Biomolecules

Biomolecules
Macromolecules which are found in living organisms (animals and plants) and essential for our
vital activities are known as Biomolecules. The most important biomolecules are
(1) Carbohydrate
(2) Protein
(3) Nucleic acid
(4) Vitamins

Biomolecules

Carbohydrates Proteins Enzymes Vitamins Nucleic Acid

Carbohydrates:The optically active polyhydroxy aldehydes or ketones or the compounds which
produce such units on hydrolysis are called carbohydrates. Sweet carbohydrates are called sugars.

• Most common sugar used in homes – sucrose.

• Sugar present in milk – Lactose.
• arbohydrates are also called saccharides.

Classification of carbohydrates:-

(i) Monosaccharides:- A carbohydrate that can not be hydrolysed further to give simpler unit of
polyhydroxy aldehyde or ketone is called a monosaccharide.
• About 20 monosaccharides are known.
• Common examples – glucose, fructose, ribose.

(ii) Oligosaccharides:- Carbohydrates that yield two to ten monosaccharides units on hydrolysis
are called oligosaccharides.
• Fructose on hydrolysis gives glucose and fructose.
• Maltose gives two molecules of glucose only. (on hydrolysis)
• Lactose produces glucose and galactose on hydrolysis.

(iii) Polysaccharides:- Carbohydrates which yield a large no. of monosaccharide units on hydrolysis
are called polysaccharides.
• Common examples: starch, cellulose, glycogen, gums etc.
• Polysaccharides are not sweet in taste, hence they are called non-sugars.

1|Page
 Biomolecules
Carbohydrates may be classified as reducing or non reducing sugars:

Reducing sugars:- Carbohydrates that reduces Fehling’s solution and Tollen’s reagent are called
reducing sugars. All monosaccharides are reducing sugars, maltose, lactose.
Non reducing sugars:- Carbohydrates that do not reduce Fehling’s solution and Tollen’s reagent are
called non reducing sugars. eg. Sucrose.
Glucose: Glucose
is aldohexose and is known as Dextrose. It is dextrorotatory compound.

Preparation of glucose:-

1. From sucrose (cane sugar) :

Sucrose on hydrolysis give glucose and fructose.
H+
C12H22O11 + H2O C6H12O6 + C6H12O6
Sucrose Glucose fructose
2. From starch:
Hydrolysis of starch produces glucose.
H+
(C6H10O5)n + nH2O nC6H12O6
Starch Glucose

Evidences for glucose structure: -

1. On prolonged heating with HI, it forms n-hexane. It indicates that all six carbons are linked in a
straight chain.

2. Glucose reacts with hydroxylamine to form an oxime and adds a molecule of HCN to give
cyanohydrin. These reactions confirm the presence of a carbonyl group in glucose.

2|Page
 Biomolecules

3. Glucose gets oxidized to gluconic acid on reaction with mild oxidizing agent like bromine water.
This indicates that carbonyl group is aldehyde.

4. Acetylation of glucose with acetic anhydride gives glucose pentaacetate which confirms the
presence of five –OH groups. Since it exists as a stable compound, five –OH groups should be
attached to different carbon atoms.

5. On oxidation with nitric acid, glucose as well as gluconic acid both yield a dicarboxylic acid,
saccharic acid. This indicates the presence of a primary alcoholic (–OH) group in glucose.

6. Formation of osazone:

3|Page
 Biomolecules

NOTE: Osazone formation and mechanism is not a part of CBSE BOARD .

On the basis of above evidences, exact structure of glucose is:-

Objection to linear structure:

i. In spite of the presence of an aldehydic group, glucose does not restore the pink colour
of Schiff’s reagent, does not give 2, 4-DNP test and does not form addition products
with sodium hydrogen sulphite and ammonia.
ii. Glucose pentaacetate does not react with hydroxyl amine. The above facts indicating
the absence of free –CHO group in glucose.

