Biomolecules Introduction to Biotechnology

[BT104]
Unit 3
BIOMOLECULES

Biomolecules Definition
- Biomolecules are molecules that occur naturally in living organisms. Biomolecules include
macromolecules like proteins, carbohydrates, lipids and nucleic acids.
- It also includes small molecules like primary and secondary metabolites and natural products.
- Biomolecules consists mainly of carbon and hydrogen with nitrogen, oxygen, sulphur, and
phosphorus.
Biomolecules are very large molecules of many atoms, which are covalently bound together.
 Classes of Biomolecules
- There are four major classes of biomolecules:
i. Carbohydrates
ii. Lipids
iii. Proteins
iv. Nucleic acids
1. Carbohydrates
- Carbohydrates are good source of energy. Carbohydrates (polysaccharides) are long chains of
sugars.
Monosaccharides are simple sugars that are composed of 3-7 carbon atoms.
- They have a free aldehyde or ketone group, which acts as reducing agents and are known as reducing
sugars. Disaccharides are made of two monosaccharides. The bonds shared between two
monosaccharides are the glycosidic bonds.
- Monosaccharides and disaccharides are sweet, crystalline and water-soluble substances. Polysaccharides
are polymers of monosaccharides. They are un-sweet and complex carbohydrates. They are insoluble in
water and are not in crystalline form.
- Example: glucose, fructose, sucrose, maltose, starch, cellulose etc.

2. Lipids
- Lipids are composed of long hydrocarbon chains. Lipid molecules hold a large amount of energy and
are energy storage molecules. Lipids are generally esters of fatty acids and are building blocks of
biological membranes.
- Most of the lipids have a polar head and non-polar tail. Fatty acids can be unsaturated and saturated fatty
acids.
- Lipids present in biological membranes are of three classes based on the type of hydrophilic head present:
 Glycolipids are lipids whose head contains oligosaccharides with 1-15 saccharide residues.
 Phospholipids contain a positively charged head which are linked to the negatively charged
phosphate groups.
 Sterols, whose head contain a steroid ring. Example steroid.
- Example of lipids: oils, fats, phospholipids, glycolipids, etc.
3. Nucleic Acids
4. Nucleic acids are organic compounds with heterocyclic rings. Nucleic acids are made of polymer of
nucleotides. Nucleotides consist of nitrogenous base, a pentose sugar and a phosphate group. A
nucleoside is made of nitrogenous base attached to a pentose sugar. The nitrogenous bases are adenine,
guanine, thyamine, cytosine and uracil. Polymerized nucleotides form DNA and RNA which are genetic
materialProteins
- Proteins are heteropolymers of stings of amino acids. Amino acids are joined together by the peptide
bond which is formed in between the carboxyl group and amino group of successive amino acids.
Proteins are formed from 20 different amino acids, depending on the number of amino acids and the
sequence of amino acids.
- There are four levels of protein structure:
(i) Primary structure of Protein - Here protein exist as long chain of amino acids arranged in a particular
sequence. They are non-functional proteins.
(ii) Secondary structure of protein - The long chain of proteins are folded and arranged in a helix shape,
where the amino acids interact by the formation of hydrogen bonds. This structure is called the pleated
sheet. Example: silk fibres.
(iii) Tertiary structure of protein - Long polypeptide chains become more stabilizes by folding and
coiling, by the formation of ionic or hydrophobic bonds or disulphide bridges, these results in the
tertiary structure of protein.
(iv) Quaternary structure of protein - When a protein is an assembly of more than one polypeptide or
subunits of its own, this is said to be the quaternary structure of protein. Example: Haemoglobin,
insulin.

 Functions of Biomolecules
- Carbohydrates provide the body with source of fuel and energy, it aids in proper functioning of our
brain, heart and nervous, digestive and immune system. Deficiency of carbohydrates in the diet causes
fatigue, poor mental function.
- Each protein in the body has specific functions, some proteins provide structural support, help in body
movement, and also defense against germs and infections. Proteins can be antibodies, hormonal,
enzymes and contractile proteins.
- Lipids, the primary purpose of lipids in body are energy storage. Structural membranes are composed
of lipids which form a barrier and controls flow of material in and out of the cell. Lipid hormones, like
sterols, help in mediating communication between cells.
- Nucleic Acids are the DNA and RNA; they carry genetic information in the cell. They also help in
synthesis of proteins, through the process of translation and transcription.

CARBOHYDRATES
Carbohydrates form a very large group of naturally occurring organic compounds which play a vital role
in daily life. They are produced in plants by the process of photosynthesis. The most common
carbohydrates are glucose, fructose, sucrose, starch, cellulose etc. Chemically, the carbohydrates may be
defined as polyhydroxy aldehydes or ketones or substances which give such molecules on hydrolysis.
Many carbohydrates are sweet in taste and all sweet carbohydrates are called as sugars. The chemical
name of the most commonly used sugar in our homes is sucrose.
2
Classification of Carbohydrates
Carbohydrates are classified into three groups depending upon their behaviour on hydrolysis.
Monosaccharides: A polyhydroxy aldehyde or ketone which cannot be hydrolysed further to a smaller
molecule containing these functional groups, is known as a monosaccharide. About 20 monosaccharides
occur in nature and glucose is the most common amongst them.

Monosaccharides are further classified on the basis of the number of carbon atoms and the functional group
present in them. If a monosaccharide contains an aldehyde group, it is known as an aldose and if it contains
a keto group, it is known as a ketose. The number of carbon atoms present is also included while classfying
the compound as is evident from the examples given in Table 29.1. Name of some naturally occuring
monosaccharides are given in brackets.

Classification of monosaccharides

No. of carbon Type of monosaccharide

atoms
present Aldose Ketose
3 Aldotriose Ketotriose
(Glyceraldehyde
4 Aldopentose ((Xylose) Ketopentos
e
5 Aldotetrose (Erythrose) Ketotetrose
6 Aldohexose (Glucose) Ketohexose
7 Aldoheptose Ketoheptose

(i) Disacccharides: Carbohydrates which give two monosaccharide molecules on hydrolysis

are called disaccharides e.g. sucrose, maltose, lactose etc.
(ii) Oligosacharides: Carbohydrates that yield 2–10 molecules of monosascharides
are called oligosaccharides.
(iii) Polysaccharides: Carbohydrates which yield a large number of monosaccharide
units on hydrolysis e.g. starch, glycogen, cellulose etc.
 Structure of Monosaccharides
Although a large number of monosaccharides are found in nature.
D-or L-before the name of monosaccharides indicates the configuration of particular stereoisomer.
Various stereoisomers are assigned relative configurations as D– or L –. This system of assigning the
relative configuration refers to their relation with the glyceraldehyde. Glyceraldehyde contains one
asymmetric carbon atom and hence exists in two enantiomeric forms as shown below.

CHO CHO

H HO H
O
H CH2OH

CH2OH

D-(+) –glyceraldehyde L-(–) –glyceraldehyde

All those compounds which can be correlated to (+) -glyceraldehyde are said to have D-configuration and
those can be correlated to (–) -glyceraldehyde are said to have L–configuration. In monosaccharides, it is
the lowest asymmetric carbon atom (shown in the box) by which the correlation is made. As in (+) glucose,
the lowest asymmetric carbon atom has –OH group on the right side which matches with (+)
glyceraldehyde; hence, it is assigned D-configuration.

