Revision Notes On CBSE Class 12 Chemistry Chapter 14 - Biomolecules Free PDF

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Revision Notes

Class 12 Chemistry
Chapter 14 Biomolecules

1. Introduction

Biomolecules are complex organic compounds that govern the common activities
of living organisms. Carbohydrates, proteins, nucleic acids, lipids, and other
complex biomolecules make up living systems. Furthermore, simple molecules
such as vitamins and mineral salts play an important role in the functions of
organisms.

2. CARBOHYDRATES

Plants are the primary producers of carbohydrates, which comprise a large group of
naturally occurring organic compounds. Cane sugar, glucose, starch, and other
common examples The majority of them have the general formula C x H2 y O y and
were thought to be carbon hydrates, hence the name carbohydrate. The molecular
formula of glucose  C6H12O6  , for example, fits into this general formula,
C6  H2O  6. However, not all of the compounds that fit into this formula are
carbohydrates. Rhamnose, C6H12O5 , is a carbohydrate, but it does not fall under
this definition. Carbohydrates can be defined chemically as optically active
polyhydroxy aldehydes or ketones, or compounds that produce such units upon
hydrolysis. Some carbohydrates with a sweet taste are also known as sugars.
Sucrose is the most common sugar found in our homes, whereas lactose is the
sugar found in milk.

2.1 Classification of Carbohydrates

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Carbohydrates are classified based on how they react to hydrolysis. They have
been broadly classified into the three groups listed below:

2.1.1 Monosaccharides

A monosaccharide is a carbohydrate that cannot be hydrolyzed further to produce


simpler units of polyhydroxy aldehyde or ketone. Examples include glucose,
fructose, ribose, and others.

Monosaccharides are further classified based on the number of carbon atoms and
the functional group they contain. When a monosaccharide contains an aldehyde
group, it is referred to as an aldose, and when it contains a keto group, it is referred
to as a ketose. As shown by the examples, the number of carbon atoms constituting
the monosaccharide is also introduced in the name.

Different types of monosaccharides

Carbon atoms General Term Aldehyde Ketone

3 Triose Aldotriose Ketotriose

4 Tetrose Aldotetrose Ketotetrose

5 Pentose Aldopentose Ketopentose

6 Hexose Aldohexose Ketohexose

7 Heptose Aldoheptose Ketoheptose

2.1.2 Oligosaccharides

Oligosaccharides are carbohydrates that, when hydrolyzed, yield two to ten


monosaccharide units. They are further classified as disaccharides, trisaccharides,
tetrasaccharides, and so on, based on the number of monosaccharides produced
during hydrolysis. Disaccharides are the most common of these. The two
monosaccharide units formed by hydrolysis of a disaccharide may be identical or

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dissimilar. Sucrose, for example, yields one molecule of glucose and one molecule
of fructose when hydrolyzed, whereas maltose yields only two molecules of
glucose.

2.1.3 Polysaccharides

Polysaccharides are carbohydrates that when hydrolyzed yield a large number of


monosaccharide units. Starch, cellulose, glycogen, gums, and other common
examples Polysaccharides do not have a sweet taste, so they are also known as
non-sugars.

2.1.4 Reducing and Non-Reducing Sugars

Carbohydrates are also classified as reducing or non-reducing sugars. Reducing


sugars are all carbohydrates that reduce Fehling's solution and Tollens' reagent.
Sugars are reduced by all monosaccharides, whether aldose or ketose.

Nonreducing sugars, such as sucrose, are formed when the reducing groups of
monosaccharides, such as aldehydic or ketonic groups, are bonded in
disaccharides. Reducing sugars, on the other hand, are sugars that have these
functional groups free, such as maltose and lactose.

3. GLUCOSE (ALDOHEXOSE)

3.1 Preparation of Glucose

(A) From Sucrose (Cane Sugar):

When sucrose is boiled in alcoholic solution with dilute HCl or H2SO4 , glucose and
fructose are obtained in equal amounts.

H
C12H22O11  H 2O 
 C6H12O6  C6H12O6
Sucrose Glucose Fructose

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(B) From Starch

Glucose is commercially obtained by hydrolyzing starch with dilute H2SO4 at 393


K under pressure.