4|Page
 Biomolecules
Cyclic Structure of Glucose:

Anomeric carbon: Carbon of carbonyl group involves in internal hemiacetal formation is

known as anomeric carbon.
Anomers: Such distereomers which are mirror image with respect to anomeric carbon is
known as anomers.
Notation of α, β - If –OH at RHS of anomeric carbon ,it is α
If –OH at LHS of anomeric carbon , it is β

Haworth structure:-
The six membered cyclic structure of glucose is called Pyranose structure because it is analogus to
Pyran .

( Structure of Pyran )

5|Page
 Biomolecules
FRUCTOSE:-
➢ It is ketohexose.
➢ It is laevorotatory compound.
➢ It is written as D-(-)-fructose.
Open chain structure:

Cyclic Structure:

Haworth structure:-
Five membered ring thus formed is called furanose because it is analogus to furan .

(Structure of furan)
The cyclic structures of two anomers of fructose are represented by Haworth structures as
given:

6|Page
 Biomolecules

Disaccharides:
Glycosidic linkage: A linkage between two monosaccharide units through oxygen atom is called
glycosidic linkage.

Common disaccharides: sucrose , maltose, lactose.

(i) Sucrose: sucrose on hydrolysis give equimolor mixture of D-(+)-glucose and D-(-)-fructose.
C12H22O11 + H2O H+ C6H12O6 + C6H12O6
D-(+) glucose D (-) – fructose

• Linkage between C1 of α – D(+) glucose and C2 of β – D (-) fructose.

• Sucrose is non reducing sugar
• Sucrose is dextrorotatory.
• Sucrose is non-reducing sugar.
• Sucrose is soluble in water and sweet in taste
• Sucrose do not form osazone
• Sucrose do not show muta rotation
• Sucrose is a commercial or kitchen sugar.
Invert Sugar: Hydrolysis of sucrose brings about a change in sign of rotation from dextro to
leavo and this change in rotation is known as inversion of cane sugar and forming mixture of
glucose and fructose is known as invert sugar.
Haworth Projection formulae of sucrose:-

7|Page
 Biomolecules

Maltose:- It is formed by C1-C4 linkage of two α – D (+)- glucose units .

• It is reducingsugar.
• Maltose gives negative test with Schiff reagent.
• Maltose shows mutarotation.
• Maltose gives positive Tollens’ test.
• Maltose does not form adduct with NaHSO3 and NH3.
• Maltose gives positive Fehling's test.

Lactose:- It is also known as milk sugar. It is composed of β – D galactose and β – D – glucose. The
linkage is between C1 of galactose and C4 of glucose.
• It is also a reducing sugar.
• Lactose gives negative test with Schiff reagent.
• Lactose shows mutarotation.
• Lactose gives positive Tollens’ test.
• Lactose does not form adduct with NaHSO3 and NH3.
• Lactose gives positive Fehling's test.

8|Page
 Biomolecules

Polysaccharides:-
Polysaccharides contain a large number of monosaccharide units joined together by glycosidic
linkages.Their general formula is (C6H10O5)n. These are non sugars as these are not sweet in
taste. eg- starch, cellulose, glycogen.
Starch:- It is a polymer of α – glucose and consists of two components .
(i) Amylose (ii) Amylopectin
(i) Amylose: Amylose is water soluble component which constitutes about 15 – 20% of starch.
Chemically amylose is a long unbranched chain with 200 – 1000 α – D – (+) –glucose units held by C1 –
C4 glycosidic linkage.

(ii) Amylopectin: It is water insoluble component which constitutes about 80 – 85 % of starch. It is a

branched chain polymer of α – D – glucose units in which chain is formed by C1 – C4 glycosidic linkage
whereas branching occurs by C1 – C6 glycosidic linkage.

9|Page
 Biomolecules

Difference between amylase and amylopectin :

Amylose Amylopectin
i. It is unbranched helical structure. i. Many branches are present.
ii. These are combined with a 1, 4-linkage ii. In straight chain, it is attached by a 1, 4 glycosidic
bond while in branched chain it is linked by a-1, 6
linkage
iii. It is water soluble. iii. It is water insoluble.
iv. They give blue colour with I2. iv. They give red colour with I2

v. It is 15–20% in starch. v. It is 80–85% in starch

Cellulose:-Cellulose occurs in plants and it is most abundant substance in plant kingdom. Cell wall is
made up of cellulose.
Cellulose is a straight chain polysaccharide composed only of β – D- glucose units by C1 – C4 glycosidic
linkage.