CHO

H OH

HO H
H OH CHO
H OH
H OH
CH2OH

CH2OH
(+) – (+) –
glucose glyceraldehyd
or D- e or D-
glucose glyceraldehyd
e

4
 If a large number of monosaccharide units are joined together, we get polysaccharides. These are the most
common carbohydrates found in nature. They have mainly one of the following two functions- either as food
materials or as structural materials. Starch is the main food storage polysaccharide of plants. It is a polymer
of -glucose and consists of two types of chains- known as amylose and amylopectin.
Amylose is a water soluble fraction of starch and is a linear polymer of -D- glucose. On the other hand,
amylopectin is a water insoluble fraction and consists of branched chain of -D-glucose.
Cellulose is another natural polysaccharide which is the main component of wood and other plant materials. It
consists of long chain of -D-glucose molecules.

Glycogen
The carbohydrates are stored in animal body as glycogen and its structure is similar to amylopectin.
It is a polysaccharide containing the -D-glucose monosaccharide and does the same energy storage
function in animals which the starch does in plants. The carbohydrates which are not needed immediately
by the body are converted by the body to glycogen for long term storage. Glycogen molecules are larger
than those of amylopectin and are having more branched structure.

Biological Importance of Carbohydrates

(i) Carbohydrates act as storage molecules. For example they are stored as starch in plants and as glycogen
in animals.
(ii) D-Ribose and 2-deoxy-D-ribose are the constituents of RNA and DNA, respectively.
(iii) Cell walls of bacteria and plants are made up of cellulose. It may be of interest to note that human
digestive system does not have the enzymes required for the digestion of cellulose but some animals do
have such enzymes.
(iv) Some carbohydrates are also linked to many proteins and lipids. These molecules are known as
glycoproteins and glycolipids, respectively. These molecules perform very specific functions in
organisms.

- Carbohydrate is an organic compound, it comprises of only oxygen, carbon and hydrogen.

- The oxygen: hydrogen ratio is usually is 2:1.
- The empirical formula being Cn(H2O)n .
- Carbohydrates are hydrates of carbon; technically they are polyhydroxy aldehydes and ketones.
- Carbohydrates are also known as saccharides, the word saccharide comes from Greek word sakkron
which means sugar.
Classification and nomenclature of carbohydrates
- The carbohydrates are divided into three major classes depending upon whether or not they undergo
hydrolysis and if they do, on the number of products formed.
1. Monosaccharides: The monosaccharides are polyhydroxy aldehydes or polyhydroxy ketones which
cannot be decomposed by hydrolysis to give simpler carbohydrates. e.g. Glucose, fructose, Galactose
etc.
2. Oligosaccharides: The oligosaccharides (Oligo: few) are carbohydrates which yield a definite number
 (2-9) of monosaccharide molecules on hydrolysis.
a) Disaccharides - Which yield two monosaccharides molecules on hydrolysis. Which have molecular
formula is C12H22O11.e.g. Sucrose, maltose etc

b) Trisaccharides - Which yield three monosaccharides molecules on hydrolysis and have molecular

formula is C18H32O16.

c) Tetrasaccharides - Which yield four monosaccharides molecules on hydrolysis and have molecular
formula is C22H42O21. eg: Stachyose [gal(α1→6)gal(α1→6)glu(α1↔2β)fru]
3. Polysaccharides: The carbohydrates which have higher molecular weight, which yield many
monosaccharide molecules on hydrolysis. E.g. Starch, glycogen, Dextrin, Cellulose etc.

- In general monosaccharides and oligosaccharides are crystalline solids, soluble in water and sweet to taste,
they are collectively known as sugars, the polysaccharides on the other hand are amorphous, insoluble in
water and tasteless, they are called non-sugars.

6
  Different between monosaccharaides, oligosaccharides and Polysaccharides

Character Monosaccharaides Oligosaccharides Polysaccharides

No. of sugar molecules 1 2-9 More than 9
Glycoside bond Absent Present Present
Molecular Weight Low Moderate High
Taste Sweet Minimally sweet taste No taste
Solubility Soluble Soluble Insoluble
Nature Always reducing sugar May or may not be Always non reducing sugar
Glucose, Starch, Glycogen, Dextrin,
Example Sucrose, Maltose
fructose, Cellulose
Galactose

 Test for carbohydrate:

  Properties of Carbohydrates
- General properties of carbohydrates
Carbohydrates act as energy reserves, also stores fuels, and metabolic intermediates.
 Ribose and deoxyribose sugars forms the structural frame of the genetic material, RNA and DNA.
 Polysaccharides like cellulose are the structural elements in the cell walls of bacteria and plants.
 Carbohydrates are linked to proteins and lipids that play important roles in cell interactions.
 Carbohydrates are organic compounds; they are aldehydes or ketones with many hydroxyl groups.
- Physical Properties of Carbohydrates
 Steroisomerism - Compound shaving same structural formula but they differ in spatial
configuration. Example: Glucose has two isomers with respect to penultimate carbon atom. They are
D- glucose and L-glucose.
 Optical Activity - It is the rotation of plane polarized light forming (+) glucose and (-) glucose.
 Diastereo isomeers - It the configurational changes with regard to C2, C3, or C4 in glucose. Example:
Mannose, galactose.
 Annomerism - It is the spatial configuration with respect to the first carbon atom in aldoses and
second carbon atom in ketoses.
- Chemical Properties of Carbohydrates
 Ozazone formation with phenylhydrazine.
 Benedicts test.
 Oxidation
 Reduction to alcohols

Structure of Carbohydrates
- There are three types of structural representations of carbohydrates:
(i) Open chain structure.
(ii) Hemi-acetal structure.
(iii) Haworth structure.

8
 Functions of Carbohydrates
 Carbohydrates are chief energy source, in many animals; they are instant source of energy. Glucose
is broken down by glycolysis/ kreb's cycle to yield ATP.
 Glucose is the source of storage of energy. It is stored as glycogen in animals and starch in plants.
 Stored carbohydrates act as energy source instead of proteins.
 Carbohydrates are intermediates in biosynthesis of fats and proteins.
 Carbohydrates aid in regulation of nerve tissue and are the energy source for brain.
 Carbohydrates get associated with lipids and proteins to form surface antigens, receptor molecules,
vitamins and antibiotics.
 They form structural and protective components, like in cell wall of plants and microorganisms.
 In animals they are important constituent of connective tissues.
 They participate in biological transport, cell-cell communication and activation of growth factors.
 Carbohydrates those are rich in fibre content help to prevent constipation.
 Also they help in modulation of immune system.
 Example of Carbohydrates
- Monosaccharides - Glucose, galactose, glycerose, erythrose, ribose, ribulose, fructose.
- Oligosaccharides - Maltose, lactose, sucrose, raffinose, stachyose.
- Polysaccharides - Starch, glycogen, cellulose, pectin, inulin, hyaluonic acid.
 Foods rich in carbohydrates are referred to as strachy foods. They are found in legumes, starchy
vegetables, whole-grain breads and cereals. They also occur naturally with vitamins and minerals in foods
like milk, fruits, and milk products. They are alsdo found in refined and processed products like candy,
carbonated beverages, and table sugar.
 Examples of Polysaccharides

