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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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