They are
 Depression
highly branched. The polypeptide chains
 Hypoglycaemia
are cross linked by the usual peptide
 Loss of Appetite
bonds. These proteins are tightly folded
 Fat deposit in the liver
into spherical or globular shape. The
 Skin and hair related problems
globular proteins include enzymes,
 Headache, weakness, irritability
protein hormones, antibodies,
and fatigue.
haemoglobin and myoglobin.
 Fibrous Proteins: They are in the form of
fibres and insoluble in water. They are

unbranched. They are highly resistant to Phosphoproteins (Contain phosphoric
digestion by proteolytic enzymes. They acid) like casein in milk and vitelline in
are linear molecules. The long linear egg yolk.
protein chains are held together by  Derived Proteins: They are intermediate
intermolecular H-bonds. They serve as products formed from natural proteins
structural proteins. The common fibrous when they are hydrolysed by heat, acids,
proteins are collagen of tendons, elastin alkalis or enzymes. For Example, Fibrin.
of connective tissue, fibroin of silk, STRUCTURE OF PROTEINS
keratin of hair, actin and myosin. Every protein has a three dimensional
On the basis of increasing structure that can have upto four levels of
complexity of structure, proteins are organisation:
classified into three groups namely
Primary Structure
simple proteins, conjugated proteins and
It is the basic linear sequence of amino
derived proteins.
acids in a polypeptide chain. For Example,
 Simple Proteins: The proteins which
Fibroin of Silk.
yield amino acids or their derivatives on
Secondary Structure
hydrolysis are called simple proteins or
It is the development of new stearic
the proteins which are made up of amino
relationships of amino acids present in the
acid only. For Example, Histones,
linear sequence inside the polypeptides
Keratins.
like in Keratin. These are of two types
 Conjugated Proteins: These are
namely α-helix and β-pleated. These are
proteins united with non-protein
accomplished through hydrogen bonding
substances. The non-protein substances
between amino acids.
linked to proteins are referred to as
α-helix is formed by a series of amino
prosthetic group. The protein part is
acid residues woven into a spiral chain. The
called apoprotein. The prosthetic group
helical structure of protein is formed by the
and apoprotein are together called
hydrogen bonds between the peptide
haloprotein. So conjugated proteins on
groups of every first and fourth amino acid
hydrolysis yield non-protein substances
residues.
in addition to amino acids. For Example,
β-pleated is formed from H-bonding
Glycoproteins (contain carbohydrates)
between two peptide chains. This bonding
like mucin in saliva, egg albumin, serum
leads to the formation of sheets of parallel
albumin and serum globulin,

chains in the form of pleated sheets. In PROPERTIES OF PROTEINS
pleated sheet structure, the chains may be
Denaturation
parallel or antiparallel. In a parallel chain
Partial or complete unfolding of the
pleated sheet structure, the N-terminal end
native (natural) conformation of the
of the polypeptide chains point in the same
polypeptide chain is known as
direction. In antiparallel chain pleated
denaturation. This is caused by heat, acids,
sheet structure, the N-terminal ends of the
alkalies, alcohol, acetone, urea, beta-
polypeptide chains point in opposite
mercaptoethanol.
directions.
Coagulation
Tertiary Structure
When proteins are denatured by heat,
It is the bending and folding of
they form insoluble aggregates known as
secondary strand of polypeptide to various
coagulum. All the proteins are not heat
types of structures. It is stabilized by
coagulable, only a few like the albumins,
several types of bonds like hydrogen
globulins are heat coagulable.
bonds, ionic bonds, van der Waals
interactions, disulphide, hydrophobic Isoelectric pH (pH1)
bonds etc. Myoglobin, Ribonulcease, The pH at which a protein has equal

Chymotrypsin, Cytochrome C etc. shows number of positive and negative charges is
tertiary structure. known as isoelectric pH. When subjected to
Quaternary Structure an electric field the proteins do not move
It is found in multimeric proteins. Each either towards anode or cathode, hence this
polypeptide develops its own tertiary property is used to isolate proteins. The
structure and functions as subunits of proteins become least soluble at pHI and
proteins. It is exhibited by proteins get precipitated. The pHI of casein is 4.5
containing more than one polypeptide and at this pH the casein in milk curdles
chain like haemoglobin. producing the curd.

