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通过在催化裂隙和蛋白质表面引入氨基酸取代来提高芽孢杆菌碱性木聚糖酶的嗜碱性

Improvement of alkaliphily of Bacillus alkaline xylanase by introducing amino acid substitutions both on catalytic cleft and protein surface.

作者信息

Umemoto Hirohito, Inami Mayuko, Yatsunami Rie, Fukui Toshiaki, Kumasaka Takashi, Tanaka Nobuo, Nakamura Satoshi

机构信息

Department of Bioengineering, Tokyo Institute of Technology, 4529 Nagatsuta, Midori-ku, Yokohama 226-8501, Japan.

出版信息

Biosci Biotechnol Biochem. 2009 Apr 23;73(4):965-7. doi: 10.1271/bbb.80869. Epub 2009 Apr 7.

DOI:10.1271/bbb.80869
PMID:19352020
Abstract

Xylanase J (XynJ) from alkaliphilic Bacillus sp. 41M-1 is an alkaline xylanase. The crystal structure has been solved with XynJ. Improvement of the alkaliphily of XynJ was attempted by amino acid substitutions. Reinforcing the characteristic salt bridge in the catalytic cleft and introducing excess Arg residues on the protein surface shifted the optimum pH of the wild-type enzyme from 8.5 to 9.5.

摘要

来自嗜碱芽孢杆菌41M-1的木聚糖酶J（XynJ）是一种碱性木聚糖酶。已解析出XynJ的晶体结构。尝试通过氨基酸替换来提高XynJ的嗜碱性。增强催化裂隙中的特征性盐桥并在蛋白质表面引入过量的精氨酸残基，使野生型酶的最适pH从8.5变为9.5。

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