Glycogen:-The carbohydrates are stored in animal body as glycogen. It is also known as animal starch.
It’s structure is similar to amylopectin. It is highly branched. It is present in liver, muscles and brain. It
is also found in yeast and fungi.

10 | P a g e
 Biomolecules
Test of Carbohydrates
(a) Carbohydrate with Tollens’ reagent (ammoniacal silver nitrate) gives silver mirror test.
(b) Carbohydrate with Fehling’s solution (alkaline CuSO4) gives a red ppt.
Molisch’s test: Carbohydrates when treated with Molisch’s reagent (1% alcoholic solution of a-
naphthol) in presence of conc. H2SO4 from violet ring.
(c) When heated in dry test tube, it melts, turns brown and finally black giving a smell of burning
sugar.

Importance of Carbohydrates:
1. Carbohydrates are major portion of our food.
2. Glucose is instant source of energy and used as medicines.
3. Carbohydrates are used as storage molecules (as starch in plants and glycogen in animals).
4. Cell wall is made up of cellulose.
5. Carbohydrates provide raw material for textiles, paper etc.
6. D – ribose and β – D - 2 – deoxyribose are present in nucleic acid.

Proteins
• Proteins are most abundant biomolecules of the living system.
• Sources are milk, cheese, pulses, fish, meat etc.
• They are required for growth and maintenance of body.
• All proteins are polymers of α – amino acids.
• Proteins are polymers of amino acids.
• Protein is 3/4 part of dry weight of tissues.
• Protein forms structure of body.
• C, H, O, N are necessarily present in proteins.
• 70 types of amino acids are known. But in proteins about 20 types of amino acids are
used. Other amino acids are called non-proteinous amino acid; e.g., citruline, ornithine
Amino Acids:-Amino acids contain amino (-NH2) and carboxyl ( - COOH) functional groups.
Depending upon the relative position of amino group with respect to carboxyl groupthe amino
acids can be classified as α, β, γ, δ and so on. Only α – amino acids are obtained on hydrolysis of
proteins.
α
R – CH – COOH

NH2
α – amino acid

11 | P a g e
 Biomolecules

Note: i. Most naturally occurring amino acids have L-configuration. L-Aminoacids are
represented by writing the –NH2 group on left hand side.
ii. Except glycine, all α – amino acids are optically active.

Amino acids are classified as acidic, basic or neutral depending upon the relative number of
amino and carboxyl groups in their molecule.
• Equal number of amino and carboxyl groups makes it neutral;
• more number of amino than carboxyl groups makes it basic .
• More carboxyl groups as compared to amino groups makes it acidic.
Classification of amino acids:
Non essential amino acids:- The amino acids which can be synthesized in the body are known
as non essential amino acids.
Examples: (1) Alanine (2) Aspargine (3) Aspartic acid (4) Cysteine (5) Glutamic acid (6) Glutamine
(7) Glycine (8) Proline (9) Serine (10) Tyrosine

Essential amino acids:- The amino acids which cannot be synthesized in the body and must be
obtained through diet are known as essential amino acids.
Examples: (1) Leucine (2) Isoleucine (3) Lysine (4) Methionine (5) Phyenylalanine (6) Threonine
(7) Tryptophan (8) Valine
Semi essential amino acids: They are 50% synthesised in body +50% taken by food.
Examples: (1) Arginine (2) Histidine

Zwitter ion:-
Any ion which is dipolar and contain both anionic part and cationic part. In aqueous solution,
the carboxylic group can lose a protein and amino group can accept a proton and produce
zwitter ion.

In zwitter ionic form, amino acids show amphoteric behaviour.