Molecular Weights of Proteins
The average molecular weight of an

amino acid is taken to be 110. The total
number of amino acids in a protein
multiplied by 110 gives the approximate
Fig.: Structural Organization of Proteins molecular weight of that protein. Different

proteins have different amino acid by other species. Invading bacteria,
composition and hence their molecular virus etc. elicit the production of
weights differ. The molecular weights of antibodies by lymphocytes.
proteins range from 5000 to 109 Daltons. Antibodies neutralize the foreign
FUNCTIONS OF PROTEINS germs. Antibodies are proteins.
Proteins play various important roles 7. Blood Clotting: Bleeding is stopped
which are the following: by the formation of clot. Clotting is
1. Enzyme Catalysts: Almost all brought about by clotting proteins
chemical reactions in the biological such as fibrinogen and thrombin.
system are catalyzed by enzymes. All 8. Transmission of Nerve Impulse:
enzymes are proteins. The nerve impulse is transmitted with
2. Transport: Proteins transport ions the help of receptor protein through
and small molecules e.g. synapse.
Haemoglobin a conjugated protein of 9. Hormonal action: Many hormones
blood transport oxygen. are proteins e.g., insulin, growth
3. Storage: Certain proteins function as hormone, parathyroid hormone etc.
a storage molecule e.g. ferritin, a 10. Thermoregulation: The blood
protein stores iron in liver. plasma of some Antarctic fish
4. Contraction and Movement: The contains antifreeze proteins which
contraction of muscle is brought prevent the blood from freezing.
about by two fibrous proteins called LIPIDS

actin and myosin. The microtubules
Lipids are group of molecules that are
of flagella and cilia are built on
insoluble in polar solvents such as water but
tubulin, a protein.
soluble in non-polar solvents such as
5. Mechanical Support: Many proteins
benzene and ether. Lipids contain relatively
serve as supporting filaments, cables
long hydrocarbon chains that are non-polar
or sheets to give biological structures
and thus hydrophobic. The term lipid was
strength, support and protection e.g.,
first introduced by Bloor in 1943. The lipids
collagen a fibrous protein is the
are important constituents of diet due to
major component of hair, finger nails
their high energy value. One gram of lipid
and feathers.
yields 9.3 kilo calories of heat. The lipids
6. Immune Protection: Many proteins
are found in all organisms including virus.
defend organisms against invasion

PROPERTIES OF LIPIDS made up of a glycerol molecule and
Lipids have three important thee fatty acids. It is called
properties. They are: triglyceride. They form insulation to
1. Lipids are insoluble in water but temperature loss. They are found in
soluble in non-polar organic liver, seeds, fruits etc. If the three
solvents, such as acetone, molecules of fatty acids are same, the
alcohol, chloroform, benzene fat is simple glyceride. If the fatty acids
and ether. are different, then the fat is a mixed
2. They contain a large proportion glyceride. If the glycerides have no
of carbon and hydrogen bonds free acid or basic groups the fat is
and release large amount of termed neutral fat. Fats have high
energy on breakdown. melting point and are insoluble in
3. On alkaline hydrolysis, lipids water. They float in water. They form
yield alcohol and fatty acids. soap with alkali. The process of
The common lipids are fats, oils, formation of soap is called
waxes, phospholipids, glycolipids, saponification. They develop
cerebrosides, sulfolipids, aminolipids, unpleasant odour on aging. It is called
steroids, terpenes, carotenoids, some rancidity. Rancidity is caused by
hormones and some vitamins. oxidation and hydrolysis.
CLASSIFICATION OF LIPIDS Fats are two types namely Animal