Name of the
Composition Occurrence Functions
Polysaccharide
Polymer of glucose containing a
straight chain of glucose molecules In several plant species
Starch (amylose) and a branched chain of storage of reserve
as main storage
glucose molecules (amylopectin) food
carbohydrate
Animals (equivalent of Storage of
Glycogen Polymer of glucose
starch) reserve food
In roots and tubers (like Storage of
Inulin Polymer of fructose
Dahlia) reserve food
Cellulose Polymer of glucose Plant cell wall Cell wall matrix
Pectin Polymer of galactose and its derivatives Plant cell wall Cell wall matrix
Hemi cellulose Polymer of pentoses and sugar acids Plant cell wall Cell wall matrix
Plant cell wall (dead
Lignin Polymer of glucose Cell wall matrix
cells like sclerenchyma)
Bodywall of arthropods. Exoskeleton
Chitin Polymer of glucose
In some fungi also Impermeable to
water
Cell wall of prokaryotic
Murein Polysaccharide cross linked with amino Structural
cells
acids protection
 Connective tissue
Ground
Hyaluronic acid Polymer of sugar acids matrix, Outer coat of substance,
mammalian eggs protection
Heparin Closely related to chrondroitin Connective tissue cells Anticoagulant
Gums - bark or trees. Retain water in dry
Gums and Polymers of sugars and sugar acids
Mucilages - flower seasons
mucilages

10
Lipids
The lipids include a large number of biomolecules of different types. The term lipid originated from a
Greek word ‘Lipos’ meaning fat. In general, those constituents of the cell which are insoluble in water and
soluble in organic solvents of low polarity (such as chloroform, ether, benzene etc.) are termed as lipids.
Lipids perform a variety of biological functions.

Classification of Lipids
Lipids are classified into three broad categories on the basis of their molecular structure and the
hydrolysis products.
(i) Simple Lipids: Those lipids which are esters and yield fatty acids and alcohols upon hydrolysis are
called simple lipids. They include oils, fats and waxes.
(ii) Compound Lipids: Compound lipids are esters of fatty acids and alcohol with additional
compounds like phosphoric acid, sugars, proteins etc.
(iii) Derived Lipids: Compounds which are formed from oils, fats etc. during metabolism. They include
steroids and some fat soluble vitamins.
Structure of lipids
The structure of all three types of lipids are briefly discussed below.

(i) Simple Lipids

The simple lipids are esters. They are subdivided into two groups, depending on the nature of
the alcohol component. Fats and oils are triglycerides, i.e. they are the esters of glycerol with
three molecules of long chain fatty acids. Variations in the properties of fats and oils is due to
the presence of different acids. These long chain acids may vary in the number of carbon
atoms (between C12 to C26) and may or may not contain double bonds. By definition, a fat
is that triglyceride which is solid or semisolid at room temperature and an oil is the one that
is liquid at room temperature. Saturated fatty acids form higher melting triglycerides than
unsaturated fatty acids. The saturated triglycerides tend to be solid fats, while the unsaturated
triglycerides tend to be oils. The double bonds in an unsaturated triglyceride are easily
hydrogenated to give a saturated product, and in this way an oil may be converted into a fat.
Hydrogenation is used in the manufacture of vanaspati ghee from oils.
Fats and oils are found in both plants and animals. Our body can produce fats from carbohydrates.
This is one method that the body has for storing the energy from unused carbohydrates. The vegetable
oils are found primarily in the seeds of plants.
The second type of simple lipids are waxes. They are the esters of fatty acids with long chain
monohydroxy alcohols 26 to 34 carbons atoms. Waxes are wide- spread in nature and occur usually as
mixtures. They form a protective coating on the surfaces of animals and plants. Some insects also
secrete waxes. The main constitutent of bees wax obtained from the honey comb of bees is myricyl
palmitate:

O
 The waxes discussed above should not be confused with household paraffin wax which is a
mixture of straight chain hydrocarbons.
(ii) Compound Lipids
Compound lipids on hydrolysis yield some other substances in addition to an alcohol and fatty
acids. The first type of such lipids are called phospholipids, because they are the triglycerides in
which two molecules of fatty acids and one molecule of phosphoric acid are present.
Glycolipids contain a sugar molecule in addition to fatty acid attached to an alcohol.
(iii) Derived Lipids
Steroids are another class of lipids which are formed in our body during metabolism. These
are the compounds with a distinctive ring system that provides the structural backbone for
many of our hormones. Steroids do not contain ester groups and hence cannot be hydrolysed.
Cholesterol is one of the most widely distributed steroids in animal and human tissues.

CH3
H3C

H3C CH3
H3C

HO (Cholesterol)

Another important group of derived lipids is that of fat-soluble vitamins. This

includes vitamins A, D, E and K, whose deficiency causes different diseases.

Biological Importance of Lipids

(i) Fats are main food storage compounds and serve as reservoir of energy.
(ii) Presence of oils or fats is essential for the efficient absorption of fat soluble
vitamins A, D, E and K.
(iii) Subcutaneous fats serve as biological insulator against excessive heat loss.
(iv) Phospholipids are the essential component of cell membrane.
(v) Steroids control many biological activities in living organisms.
(vi) Some enzymes require lipid molecules for maximum action.

- Lipids are a heterogeneous group of water-insoluble (hydrophobic) organic molecules that can be extracted
from tissues by nonpolar solvents, because of their insolubility in aqueous solutions, body lipids are
12
 generally found compartmentalized, as in the case of membrane-associated lipids or droplets of
triacylglycerol in adipocytes, or transported in plasma in association with protein, as in lipoprotein particles
or on albumin.
- Lipids are a major source of energy for the body, and they provide the hydrophobic barrier.
- Lipids serve additional functions in the body, for example, some fat-soluble vitamins have regulatory or
coenzyme functions, and the prostaglandins and steroid hormones play major roles in the control of the
body's homeostasis.
 General characters of lipids
- Lipids are relatively insoluble in water.
- They are soluble in non-polar solvents, like ether, chloroform, and methanol.
- Lipids have high energy content and are metabolized to release calories.
- Lipids also act as electrical insulators, they insulate nerve axons.
- Fats contain saturated fatty acids; they are solid at room temperatures. Example, animal fats.
- Plant fats are unsaturated and are liquid at room temperatures.
- Pure fats are colorless, they have extremely bland taste.
- The fats are sparingly soluble in water and hence are described are hydrophobic substances.
- They are freely soluble in organic solvents like ether, acetone and benzene.
- The melting point of fats depends on the length of the chain of the constituent fatty acid and the
degree of unsaturation.
- Geometric isomerism, the presence of double bond in the unsaturated fatty acid of the lipid molecule
produces geometric or cis-trans isomerism.
- Fats have insulating capacity, they are bad conductors of heat.
- Emulsification is the process by which a lipid mass is converted to a number of small lipid droplets. The
process of emulsification happens before the fats can be absorbed by the intestinal walls.
- The fats are hydrolyzed by the enzyme lipases to yield fatty acids and glycerol.
- The hydrolysis of fats by alkali is called saponification. This reaction results in the formation of glycerol
and salts of fatty acids called soaps.
- Hydrolytic rancidity is caused by the growth of microorganisms which secrete enzymes like lipases.
These split fats into glycerol and free fatty acids.
 Classification of lipids
1. Simple lipids: Esters of fatty acids with various alcohols.
a. Fats: Esters of fatty acids with glycerol. Oils are fats in the liquid state.
b. Waxes: Esters of fatty acids with higher molecular weight monohydric alcohols.
2. Complex lipids: Esters of fatty acids containing groups in addition to an alcohol and a fatty acid.
a. Phospholipids: Lipids containing, in addition to fatty acids and an alcohol, a phosphoric acid residue.
They frequently have nitrogen containing bases and other substituents, eg, in glycerophospholipids the
alcohol is glycerol and in sphingophospholipids the alcohol is sphingosine.
b. Glycolipids (glycosphingolipids): Lipids containing a fatty acid, sphingosine, and carbohydrate.
c. Other complex lipids: Lipids such as sulfolipids and aminolipids. Lipoproteins may also be placed in this
category.
3. Precursor and derived lipids: These include fatty acids, glycerol, steroids, other alcohols, fatty aldehydes,
and ketone bodies, hydrocarbons, lipid-soluble vitamins and hormones.
  Essential fatty acids
- Two fatty acids are dietary essentials in humans
(i) Linoleic acid, which is the precursor of arachidonic acid, the substrate for prostaglandin synthesis.
(ii) α-linolenic acid is the precursor for growth and development.
- Essential fatty acid deficiency can result in a scaly dermatitis, as well as visual and neurologic

