Biomolecules.

Biomolecules are the organic compounds which form the basis of life, i.e.,
they build up the living system and responsible for their growth and
maintenance.

The sequence that relates biomolecules to living organism is

Biomolecules → Organelles → Cells → Tissues → Organs → Living organism.

Carbohydrates
Optically active polyhydroxy aldehydes (aldcses) or ketones (ketoses) or
compounds which on hydrolysis give these units are known as
carbohydrates. They are also called saccharides

(Latin Saccharum = sugar) due to sweet taste of simpler members.

Depending upon their behaviour towards hydrolysis, carbohydrates can be of

following three types

Monosaccharides
These cannot be hydrolysed to simpler molecules and further subdivided into
tetroses, pentoses or hexoses depending upon the number of carbon atoms.
These are also called homopolysaccharides.

 Aldotetroses Erythrose, Threose

 Aldopentoses Xylose, Ribose,
 Aldohexoses Glucose, Galactose,
 Ketohexoses Fructose
All naturally occurring monosaccharides belong to D-series.

killiani synthesis is used to convert an aldose into next higher aldose.

Oligosaccharides
(Greek oligos = few). On hydrolysis, they generally give two to nine
monosaccharides (same or different) and are further classified as
disaccharides, e.g., sucrose, maltose, lactose, trisaccharides and so on.
C H O is a disaccharide because it gives two monosaccharides.
12 22 11

The bond formed between two monosaccharides is called a glycosidic bond

and normally it is (1, 4) bond.

Sucrose is most abundant in plants and known as cane sugar or table sugar
or invert sugar as equimolar mixture of glucose and fructose is obtained by
hydrolysis of sucrose.

Trisaccharides Raffinose (C H O ) 18 32 16

Polysaccharides
These are polymers of monosaccharides. Examples are starch, cellulose,
glycogen, etc.

1. Starch, (C H O )
6 10 5 N

It is a polymer of a-glucose and a major reserve food in plants. It turns blue

with iodine. It is a mixture of two components:

1. Amylose (20%), an unbranched water soluble polymer.

2. Amylopectin (80%), a branched water insoluble polymer.

Sources of starch are potatoes, wheat, rice, maize, etc.

2. Cellulose, (C H O )
6 10 5 n

It is the most abundant and structural, polysaccharide of plants. It is

important food source of some animals It is a polymer of D (+) β-glucose.

The chief sources of cellulose are wood (Contains 50% cellulose rest being
lignin, resins, etc) and cotton (contains 90% cellulose rest being fats and
waxes).
Several materials are obtained from cellulose:
1. Mercerised cotton Cellulose treated with cone. sodium hydroxide solution
acquire silky lustre. It is called mercerissd cotton.
2. Gun cotton It is completely nitrated cellulose (cellulose nitrate), highly
explosive in nature and is used in the manufacture of smokeless gun powder,
called blasting gelatin.
3. Cellulose acetate It is used for making acetate rayon and motion picture
films.
4. Cellulosexanthate It is obtained by treating cellulose with sodium hydroxide
and carbon disulphide and is the basic material for VISCOSE rayon.
Oligosaccharides and heteropolysaccharides are also called
heteropolysaccharides.

Reducing and Non-reducing sugars

Based upon reducing and non-reducing properties, carbohydrates are
classified as reducing and non-reducing sugars. Carbohydrates reducing
Fehling reagent or Tollen’s reagent are termed as reducing carbohydrates.
e.g., All monosaccharides and disaccharides (except sucrose). But
carbohydrates which do not reduce such reagents are known as non-
reducing carbohydrates. e.g., sucrose and polysaccharides.

Sugars and Non-sugars

On the basis of their, taste, carbohydrates are classified as sugars and non-
sugars. The monosaccharides and oligosaccharides having sweet taste are
collectively known as sugars. Polysaccharides which are insoluble in water
and not sweet in taste, are non-sugars.