fats and Plant fats.
Lipids are generally classified into
Animal Fats are relatively rich in
three types namely simple lipids,
saturated fatty acids (with C16 and
compound lipis and derived lipids.
C18 acids).
Simple Lipids or Homolipids
Plant Fats are relatively rich in
These are esters of fatty acids with
unsaturated fatty acids (poly
alcohol like glycerol (in neutral fats) and
unsaturated acids).
cetyl alcohol (in waxes). Fats, oils and
Oils: They are liquid fats. They are
waxes are simple lipids.
simple lipids. They are esters of fatty
Neutral or True Fats: They are simple
acids and glycerol. One glycerol
lipids. They are solid or semi-solid at
molecule is linked to three fatty acids.
room temperature. They are the esters
The oils are found in both plants and
of fatty acids with glycerol. A fat is
animals. The oils found in plants are

called vegetable oils e.g., coconut oil, The sperm whale wax contains
groundnut oil, cotton seed oil etc. The plamitic acid and cetyl alcohol and is
oils found in animals are called animal called cetyl palmitate.
oils e.g., fish liver oil etc. Oil remains Carnauba wax is the hardest known
liquid at room temperature and in wax and contains fatty acid esterified
tropical countries. The fatty acids with tetracosanol and tetratriacontanol.
found in oils are mostly unsaturated Waxes are insoluble in water and
fatty acids. If the three fatty acids of oil resistant to atmospheric oxidation.
are similar, the oil is called simple oil. They have high melting point.
When the fatty acids are dissimilar, the Compound Lipids or Heterolipids
oil is called mixed oil. Oils have low They are the lipids linked to non-
melting point. They are insoluble in lipids. They consist of three components
water and spread uniformly on water. namely glycerol, fatty acid and a non-lipid.
They are soluble in organic solvent. In The non-lipid may be phosphoric acid or a
water, oils are broken into minute carbohydrate. Compound lipids are of two
droplets and dispersed. This is called types namely Phospholipids (Phosphatids)
emulsification. and Glycolipids (Cerebrosides).
Waxes: Waxes are simple lipid, solid 1. Phospholipids: These are the
lipids. They are esters of fatty acids compound lipids formed by
with monohydric alcohols of higher glycerol, phosphoric acid and fatty
molecular weight. Waxes are secreted acids. They include Lecithins
by bees, cutaneous glands and plants. (found in the brain, nervous
Waxes are acting as a protective tissues, sperm and egg yolk,
coating to keep the skin pliable, seeds, sprouts), Cepahalins (found
lubricated and water proof. in animal tissues, soyabean oil);
The common examples are bee Plasmologens (found in brain,
wax, sperm whale wax (spermaceti), muscle and seeds of higher
carnauba wax. plants); Phosphoinositides (found
The bee wax contains plamitic acid in in brain tissues, soyabean);
and myricyl alcohol and it is called Phosphingosides or
myricyl palmitate. Sphingomyelins (myelin sheath of
the nerve, spinal cord and in plant
seeds).

2. Glycolipid or Galactolipids or 4. Lipids serve as an electroinsulating
Cerebrosides or material in the myelin sheath of
Glycosphingosides: These are neurons.
compound lipids containing sugars 5. Subcutaneous fats of mammals act as
and fatty acids like sphingosine an insulator against the excessive
and no phosphoric acid. It is found heat loss to the environment.
in brain, adrenals, kidney, spleen, 6. Lipids of connective tissue of internal
liver, thymus, egg yolk, lungs, organs protect them from the
retina and fish sperm and eventual damage on exposure to
leucocytes e.g. Gangliosides mechanical action.
found in brain tissue. Gangliosides 7. The major group of hormones is
contain ceramide, N-acetyl formed of steroids. They regulate the
neuraminic acid (NANA), N-acetyl large variety of physiological
galactosamine, Carbohydrates functions e.g., sex hormones and
(hexoses like glucose and adrenocorticoids.
galactose). 8. Lipids acts as carriers of natural fat
Derived Lipids soluble vitamins such as A, D and E.
They are the products of hydrolysis of 9. Lipids are essential for activation of
simple lipids and compound lipids and enzymes like glucose-6-phosphate
include compound like steroids etc.
(cholesterol), terpenes, coprostanol (occurs FATTY ACIDS

in faeces), carotenoids, ergasterol (Ergot
Fatty acids are aliphatic straight chain
and Yeast).
hydrocarbon compounds with a terminal
FUNCTIONS OF LIPIDS carboxyl group. They are the building
1. Lipids contains large amount of blocks of lipids. There are about 200 fatty
energy so are good source of acids. They have single carboxyl group and
energy. a long non-polar (=Hydrophobic or Water
2. Lipids are insoluble in water, so they hating) hydrocarbon tail. This non-polar tail
are readily stored in the body as a gives most lipids their water insoluble and
food reserve. oily or greasy nature. Fatty acids are
3. Lipids constitute an important classified into two groups based on the
component of cell membrane.