H
C6 H10O5  nH2O  nC6 H12O6
393 K,2-3 atm
Starch or cellulose Glucose

3.2 Reactions

(A) Oxidation

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(B) Reduction

Note: Reduction with HI yields n-hexane, demonstrating that all six carbons of
glucose are arranged in a straight chain.

(C) Oxime Formation

(D) Cyanohydrin Formation

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Note: Since carbonyl C has become chiral, two diastereomers are formed.

(E) Acetylation

(F) Reaction with phenylhydrazine (formation of osazone)

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Note: To produce osazone, one mole consumes three moles of PhNHNH2. Two
moles produce hydrazone, and one is used to convert a CHOH group to a carbonyl
group.

3.3 Configuration in Monosaccharides

D(+)-glucose is the correct name for glucose. The letter ‘D' before the name of
glucose represents the configuration, whereas the letter ‘(+)' represents the
molecule's dextrorotatory nature. It should be noted that the letters 'D' and 'L' have
no bearing on the compound's optical activity. The following is a definition of D–
and L– notations. The letters 'D' or 'L' before the name of any compound indicate
the stereoisomer's relative configuration. This refers to their affinity for a specific
isomer of glyceraldehyde. Glyceraldehyde has one asymmetric carbon atom and
comes in two enantiomeric forms, as shown.

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All compounds that can be chemically correlated to the (+) isomer of
glyceraldehyde have D-configuration, whereas those that can be correlated to the
(–) isomer of glyceraldehyde have L-configuration. The lowest asymmetric carbon
atom (as shown below) is compared when assigning the configuration of
monosaccharides. As with (+) glucose, –OH on the lowest asymmetric carbon is on
the right side, similar to (+) glyceraldehyde, so it is assigned D-configuration. The
structure is written in such a way that the most oxidised carbon is at the top for this
comparison.

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3.4 Cyclic Structure of Glucose

Glucose has been discovered to exist in two different crystalline forms, which are
known as  and  . The  -form of glucose (m.p. 419 K) is obtained by
crystallisation from a concentrated glucose solution at 303 K, whereas the  . -form
(m.p. 423) is obtained by crystallisation from a hot and saturated aqueous solution
at 371 K. In aqueous solution, both  -D-glucose and  -D-glucose undergo
mutarotation. Although the crystalline forms of  - and  -D (+)-glucose are quite
stable in aqueous solution, each form gradually transforms into an equilibrium
mixture of the two.

This is demonstrated by the fact that the specific rotation of a freshly prepared
aqueous solution of  -D(+)-glucose decreases with time from +111° to +52.5°,
whereas that of  -D(+)-glucose increases from +19.2° to 52.5°. Thus, mutarotation
refers to the spontaneous change in specific rotation of an optically active
compound with time to an equilibrium value. It was discovered that glucose forms
a six-membered ring, with –OH at C-5 playing a role in ring formation. This
explains the lack of a –CHO group as well as the presence of glucose in two forms,
as shown below. These two cyclic forms coexist with an open chain structure.

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The only difference between the two cyclic hemiacetal forms of glucose is the
configuration of the hydroxyl group at C1, which is referred to as anomeric carbon
(the aldehyde carbon before cyclisation). Such isomers, namely -form and -form,
are referred to as anomers. In analogy with pyran, the six-membered cyclic
structure of glucose is known as the pyranose structure (– or –). Pyran is a cyclic
organic compound with a ring containing one oxygen atom and five carbon atoms.
The Haworth structure more accurately represents the cyclic structure of glucose.

3.4.1 How to draw a Haworth Projection

A ring of 6 atoms (5 ‘C' and 1 ‘O') is drawn, with the ‘O' atom in the upper right
hand corner, as shown below.

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Number one is assigned to the carbon atom on the right side of oxygen. Then, in a
clockwise fashion, other carbon atoms are assigned numbers 2, 3,........... . In
Fischer projection, groups attached to a carbon on the right side are placed below
the ring, while groups attached to the carbon on the left side are placed above the
ring. However, by convention, the CH2OH group of carbon 5 is placed above the
plane of the ring.

