Abstract
Objectives: To improve the thermostability and catalytic property of a mesophilic 1,3-1,4-β-glucanase by combinational mutagenesis and to test its effect in congress mashing. Results: A mutant β-glucanase (rE-BglTO) constructed by combinational mutagenesis showed a 25 °C increase in optimal temperature (to 70 °C) a 19.5 °C rise in T50 value and a 15.6 °C increase in melting temperature compared to wild-type enzyme. Its half-life values at 60 and 70 °C were 152 and 99 min, which were 370 and 800 % higher than those of wild-type enzyme. Besides, its specific activity and kcat value were 42,734 U mg−1 and 189 s−1 while its stability under acidic conditions was also improved. In flask fermentation, the catalytic activity of rE-BglTO reached 2381 U ml−1, which was 63 % higher than that of wild-type enzyme. The addition of rE-BglTO in congress mashing decreased the filtration time and viscosity by 21.3 and 9.6 %, respectively. Conclusions: The mutant β-glucanase showed high catalytic activity and thermostability which indicated that rE-BglTO is a good candidate for application in the brewing industry.
Original language | English |
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Pages (from-to) | 1-10 |
Number of pages | 10 |
Journal | Biotechnology Letters |
Early online date | 15 Sept 2016 |
DOIs | |
Publication status | E-pub ahead of print - 15 Sept 2016 |
Keywords
- 1,3-1,4-β-Glucanase
- Catalytic property
- Combinational mutagenesis
- Congress mashing
- Thermostability
ASJC Scopus subject areas
- Biotechnology