Synthesis of thermostable mutants of the Trichoderma reesei xylanase

被引：0

作者：

Sung, WL ^{[1
]}

Yaguchi, M ^{[1
]}

Ishikawa, K ^{[1
]}

Huang, F ^{[1
]}

Wood, M ^{[1
]}

Zahab, DM ^{[1
]}

机构：

[1] Natl Res Council Canada, Inst Biol Sci, Ottawa, ON K1A 0R6, Canada

来源：

7TH INTERNATIONAL CONFERENCE ON BIOTECHNOLOGY IN THE PULP AND PAPER INDUSTRY - POSTER PRESENTATIONS VOL C | 1998年

关键词：

D O I：

暂无

中图分类号：

Q81 [生物工程学（生物技术）]; Q93 [微生物学];

学科分类号：

071005 ; 0836 ; 090102 ; 100705 ;

摘要：

The thermostability, temperature and pH optima of Trichoderma reesei xylanase II (TrX) have been increased by protein engineering. This was accomplished through the substitution of its (1-29) region with the corresponding sequence of the Thermomonospora fusca xylanase (TfX). The resultant chimeric xylanase showed an improvement of +10 degrees C and +0.7 unit in the optimal temperature and pH as compared to the recombinant wild-type TrX, Upstream extension from the -1 position of the new xylanase with a tripeptide G-R-R, elevated the optimal temperature and pH by 13 degrees C and 0.9 unit respectively. An improvement of thermostability by 15 degrees C was also observed. Site-specific mutagenesis of the (1-29) region of TrX identified three mutations (Asn10His, Tyr27Met and Asl29Leu) essential for the improvement in the chimeric xylanase.

引用

页码：C61 / C63

页数：3

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