presence or absence of double bonds  Hydroxy or Oxygenated Fatty
namely: Acids: Fatty acids containing
 Saturated Fatty Acids: they have single hydroxy group e.g., Ricinoleic acid,
bonds i.e. they are without double bond. Cerebronic acid.
At one end there will be an acid (-COOH)  Cyclic Fatty Acids: fatty acids with
group and at the other end there will be cyclic structures e.g., Chaulmoogric
methyl (-CH3) group. In between these acid, Hydnocarpic acid, Lactobacillic
two groups, there will be CH2 groups. acid.
These fatty acids ends with suffix „anoic‟  Essential Fatty Acids: The fatty
e.g., Stearic acid (common source animal acids which are not synthesized by
and plant fat), Decanoic acid (Common man, but they must be included in the
source Coconut and palm oil), Palmitic diet are called essential fatty acids
acid (common source animal and plant e.g., Linoleic acid, Linolenic acid and
fat). Arachidonic acid.
 Unsaturated Fatty Acids: They have one  Non-Essential Fatty Acids: Certain
or more double bonds i.e. 1 to 6 double fatty acids can be synthesized in the
bonds. These double bonds may occur tissues from other fatty acids. These
after 9,12,15,18 etc. carbon atoms. These fatty acids need not be included in
fatty acids end with suffix „enoic‟. Based the diet. Hence they are called non-
on the number of double bonds, these essential fatty acids e.g., Oleic acid,
unsaturated fatty acids may be called as Palmitoleic acid.
monoenoic (one double bond), dienoic ENZYMES
(two double bonds), trienoic (three
Enzymes are macromolecular
double bonds), and tetraenoic (four
biological catalysts that accelerate chemical
double bonds) and so on.
reactions without being utilized themselves.
Unsaturated fatty acids in general
The term enzyme was first introduced by
containing more than one double bond is
Wilhelm Kuhne in 1877. But first enzyme to
called polyunsaturated fatty acid (PUFA)
be discovered was diastase by Anselme
e.g. Linoleic acid, Oleic acid,
Payen in 1833.The study of enzyme is
Arachidonic acid etc.
known as enzymology.
Besides fatty acids are further
classified into following types namely:

NOMENCLATURE OF ENZYMES a. Glucose oxidase: Catalysis of
The International Union of glucose oxidation.
Biochemistry and Molecular Biology is b. Lactate dehydrogenase:
entrusted with designating names to Catalysis of eliminating
enzymes in addition to assigning a number hydrogen from lactate ion.
in order to identify them. c. Lactase: Hydrolysis of lactose
Apart from a few originally studied is catalyzed.
enzymes such as rennin, pepsin and d. Urease: Hydrolysis of urea is
trypsin, almost all the enzyme names end in catalyzed.
„ase‟. As per the standards, focal points of Example of Naming
nomenclature of enzymes are both the type As per the standard International
of reaction catalyzed and the substrate Union of Biochemistry, the name of the
acted upon. enzyme comprises two parts namely:
Most commonly, enzymes are named 1. Name of the substrate for the enzyme
to provide data on the function as opposed 2. Type of reaction catalyzed by the
to the structure of the enzyme. However, enzyme. The second part, therefore,
there are three significant features of the ends with „ase‟ suffix
nomenclature process of enzymes, which For Example: Lactate Dehydrogenase
are: Conventions of Naming– EC Numbers

1. Suffix -ase recognizes a substance as The nomenclature developed by the
that of an enzyme International Union of Biochemistry and
 Suffix - in is observed in the Molecular Biology has something called EC
name of first enzymes learnt as numbers where each enzyme is preceded
pepsin, chymotrypsin, trypsin by EC. The first number in this series
2. Prefix is identified by the type of classifies this enzyme on the basis of its
reaction the enzyme catalyzes mechanism.
 Enzyme hydrolase : Catalyzes EC Numbers
a hydrolysis reaction There are six groups of enzymes as
 Enzyme oxidase : Catalyzes an per the reaction that is being catalyzed.
oxidation reaction Therefore, all enzymes are designated as
3. In addition to the type of reaction, the “EC numbers”. This classification does not
identity of the substrate is taken into consider protein structure, amino acid
consideration sequence or even the chemical mechanism.