Isoelectric Point (pI): At some characteristic pH, the amino acid will not migrate towards any
electrode. This particular pH is called the isoelectric point, pI, of the amino acid. At this pH value,
the concentration of zwitterions is at its maximum and the concentrations of the anionic and
cationic species are equal. At isoelectric point an amino acid has the least solubility in water and
12 | P a g e
 Biomolecules
this property is exploited in the separation of different amino acids obtained from the hydrolysis
of a protein.
Proteins:- Proteins are the polymers of α – amino acids and they are connected to each other
by peptide bond or peptide linkage.
Peptide linkage:- An amide linkage formed between –COOH group and –NH2 group is called
peptide linkage.

• According to number of amino acid, peptide bond must be two, three, resulting into
dipeptide, tripeptide, etc., respectively.
• Number of peptide bond = (number of amino acid) –1
Difference between Fibrous Proteins and Globular proteins:-

Fibrous Proteins Globular Proteins

1. When the polypeptide chains run 1. When the chains of polypeptides coil
parallel and are held together by around to give a spherical shape,
hydrogen and disulphide bonds, then proteins thus obtained are called
fibre – like structure is formed. This is globular proteins.
called Fibrous proteins.
2. These proteins are insoluble in water. 2. These are soluble in water.
3. Common examples - Keratin (present
in hair, nails, wool, silk) and myosin 3. Common examples - are Insulin and
(present in muscles), casein in bones. albumins, haemoglobin

Structure of proteins:-
1. Primary structure:-Each polypeptide in a protein has amino acids linked with each other
in a specific sequence. This sequence is called primary structure of protein. Primary
structure refers to the number, nature and sequence of the amino acids in protein
molecule.

13 | P a g e
 Biomolecules
2. Secondary Structure:- The secondary structure of protein refers to the shape in which a
long polypeptide chain can exist. They are found to exist in two different types of
structure.
(a) α – helix structure:-In this structure, a polypeptide chain forms all possible H – bonds by
twisting into a right handed screw. H – bond exist between –NH group of each amino
acids and C =0 of the adjacent turn of the helix as shown in fig.

(b) β – Pleated structure:- In β – structure, all peptide chains are stretched out to nearly
maximum extension and the laid side by side which are held together by H – bonds. The
structure resembles the pleated folds of drapery and therefore known as β – pleated sheet.
3. Tertiary structure of proteins:- Further folding of secondary structure gives tertiary
structure. It gives two major molecular shapes viz. fibrous and globular. The main forces
which stabilize the 2° and 3° structure of proteins are hydrogen bonds, disulphide
linkages, vander Walls interaction and electrostatic force of attraction. In this structure of
protein atoms are highly coiled and form a spherical form. E.g. Albumin

4. Quaternary structure of proteins:

14 | P a g e
 Biomolecules
The quaternary structure of a protein is the association of several protein chains or
subunits into a closely packed arrangement. Each of the subunits has its own primary,
secondary and tertiary structure. The subunits are held together by hydrogen bonds and
van der Waal forces.

Denaturation of proteins:-
When a protein in its native form, is subjected to physical change like change in temperature
or chemical change like change in pH, the hydrogen bonds are disturbed. Due to this, globules
unfold and helix get uncoiled and protein loses its biological activity. This is called
denaturation of protein. During denaturation 2° and 3° structures are destroyed but 1°
structure remains intact.
Example:-
i. The coagulation of egg white on boiling.
ii. Curdling of milk.
Test of protein :
(a) Xanthoprotic test: With conc. HNO3 on heating give yellow precipitate, which on more
heating gives solution. On adding NH4OH red colour appears.
(b) Biuret test: (NH4OH) + dil. CuSO4 protein give blue violet colour.
(c) Millon’s test: Proteins on adding Millon’s reagent (a solution of mercuric [Hg(NO 3)2] and
mercurous nitrates (HgNO3) in nitric acid containing a little nitrous acid) followed by heating
the solution give red precipitate or colour.
(d) Ninhydrin test : Proteins, peptides and a-amino acids give a characteristic blue colour on
treatment with ninhydrin.
Biological importance of protein:
(a) Component of plasma membrane .
(b) All enzymes are protein .
(c) Many hormones are protein .
(d) Antigen and antibody are protein .

15 | P a g e
 Biomolecules
(e) Action and myosin protein are important in muscle contraction .
(f) Proteins are important in growth, regeneration and repairing .
(g) Calorific value 4.0 kcal .