4. FRUCTOSE (KETOHEXOSE)

Fructose has the molecular formula C6H12O6 , and based on its reactions, it was
discovered to have a ketonic functional group at carbon number 2 and six carbons
in a straight chain, just like glucose. It is a laevorotatory compound from the D-
series. D-(–)-fructose is the correct spelling. Its open chain structure is depicted
below.

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It also exists in two cyclic forms, which are obtained by adding –OH to the
carbonyl group at C5. The resulting ring is a five-membered ring known as
furanose, after the compound furan. Furan is a five-membered cyclic compound
that contains one oxygen atom and four carbon atoms.

Haworth structures are used to represent the cyclic structures of two anomers of
fructose.

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5. COMPARISON OF GLUCOSE AND FRUCTOSE

Property Glucose
Molecular formula C6 H12O6

Nature Polyhydroxy aldehyde


Melting point 146oC
Optical nature Dextro rotatory
Fehling’s solution Silver mirror
Tollen’s reagent Red ppt
Molisch test Violet colour
Phenyl hydrazine Forms osazone
Oxidation by concentrated HNO3 Saccharic acid

6. DISACCHARIDES

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An oxide linkage formed by the loss of a water molecule connects the two
monosaccharides. The linkage of two monosaccharide units via an oxygen atom is
known as glycosidic linkage.

6.1 Sucrose

Sucrose is a common disaccharide that, when hydrolyzed, yields an equimolar


mixture of D-(+)-glucose and D-(–)-fructose.

C12 H 22O11  H 2O 
 C6 H12O6  C6 H12O6
Sucrose D-  -Glucose D-  -Fructose
 D 66.5  D 52.5  D 92.4

A glycosidic linkage between C1 of  -glucose and C2 of  -fructose holds these


two monosaccharides together. Sucrose is a non-reducing sugar because the
reducing groups of glucose and fructose are involved in the formation of glycosidic
bonds.

Sucrose is a dextrorotaty compound that when hydrolyzed yields an equimolar


solution of glucose and fructose.

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Because the laevo rotation of fructose is greater than the dextro rotation of glucose,
this solution is laevorotaty.

Thus, hydrolysis of sucrose causes a change in the sign of rotation, from dextro (+)
to laevo (–), and the product is known as invert sugar, and the phenomenon is
known as sugar inversion.

6.2 Maltose

Maltose, another disaccharide, is made up of two -Dglucose units, with C1 of one


glucose (I) linked to C4 of another glucose unit (II). Because the free aldehyde
group can be produced at C1 of second glucose in solution and has reducing
properties, it is classified as a reducing sugar.

6.3 Lactose

It is more commonly known as milk sugar since this disaccharide is found in milk.
It is composed of  -D-galactose and  -D-glucose. Fischer projections of -D-
Glucose and -D-Galactose are drawn below:

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Except for C-4, the configurations of all the carbon atoms in  -D-Glucose and  -
D-Galactose are the same. Such stereoisomers that differ in configuration at only
one carbon other than anomeric carbon are referred to as epimers, and the C atom
in question is referred to as an epimeric carbon atom. As a result,  -DGlucose and
 -D-Galactose are epimers, and C-4 is an epimeric carbon atom. The linkage in
lactose is between C1 of galactose and C4 of glucose. As a result, it is also a
reducing sugar.

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7. POLYSACCHARIDES

Polysaccharides are composed of many monosaccharide units linked together by


glycosidic linkages. They primarily serve as food storage or structural materials.

7.1 Starch

Plants' primary storage polysaccharide is starch. It is the most important source of


nutrition for humans. Cereals, roots, tubers, and some vegetables have a high
starch content. It is a -glucose polymer composed of two components: Amylose
and Amylopectin. Amylose is a water-soluble component that accounts for about
15-20% of starch. Amylose is a long unbranched chain containing 200-1000  -D-
(+)-glucose units held together by a C1-C4 glycosidic linkage. Amylopectin is
insoluble in water and accounts for approximately 80-85 percent of starch. It is a
branched chain polymer of  -D-glucose units with a chain formed by C1-C4
glycosidic linkage and branching caused by C1-C6 glycosidic linkage.

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7.2 Cellulose

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Cellulose is found only in plants and is the most abundant organic substance in the
plant kingdom. It is a major component of the cell wall of plant cells. Cellulose is a
straight-chain polysaccharide made up entirely of  -D glucose units linked
together by a glycosidic linkage between C1 of one glucose unit and C4 of the next
glucose unit.