abnormalities.
Linolenic acid Linoleic acid
 Regulating Blood Cholesterol Levels
- Fats and cholesterol cannot dissolve in blood and are consequently packaged with proteins (to form
lipoproteins) for transport
o Low density lipoproteins (LDL) carry cholesterol from the liver to the rest of the body
o High density lipoproteins (HDL) scavenge excess cholesterol and carry it back to the liver for disposal
- Hence LDLs raise blood cholesterol levels (‘bad’) while HDLs lower blood cholesterol levels (‘good’)
- High intakes of certain types of fats will differentially affect cholesterol levels in the blood
o Saturated fats increase LDL levels within the body, raising blood cholesterol levels
o Trans fats increase LDL levels and decrease HDL levels within the body, significantly
raising blood cholesterol levels
o Unsaturated (cis) fats increase HDL levels within the body, lowering blood cholesterol levels

 Lipid Health Claims

- There are two main health claims made about lipids in the diet:
o Diets rich in saturated fats and trans fats increase the risk of CHD
o Diets rich in monounsaturated and polyunsaturated (cis) fats decrease the risk of CHD

14
  Health Risks of High Cholesterol
- High cholesterol levels in the bloodstream lead to the hardening and narrowing of arteries (atherosclerosis)
- When there are high levels of LDL in the bloodstream, the LDL particles will form deposits in the
walls of the arteries
- The accumulation of fat within the arterial walls leads to the development of plaques which restrict blood
flow
- If coronary arteries become blocked, Coronary Heart Disease (CHD) will result – this includes heart
attacks and strokes

Examples of Lipids
- Fatty acids - Oleic acid, Linoleic acid, Palmitoleic acid, Arachidonic acid.
- Fats and Oils - Animal fats - Butter, Lard, Human fat, Herring oil.
Plant oils - Coconut oil, Corn, Palm, Peanut, Sunflower oil.
- Waxes - Spermacti, Beeswax, Carnauba wax.
- Phospholipids - Lecithins, Cephalins, Plasmoalogens, Phosphatidyl inositols, Sphingomyelins.
- Glycolipids - Kerasin, Phrenosin, Nervon, Oxynervon.
- Steroids - Cholesterol.
- Terpenes - Monoterpenes, Sesquiterpenes, Diterpenes, Triterpenes.
- Carotenoids - Lycopene, Carotenes, Xanthophylls.
16
Biological Role of Lipids

1. Food material: Lipids provide food, highly rich in calorific value. One gram lipid produces 9.3
kilocalories of heat.
2. Food reserve: Lipids provide are insoluble in aqueous solutions and hence can be stored readily in the
body as a food reserve.
3. Structural component: Lipids are an important constituent of the cell membrane.
4. Heat insulation: The fats are characterized for their high insulating capacity. Great quantities of fat are
deposited in the subcutaneous layers in aquatic mammals such as whale and in animals living in cold
climates.
5. Fatty acid absorption: Phospholipids play an important role in the absorption and transportation of fatty
acids.
6. Hormone synthesis: The sex hormones, adrenocorticoids, cholic acids and also vitamin D are all
synthesized from cholesterol, a steroidal lipid.
7. Vitamin carriers: Lipids act as carriers of natural fat-soluble vitamins such as vitamin A, D and E.
8. Blood cholesterol lowering: Chocolates and beef, especially the latter one, were believed to cause many
heart diseases as they are rich in saturated fatty acids, which boost cholesterol levels in blood and clog the
arterial passage. But researches conducted at the University of Texas by Scott Grundy and Andrea
Bonanome (1988) suggest that at least one saturated fatty acid stearic acid, a major component of cocoa
butter and beef fat, does not raise blood cholesterol level at all. The researchers placed 11 men on three
cholesterol poor liquid diets for three weeks each in random order. One formula was rich in palmitic acid,
a known cholesterol booster; the second in oleic acid; and the third in stearic acid. When compared with
the diet rich in palmitic acid, blood cholesterol levels were 14% lower in subjects put on the stearic acid
diet and 10% lower in those on the oleic acid diet.
9. Antibiotic agent. Squalamine, a steroid from the blood of sharks, has been shown to be an antibiotic and
antifungal agent of intense activity. This seems to explain why sharks rarely contract infections and almost
never get cancer.
 Proteins
- Proteins are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid
residues.
- Proteins are known as building blocks of life.
- Proteins are the most abundant intracellular macro-molecules. They provide structure, protection to the
body of multicellular organism in the form of skin, hair, callus, cartilage, ligaments, muscles, tendons.
Proteins regulate and catalyze the body chemistry in the form of hormones, enzymes, immunoglobulin’s
etc.
 General Characteristics of Proteins
- Proteins are organic substances; they are made up of nitrogen and also, oxygen, carbon an d hydrogen.
- Proteins are the most important biomolecules; they are the fundamental constituent of the cytoplasm of the
cell.
- Proteins are the structural elements of body tissues.
- Proteins are made up of amino acids.
- Proteins give heat and energy to the body and also aid in building and repair.
- Only small amounts of proteins are stored in the body as they can be used up quickly on demand.
- Proteins are considered as the bricks, they make up bones, muscles, hair and other parts of the body.
- Proteins like enzymes are functional elements that take part in metabolic reactions.
- Antibodies, blood haemoglobin are also made of proteins.
- Proteins have a molecular weight of 5 to 300 kilo-Daltons.
Physical Properties of Proteins
- Proteins are colorless and tasteless.
- They are homogeneous and crystalline.
- Proteins vary in shape, they may be simple crystalloid structure to long fibrilar structures.
- Protein structures are of two distinct patterns - Globular proteins and fibrilar proteins.
- Globular proteins are spherical in shape and occur in plants. Fibrilar proteins are thread-like, they occur
generally in animals.
- In general proteins have large molecular weights ranging between 5 X 103 and 1 X 106.
- Due to the huge size, proteins exhibit many colloidal properties.
- The diffusion rates of proteins are extremely slow.
- Proteins exhibit Tyndall effect.
- Proteins tend to change their properties like denaturation. Many a times the process of denaturation is
followed by coagulation.
- Denaturation may be a result of either physical or chemical agents. The physical agents include, shaking,
freezing, heating etc. Chemical agents are like X-rays, radioactive and ultrasonic radiations.
- Proteins like the amino acids exhibit amphoteric property i.e., they can act as Acids and Alkalies.
- As the proteins are amphoteric in nature, they can form salts with both cations and anions based on the net
charge.
- The solubility of proteins depends upon the pH. Lowest solubility is seen at isoelectric point, the
solubility increases with increase in acidity or alkalinity.
- All the proteins show the plane of polarized light to the left, i.e., laevorotatory.
Chemical Properties of Proteins
- Proteins when hydrolyzed by acidic agents, like conc.HCl yield amino acids in the form of their
hydrochlorides.
- Proteins when are hydrolyzed with alkaline agents leads to hydrolysis of certain amino acids like
arginine, cysteine, serine, etc., also the optical activity of the amino acids is lost.
18
- Proteins with reaction with alcohols give its corresponding esters. This process is known as esterification.
- Amino acid reacts with amines to form amides.
- When free amino acids or proteins are said to react with mineral acids like HCl, the acid salts are formed.
- When amino acid in alkaline medium reacts with many acid chlorides, acylation reaction takes place.
- Xanthoproteic test - On boiling proteins with conc. HNO3, yellow color develops due to presence of
benzene ring.
- Folin’s test - This i s a s p e c i f i c t e s t f o r t y r o s i n e a m i n o a c i d , w h e r e b l u e c o l o r
d e v e l o p s w i t h phosphomolybdotungstic acid in alkaline solution due to presence of phenol group.
Structure of Proteins
- Proteins are constructed by polymerization of only 20 different amino acids into linear chains.
- Proteins are the polymers of L-a-amino acids. The structure of proteins is rather complex which can be
divided into 4 levels of organization.
1. Primary structure:
o The linear sequence of amino acids forming the backbone of proteins (polypeptides).
o Examples of protein with a primary structure are Hexosaminidase, Dystrophin.
2. Secondary structure:
o The spacial arrangement of protein by twisting of the polypeptide chain.
o Example of protein with a secondary structure is Myoglobin.
3. Tertiary structure:
o The three dimensional structure of a functional protein.
o Number of forces act to hold the polypeptide chain in this final configuration:
 Polar/Nonpolar Interactions
 Hydrogen Bonds
 Van der Waals Forces
 Ionic Interactions
 Disulfide Bonds
o Examples of protein with a Tertiary structure are Globular Proteins (Enzymes) and Fibrous
Proteins.
4. Quaternary structure:
o Some of the proteins are composed of two or more polypeptide chains referred to as
subunits. The spacial arrangement of these subunits is known as quaternary structure.
o Examples of protein with a Quaternary structure are DNA polymerase, and ion channels.