EC number is a 4 digit number for instance 4. Lyases: These are the enzymes
– a.b.c.d. Here “a” is class, “b” is subclass, which catalyse either the removal of
“c” is sub-subclass and “d” is the sub-sub- a group of atoms from their substrate
subclass. The “b” and “c” part of the EC leaving double bonds or add groups
number describes the reaction, “d” to double bonds without hydrolysis,
differentiates between different enzymes oxidation or reduction. For Example,
with similar function on the basis of the Aldolase, Enolase, Fumarase etc.
actual substrate in the reaction. 5. Isomerases or Mutases: These are
For Example: EC number of Alcohol: NAD+ enzymes which catalyse the inter-
oxidoreductase is 1.1.1.1 conversion of a compound to one of
CLASSIFICATION OF ENZYMES its isomers. For Example,
In 1961, the enzyme commission of the Phosphoisomerase.
International Union of Biochemistry (IUB) 6. Ligases or Synthetases: These
proposed a comprehensive system for the enzymes catalyze synthesis reactions
classification of enzyme. According to this by joining two molecules coupled
system, enzymes are classified into six with the breakdown of a
major classes namely: pyrophosphate bond of ATP to ADP.
1. Oxidoreductases: They are enzymes For Example, DNA ligase, RNA
which are involved in biological synthetase, Glutamine synthetase.
oxidations and reductions. For MECHANISM OF ENZYME ACTION

Example, Dehydrogenases, The breaking of substrate into end
Oxidases, Oxygenases etc. products by an enzyme is called enzyme
2. Transferases: These enzymes action. Michaelis and Mention proposed a
transfer a group from one substrate hypothesis for enzyme reaction. The
to another substrate. For Example, enzyme action involves the following steps:
Transaminase, Creatine phosphoryl 1. The enzyme molecule (E) combines
transferase etc. with a substrate molecule (S) to form
3. Hydrolases: These are enzymes an enzyme-substrate complex (ES). It
which catalyse hydrolysis i.e. direct is also called as Michaelis complex.
addition of water molecules across a 2. The enzyme contains specific sites for
bond which is cleaved. For Example, the attachment of substrate. These
Proteases, Carbohydrases, Esterases sites are called active sites or
etc.

catalytic centres. They are made up Induced Fit Hypothesis
of amino acid residues. It was proposed by Koshland n 1963.
3. The active sites loosen the chemical This theory says that the active site does not
bonds in the substrate and this leads possess a rigid and performed structure.
to the breaking of substrate into end The region of the active sites is flexible.
products. When the enzyme reacts with the substrate,
4. Finally, the enzyme dissociates from the substrate induces a conformational
the end products. change in the active site of the enzyme. The
5. The enzyme is now free to combine change results in the development of
with another molecule of substrate. attraction between enzyme and the
There are two hypotheses which substrate so that an enzyme substrate
explain the mechanism of the formation of complex is formed. It leads to the loosening
the enzyme substrate complex: of the chemical bonds linking the
Lock and Key Hypothesis components of the substrate. As the
It was proposed by Emil Fisher in reaction is completed the substrate is split
1914. According to this hypothesis, the into end products and enzyme is released.
enzyme molecule has one or more specific
points. These points are called active sites
or active centres. The active sites exist in
the enzyme in a rigid and proper
conformation even in the absence of
substrate. During enzyme action, the
Fig.: Induced Fit Hypothesis
substrate fits into the active site of the
PROPERTIES OF ENZYMES
enzyme as a key fits into the lock.
1. Most of the enzymes are simple or
conjugated protein. They exhibit all
the properties of proteins.
2. Enzymes are colloidal in nature.
3. Enzymes undergo denaturation when
subjected to changes in pH or
Fig.: Lock and Key Hypothesis increase in temperature.
4. Enzyme accelerates speed of
reactions.

