XII

Question 14.1:
What are monosaccharides?
Answer
Monosaccharides are carbohydrates that cannot be hydrolysed further to give simpler units
of polyhydroxy aldehyde or ketone.
Monosaccharides are classified on the bases of number of carbon atoms and the functional
group present in them. Monosaccharides containing an aldehyde group are known as
aldoses and those containing a keto group are known as ketoses. Monosaccharides are
further classified as trioses, tetroses, pentoses, hexoses, and heptoses according to the
number of carbon atoms they contain. For example, a ketose containing 3 carbon atoms
is called ketotriose and an aldose containing 3 carbon atoms is called aldotriose.

Question 14.2:
What are reducing sugars?
Answer
Reducing sugars are carbohydrates that reduce Fehling’s solution and Tollen’s reagent.
All monosaccharides and disaccharides, excluding sucrose, are reducing sugars.

Question 14.3:
Write two main functions of carbohydrates in plants.
Answer
Two main functions of carbohydrates in plants are:
(i) Polysaccharides such as starch serve as storage molecules.
(ii) Cellulose, a polysaccharide, is used to build the cell wall.

Question 14.4:
Classify the following into monosaccharides and disaccharides.
Ribose, 2-deoxyribose, maltose, galactose, fructose and lactose
Answer
Monosaccharides:
Ribose, 2-deoxyribose, galactose, fructose Disaccharides:

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Maltose, lactose

Question 14.5:
What do you understand by the term glycosidic linkage?
Answer
Glycosidic linkage refers to the linkage formed between two monosaccharide units through
an oxygen atom by the loss of a water molecule.
For example, in a sucrose molecule, two monosaccharide units, -glucose and βfructose,
are joined together by a glycosidic linkage.

Question 14.6:
What is glycogen? How is it different from starch?
Answer
Glycogen is a carbohydrate (polysaccharide). In animals, carbohydrates are stored as
glycogen.
Starch is a carbohydrate consisting of two components − amylose (15 − 20%) and
amylopectin (80 − 85%).
However, glycogen consists of only one component whose structure is similar to
amylopectin. Also, glycogen is more branched than amylopectin.

Question 14.7:
What are the hydrolysis products of (i) sucrose and (ii) lactose?
Answer

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(i) On hydrolysis, sucrose gives one molecule of -D glucose and one molecule of β-
Dfructose.

(ii) The hydrolysis of lactose gives β-D-galactose and β-D-glucose.

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Question 14.8:
What is the basic structural difference between starch and cellulose?
Answer
Starch consists of two components − amylose and amylopectin. Amylose is a long linear
chain of −D−(+)−glucose units joined by C1−C4 glycosidic linkage ( -link).

Amylopectin is a branched-chain polymer of -D-glucose units, in which the chain is

formed by C1−C4 glycosidic linkage and the branching occurs by C1−C6 glycosidic linkage.

On the other hand, cellulose is a straight-chain polysaccharide of β-D-glucose units joined

by C1−C4 glycosidic linkage (β-link).

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Question 14.9:
What happens when D-glucose is treated with the following reagents?
(i) HI (ii) Bromine water (iii) HNO3
Answer
(i) When D-glucose is heated with HI for a long time, n-hexane is formed.

(ii) When D-glucose is treated with Br2 water, D- gluconic acid is produced.

(iii) On being treated with HNO3, D-glucose get oxidised to give saccharic acid.

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Question 14.10:
Enumerate the reactions of D-glucose which cannot be explained by its open chain
structure.
Answer
(1) Aldehydes give 2, 4-DNP test, Schiff’s test, and react with NaHSO 4 to form the
hydrogen sulphite addition product. However, glucose does not undergo these reactions.
(2) The pentaacetate of glucose does not react with hydroxylamine. This indicates that
a free −CHO group is absent from glucose.
(3) Glucose exists in two crystalline forms − andβ. The -form (m.p. = 419 K)
crystallises from a concentrated solution of glucose at 303 K and the β-form (m.p = 423
K) crystallises from a hot and saturated aqueous solution at 371 K. This behaviour cannot
be explained by the open chain structure of glucose.