20
Secondary Structure of Proteins
Shape
o Alpha Helix: Alpha Helix is a right-handed coiled rod-like structure.
o Beta Pleated Sheet: Beta sheet is a sheet-like structure.
Formation
o Alpha Helix: Hydrogen bonds form within the polypeptide chain in order to create a helical structure.
o Beta Pleated Sheet: Beta sheets are formed by linking two or more beta strands by H bonds.
Bonds
o Alpha Helix: Alpha helix has n + 4 H-bonding scheme. i.e. Hydrogen bonds form between N-H
group of one amino residue with C=O group of another amino acid, which is placed in 4 residues
earlier.
o Beta Pleated Sheet: Hydrogen bonds are formed in between the neighboring N-H and C=O groups of
adjacent peptide chain
-R group
o Alpha Helix: -R groups of the amino acids are oriented outside of the helix.
o Beta Pleated Sheet: -R groups are directed to both inside and outside of the sheet.
Number
o Alpha Helix: This can be a single chain.
o Beta Pleated Sheet: This cannot exist as a single beta strand; there are must be two or more.
Type
o Alpha Helix: This has only one type.
o Beta Pleated Sheet: This can be parallel, anti-parallel or mixed.
Qualities
o Alpha Helix: 100o rotation, 3.6 residues per turn and 1.5 Ao rise from one alpha carbon to the second
o Beta Pleated Sheet: 3.5 Ao rise between residues
Amino Acid
o Alpha Helix: Alpha helix prefers the amino acid side chains, which can cover and protect the
backbone H- bonds in the core of the helix.
o Beta Pleated Sheet: The extended structure leaves the maximum space free for the amino acid
side chains. Therefore, amino acids with large bulky side chains prefer beta sheet structure.
Preference
o Alpha Helix: Alpha helix prefers Ala, Leu, Met, Phe, Glu, Gln, His, Lys, Arg amino acids.
o Beta Pleated Sheet: Beta sheet prefers Tyr, Trp, (Phe, Met), Ile, Val, Thr, Cys.
22
Alpha Helix Secondary Beta pleate Antiparallel: Beta pleate Parallel:
Structure of Proteins when the adjacent Adjacent polypeptide chains
polypeptide chains run running in the same direction
in opposite
direction
  Protein Classification
1. Classification of Proteins Based on Shape
i. Globular or Corpuscular Proteins
- Globular proteins have axial ratio less than 10 but not below 3 or 4.
- They are compactly folded and coiled and possess a relatively spherical or ovoid shape.
- They are usually soluble in water and in aqueous media.
- Example: Insulin, plasma albumin, globulin enzymes.
Axial ratio, for any structure or shape with two or more axes, is the ratio of the length (or magnitude) of
those axes to each other - the longer axis divided by the shorter.
In chemistry or materials science, the axial ratio (symbol P) is used to describe rigid rod-like
molecules. It is defined as the length of the rod divided by the rod diameter.

ii. Fibrous or Fibrillar Proteins

- These proteins have axial ratio more than 10, hence, they resemble long ribbons or fibres in shape.
- They are mostly found in animals, and are not soluble in water or in solution of dilute acids.
- Fibrous proteins aid in protection and structural support.
- Example: Collagen, Keratin, Elastins, Fibroin

Classification of Proteins Based on Composition and Solubility

i. Simple Proteins or Holoproteins:

- These proteins are made of only one type of amino acid, as structural component, on decomposition with
acids, they liberate constituent amino acids. They are mostly globular type of proteins except for
scleroproteins, which are fibrous in nature.
- Simple proteins are further classified based on their solubility.
a) Protamines and histones
o These proteins occur only in animals and are basic proteins.
o They possess simple structure and low molecular, are water soluble and are not coagulated by heat.
o They are strongly basic in character due to the high content of lysine, arginine.
o Example: Protamines - salmine, clupine, cyprinine; Histones - nucleoshistones, globin.
b) Albumins
o They are widely distributed in nature, mostly seen in seeds.
o They are soluble in water and dilute solutions of acids, bases and salts.
o Example: Leucosine, legumeline, serum albumin.
c) Globulins
o They are of two types, pseudoglobulins which are soluble in water,
o Other is euglobulins which are insoluble in water.
o They are coagulated by heat.
o Example: Pseudoglobulin, serum globulin, glycinine. etc.
d) Scleroproteins or Albuminoids
o These occur mostly in animals and are commonly known as animal skeleton proteins.
o They are insoluble in water, and in dilute solution of acids, based and salts.

