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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