Aoc 2 - Biocatalysis

BIOCATALYSI
S
CONTENT
 INTRODUCTION
 HISTORY
 Classification of enzymes
 Biocatalyst specificity
 Enzyme used in organic synthesis
 Recent development
 Immobilization of enzyme
INTRODUCTION
Biocatalysis refers to the use of living (biological) systems or their parts to speed up
(catalyze) chemical reactions. In biocatalytic processes, natural catalysts, such as
enzymes, perform chemical transformations on organic compounds.
Enzymes are biocatalysts- the catalysts of life. A catalyst is defined as a substance that
increases the velocity or rate of a chemical reaction without itself undergoing any change
in the overall process.
Enzymes may be defined as biocatalysts synthesized by living cells. They are protein in
nature (exception - RNA acting as ribozyme), colloidal and thermolabile in character,
and specific in their action.
HISTORICAL BACKGROUND
 Berzelius in 1836 coined the term catalysis (Greek: to dissolve).
 In 1878, Kuhne used the word enzyme (Greek: in yeast) to indicate the catalysis
taking place in the biological systems.
 Isolation of enzyme system from cell-free extract of yeast was achieved in 1883 by
Buchner. He named the active principle as zymase (later found to contain a mixture of
enzymes), which could convert sugar to alcohol.
 In 1926, James Sumner first achieved the isolation and crystallization of the enzyme
urease from jack bean and identified it as a protein.
Classification of enzyme /Biocatalyst
Classification of Biocatalyst:
1. Oxidoreductases: Enzymes involved in oxidation-reduction reactions.
2. Transferases: Enzymes that catalyse the transfer of functional groups.
3. Hydrolases: Enzymes that bring about hydrolysis of various compounds.
4. Lyases: Enzymes specialised in the addition or removal of water, ammonia,

CO2 etc.
5. Isomerases: Enzymes involved in all the isomerization reactions.
6. Ligases: Enzymes catalysing the synthetic reactions (Greek: ligate to bind)

where two molecules are joined together and ATP is used. Condensation
(usually dependent on ATP)
Biocatalyst Specificity:
Biocatalyst (enzyme) are highly specific in their action when compared with the
chemical catalysts. The occurrence of thousands of enzymes in the biological system
might be due to the specific nature of enzymes. Three types of enzyme specificity are
well-recognised:
Stereospecificity or optical specificity:

Stereoisomers are the compounds which have the same molecular formula, but
differ in their structural configuration.
(1) Stereospecificity,
(2) Reaction specificity,
(3) Substrate specificity
The enzymes act only on one isomer and, therefore, exhibit stereospecificity.
e.g. L-amino acid oxidase and D-amino acid oxidase act on L- and D-amino acids
respectively.
Reaction specificity: The same substrate can undergo different types of reactions,
each catalysed by a separate enzyme and this is referred to as reaction specificity.
An amino acid can undergo transamination, oxidative deamination,
decarboxylation, racemization etc. The enzymes however, are different for each of
these reactions.
(1) Substrate specificity: The substrate specificity varies from enzyme to enzyme. It
may be either absolute, relative or broad.
(a)Absolute substrate specificity: Certain enzymes act only on one substrate e.g.
glucokinase acts on glucose to give glucose-6 -phosphate, urease cleaves urea to
ammonia and carbon dioxide.
(b)Relative substrate specificity: Some enzymes act on structurally related

substances. This, in turn, may be dependent on the specific group or a bond present.
The action of trypsin is a good example for group.
steps:-
 Binding of substrate(s) :-Binding may be covalent but always relies on several
weak interaction , hydrogen bonding ,ionic interaction , hydrophobic interaction
 Activation of substrate(s):- Activation may be achieved by acid base catalysis,

metals, cofactor etc.
 Stabilization of transition state:-Various residues in the active site may provide

an appropriate environment.
 Product release;-Lower binding affinity than for the substrate.

EXAMPLES
In Scheme 2(A), the important features of an enzyme contributing to the different

steps are exemplified for an enzyme enabling a C–C bond formation, namely, the
acylation of resorcinol.The natural reaction of this acyltransferase is the
disproportionation of monoacetyl-phloroglucinol (Scheme 2b)
 Acyl-enzyme intermediate formed from an ester or amine can be attacked
by different nucleophiles producing, for example, esters, amides or carboxylic
acids.
Stereoselective reduction of ketones and aldehydes catalyzed

by alcohol dehydrogenases
(a) amino group transfer by transaminases.
(b)imine reduction by imine reductases.

Ethyl alcohol production
Ethanol is obtained from glucose by the enzymatic action ,glucose is converted into
ethyl alcohol and (CO2) by the enzyme catalysis of Zymase enzyme produced from
yeast.
RECENT DEVELOPMENTS
Immobilization of Enzymes
 Enzyme immobilization may be defined as a process of confining the enzyme

molecules to a solid support over which a substrate is passed and converted to
products.
Immobilization stabilizes the enzyme, moreover two or more enzymes catalyzing a

series of reaction may be placed in close proximity to one another.
Adsorption, covalent linkage , cross linking, matrix entrapment or encapsulation are

different methods for making immobilized enzymes .
Why immobilize enzymes
 Protection from degradation and deactivation.
Re –use of enzymes for many reaction cycles ,lowering the total
production cost of enzyme mediated reactions.
Easy separation of the enzymes from the product .
Enhanced stability
REFERENCES
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7844857/
Power of biocatalysis for organic synthesis-PMC
Organic synthesis using enzyme and microbes (slideshare.com)
/www.researchgate.net/publication/347973497_Biocatalysis_for_organic_synthesis
https://www.researchgate.net/publication/309242323_A_Review_on_Biological_Ca
talysts_in_Organic_Synthesis
 http://enzymetechnology.blogspot.in/2009/10/enzyme-technologyhtml

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BIOCATALYSI

 Enzyme used in organic synthesis

 Berzelius in 1836 coined the term catalysis (Greek: to dissolve).

2. Transferases: Enzymes that catalyse the transfer of functional groups.

3. Hydrolases: Enzymes that bring about hydrolysis of various compounds.

4. Lyases: Enzymes specialised in the addition or removal of water, ammonia,

5. Isomerases: Enzymes involved in all the isomerization reactions.

6. Ligases: Enzymes catalysing the synthetic reactions (Greek: ligate to bind)

Stereospecificity or optical specificity:

(b)Relative substrate specificity: Some enzymes act on structurally related

 Activation of substrate(s):- Activation may be achieved by acid base catalysis,

 Stabilization of transition state:-Various residues in the active site may provide

 Product release;-Lower binding affinity than for the substrate.

In Scheme 2(A), the important features of an enzyme contributing to the different

Stereoselective reduction of ketones and aldehydes catalyzed

(b)imine reduction by imine reductases.

 Enzyme immobilization may be defined as a process of confining the enzyme

Immobilization stabilizes the enzyme, moreover two or more enzymes catalyzing a

Adsorption, covalent linkage , cross linking, matrix entrapment or encapsulation are

Easy separation of the enzymes from the product .

Power of biocatalysis for organic synthesis-PMC

Organic synthesis using enzyme and microbes (slideshare.com)

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