Enzymes
Enzymes:- The biocatalysts are called enzymes. Almost all the enzymes are globular proteins.
Maltose
Example Maltose Glucose
Lactase
Lactose Lactic acid

Oxioreductase enzymes:-
The enzymes which catalyse the oxidation of one substrate with simultaneous reduction of
another substrate are named as oxioreductive enzymes.
Key- Lock mechanism :-
• Enzymes are highly specific in their action.
• There specificity is due to the presence of active sites. The shape of active site of any
given enzyme is like acavity such that only a specific substrate can fit into it. In the same
way a key fit into a lock.
• This specific binding leads to the formation of an enzyme substrate – Complex which
accounts for high specificity of enzyme catalysed reactions.

Vitmains:-
Certain organic compounds that are required in small amounts in our diet but their deficiency causes
specific diseases. These compounds are called vitamins.
Classification of Vitamins:-
Fat soluble vitamins:- Vitamins which are soluble in fat and oils but insoluble in water are kept in this
group. These are vitamins A, D, E and K. They are stored in Liver and adipose tissues.

Water soluble vitamins:- Vitamin B (B1, B2, B6, B12) and C are soluble in water. Water
soluble vitamins are stored in the cells in much lesser amounts. Water soluble vitamins must

16 | P a g e
 Biomolecules
be supplied regularly in diet because they are readily excreted in urine and cannot be stored
in our body.

VARIOUS VITAMINS AND DISEASES :-

Name of Vitamin Chemical name Diseases
Vitamin A Retinol Xerophthalmia, night
blindness
Vitamin B1 Thiamine Beri – Beri

Vitamin B2 Riboflavin Cheilosis,Digestive

disorder, burning sensation
of skin
Vitamin B6 Pyridoxine Convulsions

Vitamin B12 Cyanocobalmin Pernicious anaemia

Vitamin C Ascorbic acid Scurvy (Bleeding gums)

Vitamin D Calciferol Rickets and osteomalacia

Vitamin E Tocoferol Increased fragility of RBCs

and muscular weakness.
Vitamin K Phylloquinone, Increased blood clotting
menaquinones time.

Nucleic Acid
• Transmission of inherent characters is called heredity.
• Chromosomes are responsible for heredity.
• Chromosomes are made up of proteins and nucleic acids.
• There are two types of nucleic acids:-
(i) DNA (Deoxyribonucleic acid)
(ii) RNA (Ribonucleic acid)
• Nucleic acids are long chain polymers of nucleotides, so they are also called polynucleotides.

Chemical composition of Nucleic acid:-

DNA is made up of :- (i) a pentose sugar (β – D -2-deoxyribose)
(ii) Phosphoric acid
(iii) Nitrogenous base like Adenine, Guanine, Cytosine, Thymine

RNA is made up of :- (i) a pentose sugar (β – D ribose)

(ii) Phosphoric aci

17 | P a g e
 Biomolecules
(iii) Nitrogenous bases like Adenine, Guanine, Cytosine, Uracil

Structure of pentose sugar in RNA & DNA :

Structure of Nucleic acids:-

Nucleoside: The molecules in which one of the nitrogen bases (purine and pyrimidine) is
bonded with a sugar molecule is called a nucleoside. The general representation of nucleoside
is as follows,
Base + Sugar = Nucleoside
Nucleotide: When the phosphate group is attached to the nucleoside, the compound formed
is called as nucleotide.
Base + sugar + Phosphate = Nucleotide

• Nucleotides are joined together by phosphodiester linkage.

• A simplified version of nucleic acid is as shown below:-
Base Base Base
– Sugar – phosphate – (sugar – phosphate)n sugar –
Types of RNA molecules:
(i) m – RNA (messenger)

18 | P a g e
 Biomolecules
(ii) r – RNA (ribosomal)
(iii) t – RNA (transfer)

Biological function of Nucleic Acids:-

(i) DNA is the chemical basis of heredity.
(ii) DNA is reposnsible for maintaining the identity of different species of organisms.
(iii) DNA helps in synthesis of protein in the cell.

19 | P a g e