ZLGY-MM: XI 9.

BIOMOLECULES
Biomolecules: Carbon compounds present in living systems.

ANALYSIS OF ORGANIC COMPOUNDS ANALYSIS OF INORGANIC COMPOUNDS

Acid Solubility test Ash test
(Step-1) Take a living tissue (a vegetable / piece of liver). Dry
Tissue Ash Elemental analysis
(Step-2) Grind it in trichloroacetic acid (Cl3CCOOH) using a Burn
mortar and a pestle to get a thick slurry. (Step-1) Take a living tissue (leaf or liver)
(Step-2) Dry the tissue (to evaporate water).
(Step-3) Burn it to ash (to oxidize all the C-compounds to CO2).
(Step-4) The ash is subjected to elemental analysis to know
the inorganic elements (Ca2+, Mg2+ etc) and inorganic
compounds (SO42-, PO43- etc) contained in it.

BIOMICROMOLECULES
 Biomolecules having molecular weight less than 1000 Da are
called micromolecules.
1. Amino acids
 Amino acid are organic compound containing an amino group
(Step-3) Filter the slurry through a cheesecloth or cotton; it will get (-NH2), an acid group (-COOH), H & a variable group (R)
separated to 2 fractions- attached to a C- atom (Cα).

Filtrate / Retentate /
Acid-soluble pool / Acid-insoluble fraction /
Micromolecules Macromolecules
Include: Amino acids,
Proteins, nucleic acids,
nucleotides, simple sugars,  There are 20 amino acids used as building blocks for protein
polysaccharides and lipids*
nitrogen bases etc. synthesis.
Molecular weights: 18 -800 >10,000 Da E.g. -
daltons (except lipids < 800 Da)

Grinding tissue  Lipids form vesicles (water insoluble)

⸫ lipids are not strictly macromolecules.

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 Classification -  Fatty acid are organic acids with hydrocarbon chain ending in a
A. Based on requirement by animals, amino acids are 2 types: carboxyl group (–COOH).
o Essential amino acids (should get through diet) Fatty acids are 2 types:
Lysine, leucine, isoleucine, methionine, phenylalanine, o Saturated fatty acids: No double bonds between C- atoms
tryptophan, histidine, threonine, arginine and valine include in Eg: Palmitic acid-16 C.
this type.
o Non-essential amino acids (body can synthesize)
Alanine, asparagine, aspartic acid, cysteine, glutamine, glutamic
acid, glycine, proline, serine, and tyrosine. o Unsaturated Fatty acids: Have one or more C=C bonds
Eg: Arachidonic acid- 20 C, double bonds b/w C5-6, 8-9, 11-12 & 14-15.
B. Based on the no. of amino & carboxyl group
Type Definition Example
Glutamic acid
1 amino group and
2 carboxyl group It includes monoglycerides= glycerol + 1 fatty acid
Acidic OR diglycerides = glycerol + 2 fatty acids
have a acidic group triglycerides = glycerol + 3 fatty acids
(-COOH) in R
Lysine
2 amino group and
1 carboxyl group
Basic OR
have a basic group
(-NH2) in R II. Phospholipids are lipids with phosphorus compounds
E.g. Lecithin (found in cell membrane)
1 amino group and Valine
1 carboxyl group
Neutral OR
have neither acidic
nor basic group in R

 Aromatic - Amino acids with cyclic structure in the variable

group.
III. Sterols are compounds of fused hydrocarbon ring and a long
hydrocarbon side chain. e.g.: Cholesterol (C27H46O)

Ex: Tyrosine Phenyl alanine Tryptophan

 Amino acids have ionizable –NH2 & –COOH groups. So its 3. Sugars/ Saccharide
structure changes in solutions of diff. pH.  Sugars are sweet and water soluble carbohydrates.
Amino acid, at a particular pH, possessing both NH3+ (cationic) E.g.:
& COO- (anionic) is termed as zwitter ionic (zwitterGerman= both).

