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Table 1 Half-lives of wild-type TlGlu16A and its mutants for thermal inactivation

From: Improvement of the thermostability and catalytic efficiency of a highly active β-glucanase from Talaromyces leycettanus JCM12802 by optimizing residual charge–charge interactions

Enzyme

t 1/2 (min) at

65 °C

70 °C

75 °C

80 °C

TlGlu16A

25

3

1

0.5

H58D

77

56

37

31

E134R

41

3

4.5

7

D235G

39

4

3.5

25

D296K

60

15

30

22

  1. The enzyme activity was assayed at each optimal condition for 10 min
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Biotechnology for Biofuels and Bioproducts

ISSN: 2731-3654

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