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
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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.
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页码：C61 / C63
页数：3
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