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Engineering a high-performance, metagenomic-derived novel xylanase with improved soluble protein yield and thermostability.

Abstract：

:The novel termite gut metagenomic-derived GH11 xylanase gene xyl7 was expressed in Escherichia coli BL21, and the purified XYL7 enzyme exhibited high specific activity (6340U/mg) and broad pH active range of 5.5-10.0. Directed evolution was employed to enhance the thermostability of XYL7; two mutants (XYL7-TC and XYL7-TS) showed a 250-fold increase in half-life at 55°C, with a 10°C increase in optimal temperature compared to that of wild-type XYL7. A truncated enzyme (XYL7-Tr3) acquired by protein engineering showed similar catalytic properties as the wild-type, with a tenfold increase in soluble protein yield by the mutant. The reducing sugar produced by XYL7-TC was about fourfold greater than that produced by their parents when incubated with xylan at 60°C for 4h. The engineered novel xylanase exhibited superior enzymatic performance and showed promise as an excellent candidate for industrial application due to its high specific activity, stability and soluble protein yield.

journal_name

Enzyme Microb Technol

journal_title

Enzyme and microbial technology

authors

Qian C,Liu N,Yan X,Wang Q,Zhou Z,Wang Q

doi

10.1016/j.enzmictec.2014.11.005

subject

Has Abstract

pub_date

2015-03-01 00:00:00

pages

35-41

eissn

0141-0229

issn

1879-0909

pii

S0141-0229(14)00209-9

journal_volume

70

pub_type

杂志文章

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