1. Presented by : Riteksha Patel

2.  Most enzymes are Proteins (tertiary and
quaternary structures).
 Act as Catalyst to accelerates a reaction.
 Not permanently changed in the process.

3.  Oxido-reductases
 Transferases
 Hydrolases
 Lyases
 Isomerases
 Ligases

4.  A change in the shape
of an enzyme’s active
Site.
 Induced by the
Substrate.

5. 1. Irreversible Inhibitors
2.Reversible Inhibitors
a)Competitive Inhibition
b) Noncompetitive Inhibition

6. 1.Irreversible inhibition: Combine with the
functional groups of the amino acids in
the active site, irreversibly.
2.Reversible inhibition: These can be
washed out of the solution of enzyme by
dialysis.

7. a. Competitive inhibition: are chemicals
that resemble an enzyme’s normal
substrate and compete with it for the
active site.
Substrate
Competitive inhibitor

8. b. Noncompetitive inhibition:
Inhibitors that do not enter the active
site, but bind to another part of the
enzyme causing the enzyme to change
its shape, which in turn alters the active
site.
Substrate Noncompetitive
Inhibitoractive site
altered

9. Enzyme Immobilization:
 Easy separation from reaction mixture,
providing the ability to control reaction times
and minimize the enzymes lost in the
product.
 Re-use of enzymes for many reaction cycles,
lowering the total production cost of enzyme
mediated reactions.
 Ability of enzymes to provide pure products.

10.  Entrapment
 Covalent binding
 Adsorption
 Encapsulation

11.  Biosensor
 Elisa
 Enzyme thermistors
 Glucose oxidase-glucose modulated
system
 Diagnosis of syphilis

12. THANK YOU