Question 14.11:
What are essential and non-essential amino acids? Give two examples of each type.
Answer
Essential amino acids are required by the human body, but they cannot be synthesised in
the body. They must be taken through food. For example: valine and leucine Non-essential
amino acids are also required by the human body, but they can be synthesised in the body.
For example: glycine, and alanine

Question 14.12:
Define the following as related to proteins
(i) Peptide linkage (ii) Primary structure (iii) Denaturation.
Answer
(i) Peptide linkage:
The amide formed between −COOH group of one molecule of an amino acid and −NH 2
group of another molecule of the amino acid by the elimination of a water molecule is
called a peptide linkage.

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(ii) Primary structure:
The primary structure of protein refers to the specific sequence in which various amino
acids are present in it, i.e., the sequence of linkages between amino acids in a polypeptide
chain. The sequence in which amino acids are arranged is different in each protein. A
change in the sequence creates a different protein.
(iii) Denaturation:
In a biological system, a protein is found to have a unique 3-dimensional structure and a
unique biological activity. In such a situation, the protein is called native protein. However,
when the native protein is subjected to physical changes such as change in temperature
or chemical changes such as change in pH, its H-bonds are disturbed. This disturbance
unfolds the globules and uncoils the helix. As a result, the protein loses its biological
activity. This loss of biological activity by the protein is called denaturation. During
denaturation, the secondary and the tertiary structures of the protein get destroyed, but
the primary structure remains unaltered.
One of the examples of denaturation of proteins is the coagulation of egg white when an
egg is boiled.

Question 14.13:
What are the common types of secondary structure of proteins?
Answer
There are two common types of secondary structure of proteins:

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(i) -helix structure (ii) β-
pleated sheet structure -
Helix structure:

In this structure, the −NH group of an amino acid residue forms H-bond with the
group of the adjacent turn of the right-handed screw ( -helix).

β-pleated sheet structure:

This structure is called so because it looks like the pleated folds of drapery. In this
structure, all the peptide chains are stretched out to nearly the maximum extension and
then laid side by side. These peptide chains are held together by intermolecular hydrogen
bonds.

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Question 14.14:
What type of bonding helps in stabilising the -helix structure of proteins?
Answer
The H-bonds formed between the −NH group of each amino acid residue and

the group of the adjacent turns of the -helix help in stabilising the helix.

Question 14.15:
Differentiate between globular and fibrous proteins.
Answer

Fibrous protein Globular protein

It is a fibre-like structure formed by the The polypeptide chain in this

polypeptide chain. These proteins are held protein is folded around itself,
1. 1.
together by strong hydrogen and disulphide giving rise to a spherical
bonds. structure.

2. It is usually insoluble in water. 2. It is usually soluble in water.

Fibrous proteins are usually used for structural All enzymes are globular
3. purposes. For example, keratin is present in 3. proteins. Some hormones such
nails and hair; collagen in as insulin are also globular

tendons; and myosin in muscles. proteins.

Question 14.16:
How do you explain the amphoteric behaviour of amino acids?
Answer
In aqueous solution, the carboxyl group of an amino acid can lose a proton and the amino
group can accept a proton to give a dipolar ion known as zwitter ion.

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Therefore, in zwitter ionic form, the amino acid can act both as an acid and as a base.

Thus, amino acids show amphoteric behaviour.

Question 14.17:
What are enzymes?
Answer
Enzymes are proteins that catalyse biological reactions. They are very specific in nature
and catalyse only a particular reaction for a particular substrate. Enzymes are usually
named after the particular substrate or class of substrate and some times after the
particular reaction.
For example, the enzyme used to catalyse the hydrolysis of maltose into glucose is named
as maltase.

Again, the enzymes used to catalyse the oxidation of one substrate with the simultaneous
reduction of another substrate are named as oxidoreductase enzymes.

The name of an enzyme ends with ‘− ase’.