2. Lipids 4. Nucleotides
 Lipids are fatty acids esterified with various alcohols. A nucleotide has 3 components:
1. A nitrogenous base- heterocyclic compound, 2 types -
Classification - Purines: It includes Adenine and Guanine.
A. Based on melting point, lipids are 2 types: fats and oils. Pyrimidines: It includes Cytosine, Thymine & Uracil.
Fats- Solid @ room temp. (↑ mp) 2. A pentose sugar (ribose in RNA & deoxyribose in DNA)
Lipids 3. A phosphate group
(Triglycerides) Oils- Liquid @ room temp. (↓ mp)
N-glycosidic linkage ester linkage
B. Based on composition, lipids are 3 types-
I. The simple lipids are formed of alcohol like glycerol and fatty acids  Nitrogen base + Sugar = Nucleoside + phosphate = Nucleotide
 Glycerol is trihydroxy propane. Adenine + ’’ = Adenosine + ’’ = Adenylic acid
Guanine + ’’ = Guanosine + ’’ = Guanylic acid
Cytosine + ’’ = Cytidine + ’’ = Cytidylic acid
Thymine + ’’ = Thymidine + ’’ = Thymidylic acid
Uracil + ’’ = Uridine + ’’ = Uridylic acid

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 E.g:
 Starch (homopolymer of glucose)
- Store energy in plant tissues
- Forms helical structure and hence it can hold I2 molecules in
the helical portion giving blue colour.
 Cellulose (homopolymer of glucose)
- Component of plant cell wall and cotton fibre
- It is a straight chain and has no complex helices. So cannot
hold I2.

Iodine solution

BIOMACROMOLECULES
 Biomolecules having molecular weight greater than 1000 I2
Dalton (Da) is called macromolecules. Blue No particular
I2
colour
1. Proteins /Polypeptides I2
 They are heteropolymers of amino acids linked by peptide bonds.
Functions of protein: Starch solution Cellulose solution
Transport nutrients across cell membranes (e.g. GLUT-4  Glycogen (homopolymer of glucose)
enables glucose transport into cell). - Reserve food in animals.
Acts as intercellular ground substance (e.g. collagen).  Inulin (homopolymer of fructose)
Acts as antibodies to fight infectious organisms.  Chitin (homopolymer of N-acetyl glucosamine)
Acts as receptors (e.g. receptors of smell, taste, hormones). - Found in cell wall of fungi & exoskeleton of arthropods
Some are hormones (e.g. Insulin), enzymes (e.g. trypsin), etc. \

 Most abundant protein in animal world: Collagen 3. Nucleic Acids /Polynucleotide

 Most abundant protein in the biosphere: RuBisCO  Nucleic acids are heteropolymer of nucleotides which function
as genetic material.
Structure of protein 2 types:
4 levels of protein structure can be recognised: - DNA (deoxyribonucleic acid): contains deoxyribose sugar
1. Primary structure: Here, the amino acids are linked with each - RNA (ribonucleic acid): contains ribose sugar.
other to form a thread-like structure.
The first amino acid (on left) is also called as N-terminal amino acid because
its –NH2 is free. The last amino acid (on right) is called the C-terminal amino METABOLITES
acid because its –COOH is free. All the biochemical reactions taking place inside a living
system together constitute metabolism.
 Metabolites are the organic compounds taking part in metabolism.
They are 2 types:-
METABOLITES
2. Secondary structure: A protein thread is folded in the form of
a right-handed helix.
3. Tertiary structure: Long protein chain is folded upon itself. Primary metabolites: Secondary metabolites: Compounds
4. Quaternary structure: Protein that are an assembly of more Compounds present in other than primary metabolites, present in
than one polypeptide or subunits. organisms with known plants, fungi or microbes, which have no
role in normal known physiological role
E.g. Hb has 4 subunits (2 α and 2 βsubunits) physiology E.g.
E.g. Pigments: Carotenoids, Anthocyanins etc.
amino acids Alkaloids: Morphine, Codeine etc.
sugars Terpenoides: Monoterpenes, Diterpenes.
lipids Essential oils: Lemon grass oil etc.
nitrogen bases Toxins: Abrin, Ricin etc.
nucleoside Lectins: Concanavalin A.
nucleotides etc. Drugs: Vinblastin, curcumin etc.
Polymeric substances: rubber, gums,
cellulose etc.

ENZYMES
2. Carbohydrates /Polysaccharides  Enzymes are proteins which catalyse biochemical reactions in
 These are polymers of sugars (monosaccharides) linked by the cells (biological catalysts).
glycosidic bond.
In a polysaccharide chain, the right end is called the reducing end (჻ it Differences b/w enzyme and inorganic catalyst
contain an aldehyde group) and the left end is called the non-reducing
end (჻ it does not contain an aldehyde group). Inorganic catalyst Enzymes
At high temperature and Get damaged (except
high pressure- works enzymes from thermophilic
efficiently organisms)
Substrate specificity- low High

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 There are about 1300 enzymes are discovered from humans
and 3000 in total.