7.3 Glycogen

Carbohydrates are stored as glycogen in the animal body. It is also known as


animal starch due to its structure, which is similar to amylopectin but more highly
branched. It can be found in the liver, muscles, and brain. When the body requires
glucose, enzymes convert glycogen to glucose. Glycogen is found in yeast and
fungi as well.

7.4 Summary

Note:

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1. Reducing sugars are all carbohydrates that contain the CHO group, the  -
Hydroxy ketonic group, or the hemiacetal group.

2. Mutarotation is a phenomenon that occurs in all reducing sugars.

8. PROTEINS

Protein is derived from the Greek word "proteios," which means "primary" or "of
primary importance." Proteins are all polymers of  -amino acids.

8.1 Amino Acids

Amino acids have both amino (–NH2) and carboxyl (–COOH) functional groups.
The amino acids are classified as  ,  ,  ,  and so on based on the relative position
of the amino group with respect to the carboxyl group. When proteins are
hydrolyzed, only  -amino acids are produced. They may also contain other
functional groups.

All  -amino acids have innocuous names that usually reflect the compound's or its
source's property. Glycine is named after its sweet taste (glykos means sweet in
Greek), and tyrosine was first obtained from cheese (tyros means cheese in Greek).

8.2 Natural Amino Acids

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8.3 Classification of Amino Acids

The relative number of amino and carboxyl groups in an amino acid molecule
determines whether it is acidic, basic, or neutral.

Non-essential amino acids are amino acids that can be synthesized in the body.
Essential amino acids, on the other hand, are those that cannot be synthesized in
the body and must be obtained through diet.

8.4 Properties of Amino Acids

Amino acids are crystalline, colorless solids. These are water-soluble, high-
melting-point solids that act more like salts than simple amines or carboxylic acids.
The presence of both acidic (carboxyl group) and basic (amino group) groups in
the same molecule causes this behavior.

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In aqueous solution, the carboxyl group can lose a proton and the amino group can
accept a proton, resulting in zwitter ion, a dipolar ion. This is neutral, but it does
have both positive and negative charges. Amino acids exhibit amphoteric behavior
in zwitter ionic form, reacting with both acids and bases.

Except for glycine, all other naturally occurring  -amino acids are optically active
due to the asymmetry of the -carbon atom.

These are available in both 'D' and 'L' forms. The majority of naturally occurring
amino acids have an L-configuration. The –NH2 group on the left side is used to
represent L-amino acids.

8.4.1 Isoelectric Point

An amino acid's isoelectric point (pI) is the pH at which it has no net charge. In
other words, it is the pH at which the negative charge on an amino acid exactly
balances the positive charge. pI (isoelectric point) = pH at which no net charge
exists. The pI of an amino acid with no ionizable side chain, such as alanine, is
halfway between its two pKa values. This is due to the fact that at pH = 2.34, half
of the molecules have a negatively charged carboxyl group and half have an
uncharged carboxyl group, and at pH = 9.69, half of the molecules have a
positively charged amino group and half have an uncharged amino group. As the
pH rises from 2.34, more molecules' carboxyl groups become negatively charged;
as the pH falls from 9.69, more molecules' amino groups become positively
charged.

As a result, the number of negatively charged groups equals the number of


positively charged groups when the two pKa values are averaged.

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If an amino acid has an ionizable side chain, its pI is calculated by averaging the
pKa values of similarly ionizing groups (positive ionizing to uncharged or
uncharged ionizing to positive). For example, the pI of lysine is the average of the
pKa values of two groups that are positively charged in their acidic form but
uncharged in their basic form. The pI of glutamate, on the other hand, is the
average of the pKa values of the two groups, which are uncharged in their acidic
form and negatively charged in their basic form.

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8.5 Structure of Proteins –

The Peptide Bond Proteins are polymers of  -amino acids that are linked together
by peptide bonds or peptide linkage. Peptide linkage is chemically defined as an
amide formed between the – COOH group and the –NH2 group.

The reaction between two molecules of similar or different amino acids is initiated
by the combination of one molecule's amino group with the carboxyl group of the
other. This causes the removal of a water molecule and the formation of a peptide
bond –CO–NH–.