24
 ii. Conjugated or Complex Proteins or Heteroproteins:

- These are proteins that are made of amino acids and other organic compounds. The non-amino acid
group is termed as prosthetic group.
- Complex proteins are further classified based on the type of prosthetic group present.
a) Metalloproteins:
o These are proteins linked with various metals.
o Example: casein, collagen, ceruloplasmin, etc.
b) Chromoproteins
o These are proteins that are coupled with a colored pigment.
o Example: Myoglubin, hemocyanin, cytochromes, flavoproteins, etc.
c) Glycoproteins and Mucoproteins
o These proteins contain carbohydrates as the prosthetic group.
o Example: Glycoproteins - egg albumin, serum globulins, serum albumins;
Mucoproteins - Ovomucoid, mucin etc.
d) Phosphoproteins
o These proteins are linked with phosphoric acid.
o Example: casein.
e) Lipoproteins
o Proteins forming complexes with lipids are lipoproteins.
o Example: lipovitellin, lipoproteins of blood.
f) Nucleoproteins
o These are compounds containing nucleic acids and proteins.
o Example: Nucleoproteins, nucleohistones, nuclein.
g) Derived Proteins
o These are proteins that are derived from the action of heat, enzyme or chemical reagents.
o Derived proteins are of two types, primarily derived proteins and secondary derived proteins.
o Primary derived proteins
 Derivatives of proteins, in which the size of the protein molecule is not altered
materially.,.
 Primary derived proteins are classified into three types - Proteans,
Infraproteins and
Coagulated proteins.
 Example: edestan, coagulated egg-white.
o Secondary derived proteins.
 While in secondary derived proteins, hydrolysis occurs, as a result the molecules are
smaller than the original proteins.
 They are further classified into 3 types - Proteoses, Peptones and Polypeptides

EGG PROTEINS COMPOSITION OF EGG WHITE

Protein Percentage
Total protein 10-11% (on wet basis); 82.8% (on dry
basis)
Ovalbumin 70% of total proteins
Conalbumin 9%
Ovomucoid 13%
Lysozyme (G1) 2.6%
 Globulins Lysozyme (G2) 7%
Lysozyme (G3) 7%
Mucin 2%
Avidin 0.06%

26
 Classification of Proteins on Biological Function
i. Enzymic Proteins
- They are the most varied and highly specialized proteins with catalytic activity. Enzymes catalyze a
variety of reactions.
- Example: Urease, catalase, cytochrome C, etc.

ii. Structural Proteins

- These proteins aid in strengthening or protecting biological structures.
- Example: Collagen, elastin, keratin, etc.
iii. Transport or Carrier Proteins
- These proteins help in transport of ions or molecules in the body.
- Example: Myoglobin, hemoglobin, etc.
iv. Nutrient and Storage Proteins
- These proteins provide nutrition to growing embryos and store ions.
v. Contractile or Motile Proteins
- These proteins function in the contractile system.
- Example: Actin, myosin, tubulin, etc.
vi. Defense Proteins
- These proteins defend against other organisms.
- Example: Antibodies, Fibrinogen, thrombin.

vii. Regulatory Proteins

- They regulate cellular or metabolic activities.
- Example: Insulin, G proteins, etc.
viii. Toxic Proteins
- These proteins hydrolyze or degrade enzymes.
- Example: snake venom, ricin.

MILK PROTEINS
- Milk Protein contains about 0.6–0.7% protein which is not precipitated on acidification to pH 4.7.
- This represents about 20% of the protein contained in skim milk. These whey proteins are
separated into 2 fractions : lactalbumin and lactoglobulin.
- The name casein is assigned to the fraction precipitated by acidifying milk to a pH of 4.7. It is present in
cow’s milk (3-3.5%) and human milk (0.3-0.6%).
- Casein may be further purified by redissolving and precipitating again. It is of 3 types : α, β and γ.
  Function of Proteins
- Proteins are seen in muscles, hair, skin and other tissues; they constitute the bulk of body's non-
skeletal structure.
Example: The protein keratin is present in nails and hair.
- Some proteins are hormones and regulate many body functions. Example: Insulin hormone is a
protein and it regulated the blood sugar level.
- Some proteins act enzymes, they catalyze or help in biochemical reactions. Example: Pepsin and Tripsin.
- Some proteins act as antibodies; they protect the body from the effect of invading species or substances.
- Proteins transport different substances in blood of different tissues. Example: Haemoglobin is an
oxygen transport protein.
- Contractile proteins help in contraction of muscle and cells of our body. Example: Myosin is contractile
protein.
- Fibrinogen a glycoprotein helps in healing of wounds. It prevents blood loss and inhibits passage of
germs.

28
NUCLEIC ACIDS
The study of the chemistry of heredity is one of the most fascinating fields of research today. It was
recognized in the 19th century that the nucleus of a living cell contains particles responsible for heredity,
which were called chromosomes. In more recent years, it has been discovered that chromosomes are
composed of nucleic acids. These are named so because they come from the nucleus of the cell and are
acidic in nature. Two types of nucleic acids exist which are called DNA (deoxyribonucleic acid) and
RNA(ribonucleic acid).They differ in their chemical composition as well as in functions.

Structure of Nucleic Acids

Like all natural molecules, nucleic acids are linear polymeric molecules. They are chain like polymers of
thousands of nucleotide units, hence they are also called polynucleotides. A nucleotide consists of three
subunits: a nitrogen containing heterocyclic aromatic compound (called base), a pentose sugar and a
molecule of phosphoric acid. So a nucleic acid chain is represented as shown below.

base base base

— Sugar — — sugar — phosphate — sugar —

phosphate n

29
In DNA molecules, the sugar is 2-deoxyribose, whereas in RNA molecules it is ribose. In DNA, four bases
have been found. They are adenine (A), guanine (G), cytosine (C) and thymine (T). The first three of these
bases are found in RNA also but the fourth is uracil (U).

The sequence of different nucleotides

in DNA is termed as its primary 3 - 5 -end
structure. Like proteins, they also end
have secondary structure. DNA is a
double stranded helix. Two nucleic
acid chains are wound about each
other and held together by hydrogen

Minor
groove

bonds between pairs of bases. The PS A T S P

hydrogen bonds are specific between T A S 3.4 mm

P P
pairs of bases that is guanine and S
C
C P

cytosine form hydrogen bonds with Major groove S C C S

each other, whereas adenine forms
hydrogen bonds with thymine. The
two stands are complementary to
each other. The overall secondary
structure resembles a flexible ladder 3 -end 5 -end
(Fig. 29.4). This structure for DNA
2.0 mm
was proposed by James Watson and Watson and Crick’s double helix structure of DNA
Francis Crick in 1953. They were
honoured with a Nobel Prize in 1962
for this work.

Unlike DNA, RNA is a single stranded molecule, which may fold back on itself to form double helix
structure by base pairing in a region where base sequences are complimentary. There are three types of
RNA molecules which perform different functions. These are named as messenger RNA(m-RNA),
ribosomal-RNA(r-RNA) and transfer RNA (t-RNA)

Biological Functions of Nucleic Acids

A DNA molecule is capable of self duplication during cell divisions. The process starts with the unwinding
of the two chains in the parent DNA. As the two strands separate, each can serve as a master copy for the
30
construction of a new partner. This is done by bringing the appropriate nucleotides in place and linking
them together. Because the bases must be paired in a specific manner (adenine to thymine and guanine to
cytosine), each newly built strand is not identical but complimentary to the old one. Thus when replication is
completed, we have two DNA molecules, each identical to the original. Each of the new molecule is a
double helix that has one old strand and one new strand to be transmitted to daughter cells (Fig. 3.15).