Glucose
Dextrose, grape sugar, corn sugar, blood sugar (C H O ).
6 12 6

Manufacture
By hydrolysis of starch with hot dil mineral acids and by hydrolysis of
sucrose.

Extra glucose is stored in liver as glycogen.

α and β glucose
In intermolecular hemiacetal formation (cyclic structure), -CHO is converted
into -CHOH which can have two configurations as shown below.

Glucose having (i) configuration about C is the α-glucose and having (ii)
1

configuration about C is β-glucose.

1

The carbon C is known as anomeric carbon and these compounds are called
1

anomers. Both the forms are optically active. ex-D-glucosehas specific

rotation +111.5° and β-D-glucose has specific rotation + 19.5°.
Mutarotation
When either of the two forms of glucose is dissolved in water, there is a
spontaneous change in specific rotation till the equilibrium value of +52.5°.
This is known as mutarotation.
Properties of glucose
Glucose has one aldehyde group, one primary hydroxyl (-CH OH) and four
2

secondary hydroxyl (-CHOH) groups and gives the following reactions:

These reactions confirm the presence ofa carbonyl group in glucose.

(iii) Glucose reduces ammoniacal silver nitrate solution (Tollen’s reagent) to

metallic silver and also Fehling’S solution or Benedict solution to reddish
brown cuprous oxide (Cu O) and itself gets oxidised to gluconic acid. This
2

confirms the presence of an aldehydic group in glucose.

(iv) With mild oxidising agent like bromine water, glucose is oxidised to
gluconic acid. Glucose on oxidation with nitric acid gives saccharic acid.
(vii) Glucose on reaction with methyl alcohol in the presence of dry HCl(g)
forms α and β-methyl glycosides. The reaction occurs only at the OH of
hemiacetylic carbon.

Cyclic structure of glucose Given by Haworth and Hirst.

Fructose Fruit Sugar (C H O )
6 12 6

Manufacture
By hydrolysis of inulin.

α and β-fructose
The two forms have different configuration about C .2

Fructose does not reduce Br water.

2

Epimers
Monosaccharides differing in configuration at a carbon other than anomeric
carbon are called epimers, e.g., glucose and galactose differ in configuration
at C , hence called epimers.
4

Osazones
Monosaccharides and reducing disaccharides react with excess of phenyl
hydrazine to form crystalline substances of the structure

It is known as osazones glucose and fructose give same osazone.

Molisch Test for Carbohydrates

In aqueous solution of compound add solution of α-naphthol in alcohol and
then cone. H SO along the walls of the test tube. Purple coloured ring is
2 4

obtained at the junction.

Amino Acids
The compounds containing amino group (-NH ) and carboxylic group (-COOH)
2

are called amino acids.

R = H, alkyl or aryl group. Except glycine (H N.CH COOH), others are optically
2 2

active in nature.
Classification of Amino Acids

Essential and Non-essential Amino Acids

Human body can synthesise ten amino acids, called non-essential amino
acids. The remaining ten amino acids required for protein synthesis are not
synthesised by body and are called essential amino acids. They are

1. Phenylalanine

2. Histidine

3. Tryptophan

4. Valine

5. Methionine

6. Threonine

7. Arginine

8. Leucine

9. Isoleucine

10.Lysine

Nomenclature
They are known by their common names and abbreviated by first three
letters of their common names e.g., glycine as ‘gly’ and alanine a as ‘ala’.
Peptides
Peptides are condensation products of two or more amino acids.

Two molecules of different amino acids can form two dipeptides.Three

molecules of different amino acids can give six tripeptides.

Dipeptide has only one peptide bond, tripeptide has two peptide bonds and
so on. Thus, a polypeptide made up of n-amino acids has (n – 1) peptide
bonds.
Polypeptides
Condensation Products of many amino acids ( ‘In P xiucts of many amino
acids (≈ 10000) is known as polypeptide and those polypeptides which have
molecular mass above than 10000 are called proteins.

Proteins
They are linear polymers of a-amino acids.

