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Table 3 Specific activities and kinetics of wild-type TlGlu16A and its mutants with barley β-glucan and lichenan as the substrate

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

Enzymes

Barley β-glucan

Lichenan

Specific activity (U/mg)

V max (μmol/min·mg)

V max (μmol/min·mg)

k cat/K m (mL/s·mg)

Specific activity (U/mg)

K m (mg/mL)

K m (mg/mL)

K cat/K m (mL/s·mg)

TlGlu16A

15,197 ± 153

5.74 ± 0.63

38,314 ± 187

3944 ± 156

12,770 ± 98

3.69 ± 0.54

13,447 ± 112

3643 ± 115

H58D

15,066 ± 113

2.52 ± 0.75

22,936 ± 113

5384 ± 127

13,408 ± 87

3.45 ± 0.46

27,100 ± 198

4637 ± 99

E134R

11,996 ± 79

5.04 ± 0.76

26,810 ± 154

3144 ± 143

7715 ± 88

2.64 ± 0.93

13,351 ± 167

2988 ± 198

D235G

24,040 ± 102

5.41 ± 1.01

61,350 ± 187

6701 ± 154

13,886 ± 102

9.32 ± 0.98

50,761 ± 201

3221 ± 154

D296K

18,574 ± 103

3.35 ± 0.43

25,381 ± 201

4479 ± 163

14,488 ± 101

7.39 ± 1.41

22,669 ± 175

3067 ± 103

  1. Values are means ± standard deviations