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Table 3 Specific activities of the wild-type and mutant LacA enzymes using oNPG as substrate

From: Effect of mutations to amino acid A301 and F361 in thermostability and catalytic activity of the β-galactosidase from Bacillus subtilis VTCC-DVN-12-01

Transformant

Mutant LacA

Specific activity (U/mg)

Specific activity relative to wild-type (%)

WT

 

2.48 ± 0.06

100

259

F361Y

1.11 ± 0.075

44.42 ± 3.01

A524T

2.53 ± 0.078

102.19 ± 3.16

461

E62V

2.39 ± 0.045

96.31 ± 1.8

R77W

2.56 ± 0.068

103.39 ± 2.74

A191V

2.49 ± 0.073

100.6 ± 2.95

A301V

0.59 ± 0.014

23.69 ± 0.56

  1. The relative activity of β-galactosidase was determined in 100 mM buffer Z (pH 7.0) at 55°Cwith substrate oNPG (4 mg/ml)