Structure of Proteins
(a) Primary structure
It simply reveals the sequence of amino acids.

(b) Secondary structure α-helix structure maintained by hydrogen bonds

or β-pleated sheet structure when R is small group.
(c) Tertiary structure The folding and superimposition of polypeptide
chains forms a compact globular shape, termed as tertiary structure. It is
stabilised by covalent, ionic, hydrogen and disulphide bonds.
The precise arrangement constitutes the quaternary structure.

Classification on the Basis of Hydrolysis Products

(i) Simple These yield only a-amino acids upon hydrolysis.
e.g., albumin.

(ii) Conjugated proteins These yield α-amino acids and non-protein part,
called prosthetic group.
Prosthetic
Protein group

Nucleoprotein
s Nucleic acid

Phospho Phosphoric
proteins acid

Carbohydrate
Glycoproteins s
 Metalioprotein
s Metals

Lipoproteins Lipids

(iii) Derived proteins These are obtained by partial hydrolysis of simple or

conjugated proteins.
Proteins → Proteoses → Peptones → Polypeptides

Classification on the Basis Functions

1. Structural proteins Fibrous proteins
2. Enzymes Serve as biological catalyst e.g., pepsin, trypsin etc.
3. Hormones Insulin
4. Contractile proteins Found in muscles, e.g., myosin, actin.
5. Antibodies Gamma globulins present in blood.
6. Blood protein Albumms, haemoglobin and fibrinogen.
Haemoglobin is a globular protein. Its prosthetic group is heme. It Contains
574 amino acid units distributed in four polypeptide chains.

Two chains containing 141 amino acid residues each are called α-chains and
the two chains containing 146 amino acid residues are called β-chains.

Sickle cell anaemia is caused by defective haemoglobin obtained by

replacing only one amino acid, i.e., glutamic acid by valine.

Denaturation of Proteins
The process that changes the three dimensional structure of native proteins
is called denaturation of proteins. It can be caused by Change in pH, addition
of electrolyte, heating or addition of solvent like water, alcohol or acetone.

Tests of Proteins
(i) Biuret Test
Protein solution + NaOH + dil. CuSO → pink or violet colour.
4

(ii) Millon’s Test

Protein solution + Millon’s reagent → pink colour
Millon’s reagent is solution of mercuric nitrate and nitrite in nitric acid
containing traces of nitrous acid.

(iii) Iodine reaction

Protein solution + iodine in potassium iodide solution → yellow colour.

(iv)Xanthoprotic test

Enzymes
Enzymes constitute a group of complex proteinoid compounds, produced by
living organisms which catalyse the chlemical reaction.

Non-proteinous components enhance the activity of certain enzymes and are

known as co-enzymes. These include metal ions like Mn , Mg , K , Na , Zn ,
2+ 2+ + + 2+

Co etc., heterocyclic ring systems (pyrrole, purine, pyridine, etc.), a sugar

2+

residue, phosphoric acid residue of vitamins like thiamine, riboflavin etc.

Endoenzyme acts in the same cell in which it is synthesised, while exo-
enzyme acts outside the cell in which it is synthesised.
Nomenclature
They are usually named by adding the suffix ‘ase’ to the root name of the
substrate e.g., urease, maltase, diastase, invertase, etc.

Oxidative Enzymes
They catalyse oxidation-reduction reaction and are mostly conjugated
proteins.

