23.6.3 Mechanism of E
z m Action
E
z
m are the powerful catalyst; the nature of catalysis taking place in the biological
S ys
T is like that of non-biological catalysis. In any R e
at the reactants have to be a
triggered state or transition state. We know the energy required by the reactants to
carry out R e
at as activation energy (Aguilar and Hearn 1996). When the reactant is
heated then attain the energy. The catalyst reduces the activation energy (E
z
m in the
biological S ys
T ) and this causes the R e
at to proceed at a lower temperature. As we
have discussed that E
z
m do not alter the equilibrium constant, it just enhances the
rate of R e
at . The E
z
m lowers energy barrier of reactants, making the R e
at go faster.
The E
z
m reduce the activation energy of the reactants in such a way that all the
biological S ys
T occur at B
D
Y temperature (below 40 °C) (Mant and Hodges 1996).
23.6.4 Important Industrial E
z m and Their Sources
It may extract E
z
m those biologically active from any living organism. It uses a wide
range of sources for commercial E
z
m production from spinach to snake venom.
More than a hundred E
z
m being used industrially, it may prevail E
z
m from P
l
T ,
animals, bacteria, fungi or yeast sources (Aguilar 2004). A very much larger
number of E
z
m find use in chemical analysis and chemical diagnosis (Lin and
Karger 1990). They prefer microbes to P
l
T and animals as a source of E
z
m . The
details are remarked in the Tables 23.10, 23.11, 23.12, 23.13 and 23.14.
Table 23.9 International classification of E
z
m
S. No.
Classes
Type of R e
at catalysed
1
Oxidoreductases
Transfer of electrons (Hydride ions or H atom)
2
Transferases
Group transfer R e
at
3
Hydrolases
Hydrolysis R e
at (Transfer of functional groups of water)
4
Lyases
Addition of groups to double bonds, formation of double bonds
by removal of groups
5
Isomerases
Transfer of groups within molecules to yield isomeric forms
6
Ligases
Formation of C–C, C–S, C–O, and C–N bonds by condensation
R e
at coupled to ATP cleavage
Table 23.10 List of E
z
m
received from animal source
E
z
m
EC
number
Source
Industrial
use
Catalase
1.11.1.6
Liver
Food
Chymotrypsin
3.4.21.1
Pancreas
Leather
Lipase
3.4.23.4
Pancreas
Food
Rennet
3.4.23.4
Abomasum
Cheese
Trypsin
3.4.21.4
Pancreas
Leather
23 Protein and Enzymes Isolated from Plant Sources …
811
z m Action
E
z
m are the powerful catalyst; the nature of catalysis taking place in the biological
S ys
T is like that of non-biological catalysis. In any R e
at the reactants have to be a
triggered state or transition state. We know the energy required by the reactants to
carry out R e
at as activation energy (Aguilar and Hearn 1996). When the reactant is
heated then attain the energy. The catalyst reduces the activation energy (E
z
m in the
biological S ys
T ) and this causes the R e
at to proceed at a lower temperature. As we
have discussed that E
z
m do not alter the equilibrium constant, it just enhances the
rate of R e
at . The E
z
m lowers energy barrier of reactants, making the R e
at go faster.
The E
z
m reduce the activation energy of the reactants in such a way that all the
biological S ys
T occur at B
D
Y temperature (below 40 °C) (Mant and Hodges 1996).
23.6.4 Important Industrial E
z m and Their Sources
It may extract E
z
m those biologically active from any living organism. It uses a wide
range of sources for commercial E
z
m production from spinach to snake venom.
More than a hundred E
z
m being used industrially, it may prevail E
z
m from P
l
T ,
animals, bacteria, fungi or yeast sources (Aguilar 2004). A very much larger
number of E
z
m find use in chemical analysis and chemical diagnosis (Lin and
Karger 1990). They prefer microbes to P
l
T and animals as a source of E
z
m . The
details are remarked in the Tables 23.10, 23.11, 23.12, 23.13 and 23.14.
Table 23.9 International classification of E
z
m
S. No.
Classes
Type of R e
at catalysed
1
Oxidoreductases
Transfer of electrons (Hydride ions or H atom)
2
Transferases
Group transfer R e
at
3
Hydrolases
Hydrolysis R e
at (Transfer of functional groups of water)
4
Lyases
Addition of groups to double bonds, formation of double bonds
by removal of groups
5
Isomerases
Transfer of groups within molecules to yield isomeric forms
6
Ligases
Formation of C–C, C–S, C–O, and C–N bonds by condensation
R e
at coupled to ATP cleavage
Table 23.10 List of E
z
m
received from animal source
E
z
m
EC
number
Source
Industrial
use
Catalase
1.11.1.6
Liver
Food
Chymotrypsin
3.4.21.1
Pancreas
Leather
Lipase
3.4.23.4
Pancreas
Food
Rennet
3.4.23.4
Abomasum
Cheese
Trypsin
3.4.21.4
Pancreas
Leather
23 Protein and Enzymes Isolated from Plant Sources …
811