8.6 Classification of Proteins

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Proteins can be classified into two types on the basis of their molecular shape.

(A) Fibrous Proteins

A fibrelike structure is formed when polypeptide chains run parallel and are held
together by hydrogen and disulphide bonds. In general, such proteins are insoluble
in water.

Keratin (found in hair, wool, and silk) and myosin (found in muscles) are two
common examples.

(B) Globular Proteins

This structure is formed when polypeptide chains coil around to form a spherical
shape. These are usually water soluble. Insulin and albumin are two common
globular proteins. Protein structure and shape can be studied at four different
levels: primary, secondary, tertiary, and quaternary.

(i) Primary Structure

One or more polypeptide chains can be found in proteins. Each polypeptide in a


protein contains amino acids that are linked together in a specific sequence, and
this sequence of amino acids is referred to as the protein's primary structure. Any
change in this primary structure, i.e., the amino acid sequence, results in a different
protein.

(ii) Secondary Structure

A protein's secondary structure is the shape in which a long polypeptide chain can
exist. They have been discovered to exist in two different structures:  -helix and
 -pleated sheet. These structures form as a result of the regular folding of the

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polypeptide chain's backbone caused by hydrogen bonding between the peptide
bond's C = O and –NH– groups.

The –NH group of each amino acid residue is hydrogen bonded to the C = O of an
adjacent turn of the  helix in one of the most common ways in which a
polypeptide chain forms all possible hydrogen bonds by twisting into a right
handed screw (helix).

All peptide chains in  -structure are stretched to nearly maximum extension and
then laid side by side, held together by intermolecular hydrogen bonds.

(iii) Tertiary Structure

Protein tertiary structure represents overall folding of polypeptide chains, i.e.,


further folding of the secondary structure. It produces two major molecular shapes:
fibrous and globular. Hydrogen bonds, disulphide linkages, van der Waals forces,
and electrostatic forces of attraction are the main forces that keep proteins' 2° and
3° structures stable.

(iv) Quaternary Structure

Some proteins are made up of two or more polypeptide chains known as sub-units.
The relationship of subunits to one another is referred to as quaternary structure.

8.7 Denaturation of Proteins

A native protein is a protein found in a biological system that has a distinct three-
dimensional structure and biological activity. When a protein in its native form is
subjected to physical change, such as temperature change, or chemical change,
such as pH change, the hydrogen bonds are disrupted. As a result, globules unfold,
helixes uncoil, and protein loses biological activity. This is referred to as protein
denaturation. A common example of denaturation is the coagulation of egg white

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when heated. Another example is milk curdling, which is caused by the bacteria
present in milk producing lactic acid.

9. NUCLEIC ACIDS

Every generation of every species resembles its ancestors in a variety of ways.


How are these traits passed down from one generation to the next? It has been
discovered that the nucleus of a living cell is in charge of the transmission of
inherent characteristics, also known as heredity. The particles in the nucleus of the
cell that are responsible for heredity are known as chromosomes, and they are
made up of proteins and another type of biomolecule known as nucleic acids.
These are primarily of two kinds: deoxyribonucleic acid (DNA) and ribonucleic
acid (RNA) (RNA). Because nucleic acids are long chain polymers of nucleotides,
they are also referred to as polynucleotides.

9.1 Chemical Composition of Nucleic Acids

When DNA (or RNA) is completely hydrolyzed, it produces a pentose sugar,


phosphoric acid, and nitrogen-containing heterocyclic compounds (called bases).
The sugar moiety in DNA molecules is  -D-2-deoxyribose, whereas the sugar
moiety in RNA molecules is  -D-ribose.

Adenine (A), guanine (G), cytosine (C), and thymine are the four bases found in
DNA (T). The first three bases of RNA are the same as those of DNA, but the
fourth is uracil (U).

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9.2 Structure of Nucleic Acids

A nucleoside is a unit formed by the attachment of a base to the 1' position of a


sugar. The sugar carbons in nucleosides are labeled as 1', 2', 3', and so on. To
differentiate these from the bases. A nucleotide is formed when a nucleoside is
linked to phosphoric acid at the 5'-position of the sugar moiety.