Some Common Enzyme

Name Substrate Products

CO₂ +
Urease Urea NH₃

Maltase Maltose Glucose

 Invertase Sucrose Glucose + fructose

Amylase Starch Maltose

Trypsin Proteins Amino acids

Ascorbic acid Ascorbic

oxidase acid Dehydroascorbic acid

Characteristic Features of Enzymes

1. Rate of reaction They increase the rate of reaction up to 10 to 10 times.
6 7

2. Specific nature Urease catalyse the hydrolysis of urea and not methyl urea,
so these are specific in nature.
3. Optimum temperature It is about 20-30°C.
4. pH of medium It is about 7 but for pepsin, it is 1.8·2.2 and for trypsin, it is
7.5-8.3.
5. Concentration Dilute solutions are more effective.
6. Amount of enzyme Very small amount can accelerate the reaction.
7. Enzyme inhibitors These compounds inhibit the enzyme action. With the
help of such compounds, the reaction can be controlled.
Mechanism of Enzyme Action
Enzyme + Substrate → [Enzyme substrate] → Product + Enzyme Activated
complex

Applications of Enzymes
(i) Treatment of diseases The congenital disease phenyl ketonurie caused
by phenylalanine hyroxylase can be cured by diet of low phenylalanine
content. Enzyme streptokinase is used for blood clotting to prevent heart
disease.
(ii) In industry Tanning of leather, fermentation process etc.
Nucleic Acids
Important Terms of Nucleic Acids
1. Nucleotldes
Nucleotides consist of 5-carbon sugar + nitrogenous base + 1, 3-phosphate
groups.
2. Pentose sugar
It is either ribose or deoxy ribose (not having oxygen at C ).
2

3. Nitrogenous base
Derived from purines having two rings in their structure e.g., Adenine (A) and
Guanine (G) and derived from pyrimidines having one ring in their structure
e.g.,

Thymine (T), Uracil (U) and Cytosine (C).

Two H-bonds are present between A and T (A = T) while three H-bonds are
present between C and G (C ≡ G).

4. Ribonucleotide
Phosphate unit + Ribose + one base unit from A, G, C, or U.

5. Deoxyrlbo nucleotide
Phosphate unit + Deoxyribose + one base from A, G, C or T.

6. Nucleoside
Ribose-/deoxyribose + one base unit from A, G, C, Tor U.

DNA and RNA

Nucleic acid is polynucleotide, present in the living cells or bacterial cells
having no nucleus and in viruses having no cells.

(i) DNA Deoxy ribonucleic acid.

DNA + H 2O → Phosphoric acid + deoxyribose + A, G, C, T

(ii) RNA Ribonucleic acid

RNA + H 2O → Phosphoric acid + Ribose + A, G, C, U

Structure of DNA
It consists of two polynucleotide chains, each chain form a right handed
helical spiral with ten bases in one turn of the spiral. The two chains coil to
double helix and run in opposite direction. These are held together by
hydrogen bonding.

Structure of RNA
It is usually a single strand of ribonucleotides and take up right handed
helical conformation. Up to 12000 nucleotides constitute an RNA.

It can base pair with complementary strands of DNA or RNA according to

standard base pairing rules-G pairs with C, A pairs with U or T. The paired
strands in RNA-RNA or RNA-DNA are anti parallel as in DNA.

In both DNA and RNA, heterocyclic base and phosphate ester linkages are at
C and C ‘ respectively of the sugar molecule.
1 5

Types of RNA
1. Messanger RNA (m-RNA) It is produced in the nucleus and carries information
for the synthesis of proteins.

2. Transfer RNA (Soluble or Adoptive RNA) (s-RNA, t-RNA) It is found in

cytoplasm. Its function-is to collect amino acids from cytoplasm for protein
synthesis.

Functions of Nucleic Acids

1. Direct the synthesis of proteins.

2. Transfer the genetic information (hereditary characters).

Replication
It is a process in which a molecule of DNA can duplicate.

Template It means pattern. In the process of replication of DNA, the parent

strand serves as template.
Gene The portion of DNA carrying information about a specific protein is
Called gene.
Genetic code The relation between the amino acid and the nucleotide
triplet is called genetic code.
Codons The nucleotide bases in RNA function in groups of three (triplet) in
coding amino acids. These base triplets are called codons.
The world code is used with reference to DNA, codon with reference to m-
RNA and anticodon with reference to t-RNA.

