Enzymes

Enzymes

Definition,
properties, classification and applications

Content

Ø    Definition

Ø    Properties of enzymes

Ø    Classification

Ø    Application of enzymes

Ø    Isolation of enzymes

Session Objectives

At the end of the session, student will be able to

Ø    Describe the properties of enzymes

Ø    Classify enzymes

Ø    Discuss the various applications of enzymes

Ø    Explain the different steps involved in
isolation of enzymes

Enzymes

Ø    Enzymes – soluble, colloidal organic
catalysts – produced by living cells but are capable of acting independently of
the cells

Ø  Accelerates
and catalyses thousands of biochemical reactions in the living cells   

Ø  Functional
unit of cell metabolism 

Ø    Proteinaceous in nature

Enzymes – Properties

         
Proteinaceous and High molecular weight – 12,000
– 1 million

         
Colloidal in nature

         
Soluble – water, buffer and dilute alcohol

         
Insoluble – Conc. Alcohol, acetone and other
organic solvent

         
Highly selective and specific  – action

         
Required in small quantities relative to the
substrate concentration

         
35˚ C 
40˚ C

         
Temp above 65˚ C or 0˚ C – loss of catalytic
activity – due to the disruption of polypeptide chains

         
Hence stored 
– low temp  – moisture free
container

         
Enzymes – require – a specific, heat stable, low
molecular weight organic molecule – Coenzyme

         
Some enzymes – coenzyme and one more metal
ions  – activity

         
Does not change the final equilibrium position
of reactions – only the rate of attainment of equilibrium – increased

Non protein part – co enzyme or metal (Prosthetic group) + Protein part
(Apoenzyme) = Enzymes

Structure of enzyme

       Co
enzymes – Coenzyme A, FAD, NAD

       Co
factors – Glucose – 6-phosphate – Mg, Arginase – Mn

       Protein
– Linear chain of amino acid residues joined 
– peptide bond

       Catalytic
activity depends  – L-amino acid sequence
and peptide bond constituting the protein molecule

       Localized
folding of primary structure – secondary structure

       Overall
folding – molecule – tertiary structure

       Agglomeration
of several folded chains – Quaternary structure

Enzymes – Classification

IUB classification:

1. Oxido reductases – catalyzing oxidation and
reduction between two substrates 

S reduced
+ S’ oxidized = S oxidized + S’ reduced

Eg. Alcohol dehydrogenase, lactate dehydrogenase

2. Transferase – catalyzing – transfer of S, C, N, P
other than H

S – G + S’ = S’- G
+S

Eg. Hexokinase, acetyl transferase

3. Hydrolases – catalyzing – hydrolysis of ester,
ether, peptides, glycosyl, C-C, C-halide bonds

                          
Acylcholine + H2O = Choline + acid

Eg. Urease

4. Lyases – Catalyses removal of groups from
substrates – other than hydrolysis leaving double bond – acts on C-C, C-O, C-N,
C-S bond

Eg.  Aldolase,
fumerase

5. Isomerase – catalyses – interconversion – optical,
geometric or positional isomers —- Eg. Alanine isomerase

6. Ligases – an enzyme that can catalyze the joining
of two large molecules by forming a new chemical bond, usually with
accompanying hydrolysis of chemical group on one of the larger molecules. Eg.
Pyruvate carboxylase, glutamine synthetase                                           

Other method of classification

1. Extracellular enzymes or exoenzymes  – secreted outside the cell

Eg. Cellulose, polyglucturonase

2. Intracellular enzymes or endoenzymes – secreted
within the cell

Eg. Invertase, asparaginase

Applications:

Medicinal applications

Digestive disorders-

         Papain
(Papaya)

         Pancreatin (animal pancreas)

         ß-Galactosidase (A. Oryzae)

         Penicillinase (B. subtilis)

Deworming agents

         Papain
(Papaya)

         Ficin (fig)

Anticancer agents

         Asparginase (E
coli, guinea pig)

Inflammation

         Bromelain (Pineapple)

Anti-coagulant agents

         Streptokinase
(β-hemolytic strepto cocci)

         Urokinase
(Human urine)

Surface disinfectants

         Trypsin (animal
pancreas)

Diagnostic agents

         Glucose
isomerase (diabetes)

         SGOT, SGPT,
ALP (Liver disorders)

Upper Respiratory disorders

         Chymotrypsin
(Bovine pancreas)

Food industrial applications

Tenderization of meat

         Papain (Papaya)

         Bromelain (Pineapple)

Ice cream industry

         Lactase
(prevention of lactose crystals)

Beverage industry

         Invertase
(yeast)

Chacolate industry

         Invertase (yeast)

Juice & wine processing

         Pectinase

Industrial applications

Textile industry (Destarching)

         Amylase
(Bacteria, fungi)

Leather industry (Bating)

         Proteolytic
enzymes (Bacteria, and fungi)

Detergents (Destaining)

         Alcalase

Paper industry (Bleaching of pulp)

         Xylenase
(Bacteria)

         Cellulase
(Bacteria)

Organic compounds

         Acetone

Enzymes – Production

Source of Enzymes: Living cells

1.  Plant:
Papain, Bromelain

2.  Animal: Urokinase

3.  Microorganism:

Advantages of microorganisms over other sources of
enzymes

Ø    Growth is very fast   
Grown on medium containing cheap raw materials

Ø   Genetic engineering and manipulations of
microbial cell – possible – increase the yield of enzyme

Ø   Large quantity of enzymes are produced

Ø   Animal sacrifice can be minimized

Selection of microorganism:

Ø     Non-pathogenic

Ø    Should produce extra cellular enzymes

Ø    Fermentation time should be less

Ø    Must grow on medium with cheap raw material

Ø    Must give high yield of enzymes

Ø    Must be compatible with physical and chemical
properties of medium

Ø    Strain must not produce byproducts – inhibit
the growth of m/o  Aspergillus and
Bacillus – industrial production

Isolation of enzymes

1. Extraction                            

Cell disintegration/ Cell disruption

Removal of lipids

2. Preparation of crude enzyme

Removal of nucleic acids

Centrifugation

Addition of acid or base

3. Precipitation

Salting out method

Addition of organic solvents

Addition of non-ionic polymers

Dialysis

4. Purification

Chromatographic techniques

Electrophoresis

1. Extraction

Ø    Liberation of enzyme from the cells or
cellular constituents

Ø    Break the cell wall or membrane – physical,
chemical, mechanical

Ø    Extraction medium : Buffer solution,
Temperature and pH : Optimum

Modification of extraction medium: To achieve enzyme
with maximum activity buffers can be modified by adding

              EDTA (To
remove heavy metals)

              Mercapto
ethanol (to prevent the breakage of disulphide bond of enzymes containing
cystein amino acid)

              Triton-X
(cell disruption)

Disintegration of animal and plant tissues

             Plant
tissues:
By using hammer mill/chopper mill

             Animal
tissues:   Organs or in muscles        

Defatted

â

Minced – vertical
cutter mixer

           â
Frozen

Colloidal mill

â

Cell disintegration

Summary

Ø  Enzymes
are biocatalysts, high mol.wt, Proteinaceous and water    soluble compounds

Ø    Activity 
is affected by temp, pH and heavy metals, specific in their action

Ø     Classification according to IUMAB and site
of action

Ø     Enzymes have medicinal, food and industrial
applications

Ø     Main source is plant, animal and micro
organisms

Ø     Isolation involves extraction, preparation
of crude enzyme, precipitation and purification