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The phosphodiester linkage between the pentose sugar's 5' and 3' carbon atoms
connects nucleotides. The following is a simplified version of the nucleic acid
chain.

The primary structure of a nucleic acid is information about the sequence of


nucleotides in its chain. Secondary structure is also present in nucleic acids. The
double strand helix structure of DNA was proposed by James Watson and Francis
Crick. Two nucleic acid chains are wrapped around each other and held together
by hydrogen bonds formed by base pairs. Because hydrogen bonds form between
specific pairs of bases, the two strands are complementary to one another. Adenine
and thymine form hydrogen bonds, whereas cytosine and guanine form hydrogen
bonds. There are helices in the secondary structure of RNA that are only single
stranded. They can fold in on themselves to form a double helix structure. There
are three types of RNA molecules, each of which serves a different purpose. They
are known as messenger RNA (m-RNA), ribosomal RNA (r-RNA), and transfer
RNA, respectively (t-RNA).

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9.3 DNA Vs RNA

9.4 Biological Functions of Nucleic Acids

DNA is the chemical basis of heredity and can be thought of as a repository of


genetic information. Over millions of years, DNA has been solely responsible for
maintaining the identity of various species of organisms. During cell division, a
DNA molecule can self-replicate, and identical DNA strands are transferred to
daughter cells. Protein synthesis in the cell is another important function of nucleic
acids. Actually, proteins are synthesised by various RNA molecules in the cell, but
the message for a specific protein's synthesis is present in DNA.

10. ENZYMES

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Enzymes function as biological catalysts. Enzymes are all globular proteins
chemically. The following are some important enzymes and their functions.

Enzyme Reaction catalysed

(i) Invertase or sucrose Sucrose  Glucose + Fructose

(ii) Maltose Maltose  Glucose + Glucose

(iii) Lactase Lactose  Glucose + Galactose

(iv)  -Amylase Starch  n  Glucose

(v) Emulsin Cellulose  n  Glucose

(vi) Urease NH2CONH2  CO2 + 2NH3

(vii) Carbonic anhydrase H2CO3  CO2 + H2O

(viii) Pepsin Protein    Amino acids

(ix) Trypsin Proteins    Amino acids

(x) Nucleases DNA or RNA  Nucleotides

(xi) DNA polymerase Deoxynucleotide  DNA Triphosphate

(xii) RNA polymerase Ribonucleotide  RNA triphosphates

11. Vitamins

Vitamin Sources Deficiency diseases

(i) Vitamin-A- Milk, cod liver oil, Night blindness,


(Retinol or eye butter, carrots, green xerosis
vitamin) leaves, tomatoes, eggs
etc.

(ii) Vitamin-B1 Pulses, nuts, green Beriberi and loss


Thiamine or vegetables, polished apetite
rice, yeast and egg

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Aneurin yolk.

(iii) Vitamin-B2 or Milk, meat, green Dard red tongue and


Riboflavin or vegetables and yeast. cheilosis
Lactoflavin

(iv) Vitamin-B6 or Rice, bran, yeast, meat, Pellagra anaemia,


Pyridoxine or fish, egg, yolk, maize, convulsions and
Adernine spinach and lettuce. specific dermatitlis
called acrodynia.

(v) Vitamin-B12 or Milk, liver, kidney and Inflammation of


Cyanocoblamin eggs. mouth, tongue and
pernicious anaemia etc.

(vi) Vitamin-C or L- Citrous fruits, amla, Brittleness and scurvy


ascorbic acid (oranges, lemons), of bones, swelling and
sprouted pulses, loosening of teeth.
germinated.

(vii) Vitamin D or Fish liver oil, cod liver Rickets in children,


Ergocal eiferol (or oil, milk and eggs. controls calcium and
antirachtic Vitamin phosphorus
of sunshine metabolism.
vitamin)

(viii) Vitamin-E or Eggs, milk, wheat Loss of sexual power


Tocopherols germ, oil cotton seed and reproduction
 ,  ,   or oil etc.
Antisterility factor

(ix) Vitamin-H (Biotin) Yeast, kidney, liver Loss of hair, dermatitis


and milk. and paralysis.