Fastest enzyme
Carbonic anhydrase
CO2 + H2O H2CO3
Carbonic acid

Turnover in the absence of enzyme: 200 molecules / hr

Turnover in the presence of enzyme: 6,00,000 molecules / sec
Structure of Enzyme Factors affecting enzyme activity
 Enzymes are made-up of 30 proteins.
Exception: Sometimes RNA act as enzymes a) Temperature
called Ribozymes.  Optimum temperature: Temperature at which particular enzymes
 The 30 structure of an enzyme has some show highest activity.
pockets called ‘active site’ into which the Activity declines below and above optimum value.
substrate fits. o At low temperature: Enzyme temporarily inactive.
o At high temperature: Enzymes get denatured by heat.
ENZYMES

Simple Enzyme Holoenzyme

Made up of only Made-up of protein +
proteins Non-protein part

Protein part Non-protein part

b) pH
(Apoenzyme) (Co-factor)
 Optimum pH: pH at which particular enzymes show highest
activity. Enzyme activity declines below and above optimum pH.
Prosthetic group: Co-enzymes: Organic. Metal ions: Form c) Concentration of substrate
Organic. Permenantly Bound to apoenzyme co-ordination bonds Velocity of enzyme action rises with the increase in substrate
bound to apoenzyme. only during the time of with active site and
E.g. Haem in peroxidase catalysis. the substrate. concentration
and catalase. E.g. Niacin in NAD and E.g. Zn in ↓
NADP Carboxypeptidase. Reaches a maximum velocity (Vmax)
↓
Velocity does not exceeded by further rise in concentration.
Reason: Enzyme molecules are fully saturated. i.e., no active
site is left free to bind with additional substrate molecules.

Km (Michaelis –
Menten constant) is
the substrate
Enzyme action (Catalytic Cycle) Vmax concentration at
2 which the reaction
(Step-1) The substrate binds to the active site of enzyme (E+S). rate is half of the
(Step-2) Enzyme alter its shape and fits more tightly around Vmax
the substrate (ES).
(Step-3) The active site breaks / makes chemical bonds of the
Km
substrate. As a result, new enzyme-product complex is
formed (EP). d) Presence of inhibitors
(Step-4) The enzyme releases the products (E+P)  The binding of specific chemicals (inhibitor) shuts off enzyme
The free enzyme is ready to bind to another substrate. activity. This is called inhibition.
 Competitive inhibitor: inhibitor which is similar to substrate.
It competes with the substrate for the binding site of the enzyme.
↓
Inhibitor binds with binding site (substrate cannot bind)
Mechanism of Acceleration (Concept of Activation Energy) ↓
In a reaction, the substrate has to go through a much higher Enzyme action declines
energy state. It is called transition state energy. e.g. Inhibition of succinic dehydrogenase by malonate.
 Activation energy is the difference between average energy of
substrate and transition state (ES) energy.
 Role of enzyme: In a biochemical reaction, enzymes lower
Succinate Fumarate Malonate

the activation energy. As a result, speed of the reaction

increases. Active site
Succinic
dehydrogenase

Competitive inhibitors are used in the control of bacterial pathogens.

e.g. Penicillin is a competitive inhibitor that blocks the active site of
an enzyme that many bacteria use to construct their cell wall
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 Classification of Enzymes
Class Type of reaction catalysed Exemplified Reaction
1. Oxidoreductases/ Reaction involving the exchange of H2 atom or
S red + S’ ox S ox + S’red
dehydrogenases ion between two substrates
Transfer of a group (other than H) between a
2. Transferases S – G + S’ S + S’– G
pair of substrate S and S’
Hydrolysis of ester, ether, peptide, glycosidic, C-
3. Hydrolases S + H2O X+ Y
C, C-halide or P-N bonds.
Removal of groups from substrates by X Y
4. Lyases mechanisms other than hydrolysis leaving X-Y + C=C
double bond. C C
The rearrangement of molecular structure to
5. Isomerases X Y
form isomer.
The linking together of 2 compounds of C-O, C-S,
6. Ligases X + Y X–Y
C-N, P-O etc. bonds.

Chemical reactions
Chemical compounds undergo 2 types of changes:
i. Physical change: Change in shape without breaking bonds
ii. Chemical changes: Change involving breaking or making bonds
a. Inorganic chemical reactions:
e.g.: Ba(OH)2 + H2SO4  BaSO4 + 2H2O
b. Organic chemical reactions:
e.g.: Hydrolysis of starch into glucose

Rate of a reaction-

Rate doubles for 100C increase in temperature

Influence of temperature
Rate halves for 100C decrease in temperature

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 Nomenclature of Enzymes

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