Construction of a highly thermostable 1,3-1,4-β-glucanase by combinational mutagenesis and its potential application in the brewing industry

Chengtuo Niu, Linjiang Zhu, Anne Elizabeth Hill, Robert Alexander Speers, Qi Li

Research output: Contribution to journalArticle

2 Citations (Scopus)
36 Downloads (Pure)

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 languageEnglish
Pages (from-to)1-10
Number of pages10
JournalBiotechnology Letters
Early online date15 Sep 2016
DOIs
Publication statusE-pub ahead of print - 15 Sep 2016

Keywords

  • 1,3-1,4-β-Glucanase
  • Catalytic property
  • Combinational mutagenesis
  • Congress mashing
  • Thermostability

ASJC Scopus subject areas

  • Biotechnology

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