(x) Vitamin-K or Cabbage, spinach, Lengthens time of


Phylloquinones or alfalfa and carrot tops. blood clotting and
Antihaemorrhagic dermatitis
vitamin

(xi) Coenzyme Q10 Chloroplasts of green Low order of body


plants and immune system against

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mitochondria of many diseases.
animals.

12. HORMONES

Hormones are biomolecules that are produced in the ductless (endocrine) glands
and transported by the bloodstream to various parts of the body where they control
various metabolic processes. These are required in minute amounts and, unlike fats
and carbohydrates, are not stored in the body but are constantly produced.

12.1 Steroidal Hormones

Name Organ Functions


of
secretion

A Sex hormones Testes Control the growth and normal


function of androsterone and
(a) Androgens male sex organs.
(Testosterone)

Control the growth and normal


function of female sex organs.
(b) Estrogens Ovary

(Estrone, Estradiol, Estriol)


Control the onset and
continuation of pregnancy.
(c) Gestogens Corpus
(Progesterone) Iuteum

B Adenal Cortex hormones or Adernal Control the balance of water


corticoids (Cortisone, cortex and minerals in the body;
Corticosterone Aldesterone regulate the metabolism of fats,
etc.) proteins, and carbohydrates.

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12.2 Peptide Hormones

Name Organ of secretion Functions

(i) Oxytocin Posterior pituitary gland Controls uterine


contractions after
childbirth and releases
milk from the mammary
glands.

(ii) Vasopressin Posterior pituitary gland Controls water


reabsorption in the
kidney.

(iii) Angiotensin II Blood plasma of persons High blood pressure is a


potent vasoconstrictor,
which means it contracts
the blood vessels.

(iv) Insulin Pancreas Controls glucose


metabolism and keeps
blood glucose levels
stable.

12.3 Amine Hormones

Name Organ of Functions


secretion

(i) Adrenaline or Adrenal medulla It is an amine compound and the


Epinephrine first hormone discovered. Prepare
animals and humans for
emergencies in a variety of ways,
including increasing pulse rate,
blood pressure, and stimulating
the breakdown of glycogens in the
liver into blood glucose and fats
into fatty acids during an
emergency. Adrenaline is one of
the most valuable drugs used in
medicine because of these

Class XII Chemistry www.vedantu.com 35


properties.

(ii) Thyroxine Thyroid gland Controls carbohydrate, lipid, and


protein metabolism.

13. TEST FOR BIOMOLECULES

13.1 Test of Carbohydrates

13.1.1 Molish Test

The Molish test detects all types of carbohydrates, including monosaccharides,


disaccharides, and polysaccharides. Molisch reagent (1 percent alcoholic solution
of  -naphthol) is added to an aqueous carbohydrate solution, followed by conc.
H2SO4 along the test tube's sides. At the intersection of the two layers, a violet ring
forms.

13.2 Test for Proteins

13.2.1 Biuret Test

An alkaline solution of a protein when treated with a few drops of 1% CuSO4


solution, produces a violet colouration. The colour is due to the formation of a
coordination complex of Cu +2 with carbonyl group and –NH– groups of the
peptide linkages.

13.2.2 Xanthoproteic Test

When a protein is treated with concentrated HNO3 , it turns yellow. This test is
performed by a protein composed of  -amino acids containing a benzene ring,
such as tyrosine, phenylalanine, and others, and the yellow color is caused by
benzene ring nitration. An important example of this test is when concentrated

Class XII Chemistry www.vedantu.com 36


HNO3 , is spilled on your hands, the skin turns yellow due to nitration of the
benzene ring of the amino acids in your skin's proteins.

13.2.3 Millon’s Test

Millon's reagent is a nitric acid solution of mercurous nitrate and mercuric nitrate
with little nitrous acid. When Millon's reagent is added to an aqueous protein
solution, a white ppt. is formed. All proteins containing phenolic  -amino acids,
such as tyrosine, pass this test. As a result, gelatin that does not contain phenolic 
-amino acids fails this test.

13.2.4 Ninhydrin Test

A blue-violet color is produced when proteins are boiled in a dilute aqueous


solution of ninhydrin (2, 2-dihydroxyindane-1,3-dione). This test is provided by all
 -amino acids. Proteins and peptides both pass this test because they give  -
amino acids when hydrolyzed.

Class XII Chemistry www.vedantu.com 37

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