31
 OLD OLD
A T
T A
A T

O C
O C
T A
C O

A T
O C
C O
A T

T A
C O
A T
C O
C O C
OC O C
O

T A T A
A T A T
T A T A
T A T A

A T A T
T A T
AT A T
A
OLD NEW NEW OLD
Replication of DNA
Another important function of nucleic acids is the protein synthesis. The specific sequence of bases in DNA
represents coded information for the manufacture of specific proteins. In the process, the information
from DNA is transmitted to another nucleic acid called messenger RNA, which leaves the nucleus and
goes to the cytoplasm of the cell. Messenger RNA acts as template for the incorporation of amino acids in the
proper sequence in protein. The amino acids are brought to the messenger RNA in the cell, by transfer RNA.
Where they form peptide bonds. In short it can be said that DNA contains the coded message for protein
synthesis whereas RNA actually carries out the synthesis of protein.
1. .

32
ENZYMES
In a living system, many complex reactions occur at the temperature of about 310K. An example of this
is the digestion of food, during which stepwise oxidation to CO2 and water and energy production. These
reactions are carried out under such mild conditions due to presence of certain chemicals which are called
enzymes. They act as catalysts for biochemical reactions in living cells. Almost all the enzymes are globular
proteins.
Enzymes are very selective and specific for a particular reaction. They are named after the compound or
class of compounds upon which they work or after the reaction that they catalyze. The ending of an
enzyme name is- ase. For example, maltase is an enzyme that specifically catalyzes the hydrolysis of
maltose into glucose. Similarly, an esterase is an enzyme which induces hydrolysis of ester linkage.

Mechanism of Enzyme Action

Just like chemical catalysts, enzymes are needed only in small quantities. Similar to the action of chemical
catalysts, enzymes lower the energy barrier that reactants must pass over to form the products. For
example, hydrolysis of the ester that needs boiling with aqueous NaOH in the laboratory, whereas it
occurs at nearly neutral pH and at moderate temperature when catalyzed by an enzyme.
There is a particular enzyme for each substrate and they are said to have lock and key arrangement. It is
said that first the substrate molecule binds to the active site of the enzyme which results in the formation
of an enzyme-substrate complex. In this complex, the substrate is placed in the right orientation to
facilitate a given reaction (Fig.29.6). This complex then breaks to give the molecule of the product and
regenerates the enzyme for the next molecule of the substrate.

Lock and Key arrangement of enzyme action

Characteristics of Enzymes
(i) Enzymes speed up biochemical reactions up to ten million times compared
to the uncatalysed reaction.

(ii) Enzyme catalysed reactions rapidly attain equilibrium.

(iii) Enzymes function in dilute aqueous solutions, at moderate temperatures and at a specific
pH.
(iv) They are very specific and selective in their action on substrates.
(v) Enzymes are highly efficient and are needed in small amounts only.
(vi) In addition to the protein structure, most active enzymes are associated with some non-
protein component required for their activity, called coenzymes. For example nicotinamide

33
MICROBES

BACTERIA

Bacteria are typically one celled organisms. Although some forms of such microbes must have been
present ever since life began on earth, yet they remained unnoticed until Antony Von Leeuwenhoek
discovered them in 1683 using lenses made by him.

Bacteria are the oldest, the most numerous and diversified forms of life on earth and are distributed
universally. They are present everywhere, can exist in all kinds of situations and some of them can
withstand even extreme temperatures. They are present in soil, water, air, sewage, waste, depths of
ocean, streams, springs, the food we take, the water we drink, the objects we touch and even on or
inside our bodies. There is hardly any aspect of our life (food, cloth, shelter, health) that is not
directly or indirectly affected by the growth of microbes.

Chemically bacteria are very active. When they grow on a material, they cause several changes such
as fermentation (decomposition of carbohydrates), putrefaction (decomposition of proteins) and a
few species of bacteria can even break down fat to fatty acids. Several species of bacteria have the
ability to produce complicated organic compounds, i.e. pigments. An extremely important property
of certain pathogenic bacteria is their ability to produce exotoxins/endotoxins and through the
knowledge of these pathogenic microbes, we as individuals can be in a better position to combat
them.

Glycogen
granules

Vacuole
granules
Flagella Capsule
Basal granule

Cell wall

Cytoplasm

Cytoplasmic
membrane
Ribosomes

Nuclear body

Schematic diagram of a bacterial cell (highly magnified)

34
1) Flagella
They are the organs of locomotion. They are fine hair-like protein fibrils
attached to the cell in various locations and each flagellum originates from
a basal granule. They are present in motile bacteria and in some spiral
forms. The number and arrangement of flagella are characteristic for each
bacterium. Flagella may be arranged on bacteria in four ways as shown in
Fig. 1.3.
a) Monotrichate: A single flagellum at one end of the cell. Example: Cholera vibrios.
b) Amphitrichate: Two flagella, one at each pole. Example: Alcaligenes faecales.
c) Lophotrichate: A tuft of flagella at one or both ends. Example: Pseudomonas.
d) Petritrichate: Several flagella present all over the surface. Example: Salmonella typhi.

Monotrichate Lophotrichate

Peritrichate

Amphitrichate

Arrangements of flagella

2) Capsule
Some bacterial cells are surrounded by a thick protective gelatinous layer known as
capsule. It is concerned with the virulence of the bacterium, e.g. diplococcus pneumoniae.

35
 Distinction between the cell wall and capsule is not always clear. When the capsule is in the form of a
loose secretion, it is called a slime layer and if it is too thin it is known as microcapsule.
3) Cell Wall
It is present just beneath the capsule or slime layer. It is tough, somewhat rigid and gives shape to the cell.
It forms a rigid frame and protects the cell from damage. It varies in thickness, rigidity and in chemical
composition. Gram positive bacteria have a simpler chemical composition as compared to Gram negative
bacteria. Bacterial cell wall is composed of cellulose, protein and lipid.
4) Cytoplasmic Membrane
The cell membrane in bacteria is very thin, weak, highly flexible and it is commonly called as cytoplasmic
membrane. It is a thin layer lining the inner surface of the cell wall and separates it from the cytoplasm. It
acts as a semipermeable membrane and controls the passage of nutrients and waste products into and out
of the cell. Damage to this membrane results in leaking the vital material out of the cell and the cell
ultimately dies. Chemically it consists of lipoprotein with a small amount of carbohydrate.
5) Cytoplasm
Inside the cell bounded by the cytoplasmic membrane is a clear watery substance called cytoplasm,
which is slightly viscous and homogeneous in appearance. It is a colloidal system containing a variety of
macromolecules (proteins, nucleic acid, polysaccharides and lipids), organic and inorganic solutes.
Cytoplasm contains ribosomes, mesosomes, vacuoles and stored food granules viz. glycogen and
volutin.
a) Ribosomes: These are in the form of tiny granules and are the centre of protein synthesis.
b) Mesosomes: These are formed by the invagination of the cytoplasmic membrane and are the
principal sites of the respiratory enzymes.
c) Vacuoles: These are fluid containing cavities.
d) Glycogen and Volutin Granules: These are stored food granules.
6) Nuclear Body (Nucleus)
The nucleus of bacteria for a long time was a controversial structure. In the past, some considered the
entire bacterial cell as a nucleus and others regarded the staining body in the centre as nucleus. Feulgen
stain reveals the presence of primitive form of nucleus in bacteria consisting of a long filament of
deoxyribose nucleic acid (DNA) tightly coiled inside the cytoplasm. It represents the chromosome and is
responsible for transmission of hereditary characters. DNA replicates and is equally distributed among
the daughter cells. A bacterial cell has no nuclear membrane or nucleous. An organised nucleus as found
in animals and higher plants is absent in bacteria.