Lipids
The constituents of animals and plants soluble in organic solvents (ether,
chloroform. carbon tetrachloride), but insoluble in water are called lipids.
(Greek lipose = fat)

Types of Lipids
(i) Simple lipids
(a) Fats and oils on hydrolysis give long chain fatty acids + glycerol.

(b) Waxes Long chain fatty acids + long chain alcohols.

Vegetable and animal oils and fats have similar chemical structure and are
triesters of glycerol, called glycerol.

Simple glycerides contain one type of fatty acids. Mixed glycerides contain
two or three types of fatty acids.

Common saturated fatty acids CH -(CH ) COOH.

3 2 n

When n = 4 caproic acid; n = 6 caprylic acid; n = 8 capric acid, n = 10 lauric

acid n = 12 myristic acid; n = 14 palmitic acid, n = 16 stearic acid.

Common unsaturated acids

C H COOH oleic acid; C H COOH linoleic acid.
17 33 17 33

Difference between oils and fats Oils are liquids at ordinary temprature
(below 20° and contain lower fatty acids or unsaturated fatty acids.
Fats are solids or semisolids above 20°C and contain higher saturated fatty
acids. Oils and fats act as “energy reservoirs” for the cells.
(ii) Phospholipids Phosphate + glycerol + fatty acids + a nitrogen
containing base.
Function of phospholipids are
1. As emulsifying agents since they carry hydrophilic polar groups and
hydrophobic non-polar groups.

2. They absorb fatty acids from the intestine and transport to blood cells.

(iii) Glycolipids They contain one or more simple sugars and are important
components of cell membranes and chlorplast membranes.

(iv) Steroids and Terpenes Menthol, camphor are common plant terpenes.
Carotenoids and pigments are also terpenes.

(a) Essential oils The volatile, sweet smelling liquids obtained from flowers,
leaves, stems, etc. Example of terpenes are esters of lower fatty acid, e.g.,
clove oil, rose oil, lemon oil.
(b) Drying oils The oils which are converted into tough, transparent mass
when exposed to air by oxidation polymerisation process are called drying
oils. e.g., Linseed oil, perilla, poppy seed oils.

Cotton seed oil and til oil are semidrying oils.

Acid Value
It is the number of milligrams of KOH required to neutralise the free acid
present in 1 g of oil or fat.

Saponification Value
It is the number of milligrams of KOH required to saponify 1g of oil or fat or
the number of milligrams of KOH required to neutralise the free acidresulting
from the hydrolysis of 1 g of an oil or fat.

Iodine Value
It is the number of grams of iodine absorbed by 100 g of oil or fat.

Relchert-Meissel Value (R/M Value)

It is the number of cc of N/10 KOH required to neutralise the distillate of 5 g
of hydrolysed fat.

Blood
An average person has about 6.8 L of blood which is about 6-10% of the
body weight. pH of blood is about 7.4.

Haemoglobin is globular protein. It is made up of four polypeptide chains

which are arranged in tetrahedral manner. Each chain is associated with a
non-protein part, called haem.
Haemoglobin
These axe the chemical substances which are produced by ductless glands in
the body. Hormones acts as chemical messengers.

Some examples of ductless ‘(endocrine) glands are thyroid, pitutary, adrenal,

pancreas, testes and ovaries.

Hormones are divided into three types:

1. steroids

2. proteins or polypeptides

3. amines.
Insulin is a protein hormone which is secreted by β-cells of the pancreas.
Insulin was the first polypeptide in which the amino acid sequence was
experimentally determined. Its deficiency leads to diabetes mellitus.

Vitamins
The organic compounds other than carbohydrates, proteins and facts which
are required by body to maintain normal health, growth and nutrition are
called vitamins.

The vitamins are complex organic molecules. They are represented by letters
such as A, B, C, D, E, K.

Vitamins are broadly classified into two types,

1. Water soluble vitamins and

2. oil soluble vitamins.

Vitamins A, D, E and K are oil soluble whereas vitamins B and C are water
soluble. Vitamin H is neither fat soluble nor water soluble.