Increased alkali stability in Trichoderma reesei endo-1,4-β-xylanase II by site directed mutagenesis

被引：27
|
作者：
Fenel, F
Zitting, AJ
Kantelinen, A
机构：
[1] Carbozyme Ltd, Espoo 02150, Finland
[2] Genencor Int, Jamsankoski 42300, Finland
来源：
JOURNAL OF BIOTECHNOLOGY | 2006年 / 121卷 / 01期
关键词：
endo-1,4-beta-xylanase; Trichoderma reesei; alkali stability;
D O I：
10.1016/j.jbiotec.2005.07.010
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：
A number of engineered Trichoderma reesei endo-beta-1,4-xylanase (Xyn II) mutants were created and activity tests were performed for increased stability. The stability of the earlier characterized mutant Y5 (T2C, T28C, K58R, +191D) was further increased by the mutations creating the constructs P9 (N97R+F93W+H144K), P12 (H144C+N92C), P15 (F180Q+H144C+N92C) and P21 (H22K+F180Q+H144C+N92C). The resistance towards thermal inactivation at alkaline pH was increased in all of the mutants. Residual activity T-50% was increased 4-5 degrees C for P9 at pH 9. The performance of the P9 mutant in sulphate pulp bleaching was also tested and was shown to increase brightness markedly compared to the reference. The bleaching results showed the industrial potential of the obtained mutant. (c) 2005 Elsevier B.V. All rights reserved.
引用
收藏
页码：102 / 107
页数：6
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