5. The enzyme promotes a given
reaction, but itself remains
unchanged at the end of the reaction.
6. Only small amount of enzyme is
required by a biological system for a
complete reaction.
7. Every enzyme has an optimum
temperature at which the rate of
activity is maximum.
8. Most of the enzyme are characterized
by the reversibility of their actions
i.e. enzymes act in either direction
e.g. phosphoglucomutase.
9. Each enzyme will react with only one
type of substrate or group of related
substrate. This property of enzyme is
called specificity of enzymes e.g.,
lactase acts only on lactose.
Any Error in this document is silent

testimony of the fact that it was a human
effort”
“Dr. WKB”

Unit I Structure and Function of Biomolecules Nep 2020

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ZOOLOGY

DR. WKB’S ZOOLOGY STUDY MATERIAL

UG SEMESTER-I UNDER NEP-2020 (ZOOLOGY)

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Glucose configuration of the hydroxyl group at

Fig.: Structure of Monosaccharides

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Fig.: Structure of Monosaccharides

the solution and it is a reducing sugar as it with water.

shows reducing properties. Starch is a storage compound in

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The amylose chain forms a helix. This 5. Carbohydrates aid in regulation of

with iodine. Amylose is poorly soluble in source for brain.

water, but forms micellar suspensions. 6. Carbohydrates get associated with

Amylopectin-a glucose polymer with lipids and proteins to form surface

mainly α - (1→4) linkages, but it also has antigens, receptor molecules,

branches formed by α -(1→6) linkages. vitamins and antibiotics.

Amylopectin causes a red-violet transport, cell-cell communication

darker reaction of amylose to iodine. content help to prevent constipation.

BIOLOGICAL IMPORTANCE OF 11. Also they help in modulation of

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acids neurotransmitters and melanin,

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bonds etc. Myoglobin, Ribonulcease, The pH at which a protein has equal

proteins. It is exhibited by proteins get precipitated. The pHI of casein is 4.5

chain like haemoglobin. producing the curd.

The average molecular weight of an

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Proteins play various important roles 7. Blood Clotting: Bleeding is stopped

which are the following: by the formation of clot. Clotting is

1. Enzyme Catalysts: Almost all brought about by clotting proteins

chemical reactions in the biological such as fibrinogen and thrombin.

system are catalyzed by enzymes. All 8. Transmission of Nerve Impulse:

enzymes are proteins. The nerve impulse is transmitted with

2. Transport: Proteins transport ions the help of receptor protein through

and small molecules e.g. synapse.

Haemoglobin a conjugated protein of 9. Hormonal action: Many hormones

blood transport oxygen. are proteins e.g., insulin, growth

3. Storage: Certain proteins function as hormone, parathyroid hormone etc.

a storage molecule e.g. ferritin, a 10. Thermoregulation: The blood

protein stores iron in liver. plasma of some Antarctic fish

4. Contraction and Movement: The contains antifreeze proteins which

contraction of muscle is brought prevent the blood from freezing.

about by two fibrous proteins called LIPIDS

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Lipids have three important thee fatty acids. It is called

properties. They are: triglyceride. They form insulation to

soluble in non-polar organic liver, seeds, fruits etc. If the three

solvents, such as acetone, molecules of fatty acids are same, the

alcohol, chloroform, benzene fat is simple glyceride. If the fatty acids

and ether. are different, then the fat is a mixed

2. They contain a large proportion glyceride. If the glycerides have no

energy on breakdown. melting point and are insoluble in

3. On alkaline hydrolysis, lipids water. They float in water. They form

The common lipids are fats, oils, formation of soap is called

waxes, phospholipids, glycolipids, saponification. They develop

cerebrosides, sulfolipids, aminolipids, unpleasant odour on aging. It is called

steroids, terpenes, carotenoids, some rancidity. Rancidity is caused by