Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching

被引：33
作者：
Oakley, AJ
Heinrich, T
Thompson, CA
Wilce, MCJ
机构：
[1] Univ Western Australia, Sch Med & Pharmacol, Sch Biomed & Chem Sci, Nedlands, WA 6009, Australia
[2] Ind Biosyst Pty Ltd, Belmont, WA 6104, Australia
来源：
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2003年 / 59卷
关键词：
D O I：
10.1107/S0907444903001227
中图分类号：
Q5 [生物化学];
学科分类号：
071010 ; 081704 ;
摘要：
Enzymes such as family 11 xylanases are increasingly being used for industrial applications. Here, the cloning, structure determination and temperature-stability data of a family 11 xylanase, Xyn11X, from the alkali-tolerant Bacillus subtilis subspecies B230 are reported. This enzyme, which degrades xylan polymers, is being produced on an industrial scale for use in the paper-bleaching industry. Xyn11X adopts the canonical family 11 xylanase fold. It has a greater abundance of side chain to side chain hydrogen bonds compared with all other family 11 xylanase crystal structures. Means by which the thermostability of Xyn11X might be improved are suggested.
引用
收藏
页码：627 / 636
页数：10
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