Question 14.18:
What is the effect of denaturation on the structure of proteins?
Answer

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As a result of denaturation, globules get unfolded and helixes get uncoiled. Secondary and
tertiary structures of protein are destroyed, but the primary structures remain unaltered.
It can be said that during denaturation, secondary and tertiary-structured proteins get
converted into primary-structured proteins. Also, as the secondary and tertiary structures
of a protein are destroyed, the enzyme loses its activity.

Question 14.19:
How are vitamins classified? Name the vitamin responsible for the coagulation of blood.
Answer
On the basis of their solubility in water or fat, vitamins are classified into two groups. (i)
Fat-soluble vitamins: Vitamins that are soluble in fat and oils, but not in water, belong
to this group. For example: Vitamins A, D, E, and K
(ii) Water-soluble vitamins: Vitamins that are soluble in water belong to this group.
For example: B group vitamins (B1, B2, B6, B12, etc.) and vitamin C However,
biotin or vitamin H is neither soluble in water nor in fat.
Vitamin K is responsible for the coagulation of blood.

Question 14.20:
Why are vitamin A and vitamin C essential to us? Give their important sources.
Answer
The deficiency of vitamin A leads to xerophthalmia (hardening of the cornea of the eye)
and night blindness. The deficiency of vitamin C leads to scurvy (bleeding gums). The
sources of vitamin A are fish liver oil, carrots, butter, and milk. The sources of vitamin C
are citrus fruits, amla, and green leafy vegetables.

Question 14.21:
What are nucleic acids? Mention their two important functions.
Answer
Nucleic acids are biomolecules found in the nuclei of all living cells, as one of the
constituents of chromosomes. There are mainly two types of nucleic acids −

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deoxyribonucleic acid (DNA) and ribonucleic acid (RNA). Nucleic acids are also known as
polynucleotides as they are long-chain polymers of nucleotides.
Two main functions of nucleic acids are:
(i) DNA is responsible for the transmission of inherent characters from one generation
to the next. This process of transmission is called heredity.
(ii) Nucleic acids (both DNA and RNA) are responsible for protein synthesis in a cell.
Even though the proteins are actually synthesised by the various RNA molecules in a cell,
the message for the synthesis of a particular protein is present in DNA.

Question 14.22:
What is the difference between a nucleoside and a nucleotide?
Answer
A nucleoside is formed by the attachment of a base to position of sugar.
Nucleoside = Sugar + Base

On the other hand, all the three basic components of nucleic acids (i.e., pentose sugar,
phosphoric acid, and base) are present in a nucleotide. Nucleotide = Sugar + Base +
Phosphoric acid

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Question 14.23:
The two strands in DNA are not identical but are complementary. Explain.
Answer
In the helical structure of DNA, the two strands are held together by hydrogen bonds
between specific pairs of bases. Cytosine forms hydrogen bond with guanine, while adenine
forms hydrogen bond with thymine. As a result, the two strands are complementary to
each other.

Question 14.24:
Write the important structural and functional differences between DNA and RNA.
Answer
The structural differences between DNA and RNA are as follows:

DNA RNA

The sugar moiety in DNA molecules is The sugar moiety in RNA molecules
1. 1.
β-D-2 deoxyribose. is β-D-ribose.

DNA contains uracil (U). It does not RNA contains thymine (T). It does
2. 2.
contain thymine (T). not contain uracil (U).

The helical structure of DNA is The helical structure of RNA is

3. 3.
double-stranded. single-stranded.

The functional differences between DNA and RNA are as follows:

DNA RNA

DNA is the chemical basis

1. 1. RNA is not responsible for heredity.
of heredity.

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 Proteins are synthesised DNA molecules do not synthesise proteins,
2. by RNA molecules in the 2. but transfer coded message for the synthesis
cells. of proteins in the cells.

Question 14.25:
What are the different types of RNA found in the cell?
Answer
(i) Messenger RNA (m-RNA)
(ii) Ribosomal RNA (r-RNA)
(iii) Transfer RNA (t-RNA)

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