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Table 3 Substrate specificity and chemoselectivity of purified nitrilase isolated from A. niger K10 (Nit-ANigWT) and heterologously expressed nitrilase (Nit-ANigRec)

From: Heterologous expression, purification and characterization of nitrilase from Aspergillus nigerK10

Substrate

Relative activity, %

Amide, molar % of total product

 

Nit-ANigWT

Nit-ANigRec

Nit-ANigWT

Nit-ANigRec

Benzonitrile

27

4.9

9

0

2-Chlorobenzonitrile

0

0

-

-

3-Chlorobenzonitrile

10

3.7

3

5

4-Chlorobenzonitrile

8.4

0.2

80

0

2-Cyanopyridine

2.4

100

88

23

3-Cyanopyridine

4.6

12.9

6

2

4-Cyanopyridine

100

0.8

36

0

Phenylacetonitrile

4.9

0.2

0

0

2-Phenylpropionitrile

traces

0

0

0

  1. Enzyme activity was assayed as described in Methods. The specific activities of Nit-ANigWT and Nit-ANigRec for their best substrates 4-cyanopyridine (306 U mg-1 at 45°C) and 2-cyanopyridine (9.0 U mg-1 at 38°C), respectively, were taken as 100%. Data represent the mean of four independent measurements with relative standard deviation values <5%.
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BMC Biotechnology

ISSN: 1472-6750

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