Reproduction
Most common method of reproduction in bacteria is by transverse binary fission which occurs under
favourable conditions. This is illustrated in Fig. 1.4. In this method the parent cell elongates, the cell wall
invaginates, the transverse wall is formed which separates the parent cell into two daughter cells. Each
daughter cell repeats the process. Thus after every twenty minutes, a bacterial cell divides by transverse
fission into two. Sometimes bacterial population, when they are growing, produce substances such as
alcohol or acids which are toxic to them and cause a decrease in the rate of reproduction. Thus, the
number of new cells produced is almost equal to the number of cells that die and the steady population is
normally maintained. Sometimes the death rate even exceeds to the rate of reproduction and all cells may
die

36
Spore Formation
Some types of bacteria particularly members of the genus bacillus and
clostridium under unfavourable conditions have the capability to form
highly resistant resting stages called spores. Since in bacteria these spores
are formed inside the parent cells, they are called endospores. In the
process of spore formation, protoplasm within the cell concentrates into a
small sphere which develops its own thick wall to form an endospore.

Terminal Subterminal Central

Types of Spores
Morphological Classification of Bacteria

Bacteria

a) Cocci (Spherical) b) Bacilli (Rod shaped) c) Spirilli (Spiral shaped)

i) Micrococci e.g. i) Microbacilli i) Vibrio (comma shaped)

Micrococcus pyogenes e.g. Brucella e.g. Vibrio cholerae

ii) Diplobacilli e.g. ii) Spirilla (short, rigid,

ii) Diplococci
Klebsiella pneumoniae spiral shaped) e.g.
e.g. Diplococcus
Spirilla
pneumoniae
iii) Streptobacilli iii) Spirochaetes (long,
iii) Neisseria e.g. Bacillius anthracis flexible, spiral shaped)
e.g. Treponema
iv) Chinese letter pattern pallidum and Leptospira
iv) Streptococci e.g. Corynebacterium
e.g. Streptcoccus diphtheriae
v) Staphylococci e.g.
v) Branched filaments
Staphylococcus aureus e.g. Actinomycetes

vi) Sarcina e.g. Sarcina vi) Coccobacilli

lutea e.g. Brucella

37
 Cocci (Spherical Bacteria)

These are spherical or oval in shape about 1 micron (v) in diametre. Many bacteria of this form
exhibit patterns of arrangement that are important for identification purposes and are characteristic
of particular species of bacteria.
1. Micrococci: These are found singly or in small clusters like bunches of grapes, e.g.
micrococcus pyogenes causing boils on skin.
2. Diplococci: These are cocci in pairs, e.g. diplococcus pneumoniae which causes pneumonia.
3. Neisseria: These are cocci in pairs but bean shaped, e.g. neisseria gonorhoeae and
N. meningitis.
4. Streptococci: These are cocci in chains, e.g. streptococcus lactis which causes souring milk and
cheese.
5. Staphylococci: These are cocci in clusters, e.g. staphycoccus aureus causing pyogenic
infection.
6. Sarcina: These are cocci in packet arrangement with 8 or more cells. They divide in three planes at
right angles to one another resulting in a regular pattern of cubes or packets of cells, e.g. sarcina
lutea found in water, air and soil.

38
 Micrococci Diplococci

Neisseria gonorrhoeae Neisseria meningitis

Staphylococci Streptococci

Sareina

Shapes and arrangements of cocci

Bacilli (Rod Shaped Bacteria)

i) Microbacilli: They occur as single unattached cells, e.g. Brucella.
ii) Diplobacilli: They occur in pairs, e.g. klebsiella pneumoniae.
iii) Streptobacilli: They are found in chains, e.g. bacillus anthracis.
iv) Chinese letter pattern: They are arranged in straight, V, L, I, Y
39
 shapes, i.e. Chinese letter pattern, e.g. corynebacterium diphtheriae.
v) Branched Filaments: They may be arranged in the form of branched filaments, e.g.
actinomycetes.
vi) Coccobacilli: Sometimes in bacilli the length may approximate
the width of the organism. Such organisms are called cocobacilli,
e.g. brucella.
Spirilli (Spiral Shaped Bacteria)
They are curved or spiral shaped motile bacteria. They occur mostly as
unattached individuals found freely in water. The individual cells of
different species show striking differences in length, number of coils and
rigidity of cell walls. They are of three types:
Microbiology-

Microbacilli
Diploba
cilli Streptobacilli

Chinese Letter Coccobacilli

Pattern
Actinomy
cetes

Shapes and arrangements of bacilli

40
 Spirilla
Vibrio cholerae

Treponema pallidum
(Spirochaete)

Leptospira
(Spirochaete)

Different types of spirilli

1. Vibrio: Vibrio is a short curved comma shaped Gram negative motile bacteria. The pathogenic species is
Vibrio cholerae which causes cholera in human being.
2. Spirilla: They are short rigid spiral shaped organisms found freely in water. They have very few wavy
bands along the long axis, e.g. spirilla.
3. Spirochactes: They are thin long spiral flexible organisms. They are able to wriggle, flex and bend
themselves like coiled steel spring. Many spirochaetes are free living found in water, soil and decaying
organic matters while others occur as commensals in the human mouth and genitalia and some are
pathogenic to human being.

41
 FUNGI
Fungi are placed in plant kingdom in the division. Thallophyta which are
irregular plant masses and the body is not differentiated into root, stem and
leaves. Thallophyta is divided into two groups; Algae and Fungi. Algae are
larger, grow in water, possess chlorophyll, prepare their own food and
cannot live in darkness. On the other hand, fungi are smaller, live as
parasites or saprophytes on decaying organic matter, do not possess
chlorophyll, cannot prepare their own food and can live in darkness. For
present purposes, we may disregard Algae since none is pathogenic to
human being.

MORPHOLOGICAL CLASSIFICATION OF FUNGI

To combat the fungi which cause disease in human being, we should learn
in brief the morphology and their living conditions. Based on morphology,
fungi can be divided into four groups, viz. yeasts, yeast like fungi, moulds
(Filamentous fungi) and dimorphic fungi as shown below in Table 1.3).

Morphological Classification of Fungi

Fungi

Yeasts Yeast like fungi Moulds (Filamentous Dimorphic fungi

Round or oval Partly as round oval fungi) True Mycelia Exist either as yeast
unicellular e.g. yeasts and partly as with aerial and or filaments
Cryptococcus chains of cells vegetative mycelia e.g. Histoplasma
neoformans forming e.g. capsulatum &
psuedomycelium Penicillium, Aspergillus, Blastomyces
e.g. Candida Mucor & Rhizopus
albicans

42
Yeasts
Yeast cells are round or oval unicellular microscopic organisms much larger than
bacteria. They have no flagella or any other structure for locomotion. They are mostly
saprophytic fungi and grow abundantly in organic substances rich in sugar. They are also
found in soil, animal excreta and in air. Some yeasts also occur as parasites on humans.
The only important yeast pathogenic to human being is cryptococcus neoformans.

Yeast cells normally divide by budding and form spores. The yeast cells as well as spores
are carried away by insect carriers, by wind or by aerial currents and remain widely
distributed in nature.
Yeast Like Fungi
They are oval yeast like fungi. They grow partly as round oval yeast cells and partly as
chains of elongated budding cells forming pseudomycelium. Example: Candida
albicans (Monilia albicans) which causes the disease Candidiasis (Moniliasis) in
humans.

43