| Literature DB >> 12657781 |
Aaron J Oakley1, Tatjana Heinrich, Colin A Thompson, Matthew C J Wilce.
Abstract
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.Entities:
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Year: 2003 PMID: 12657781 DOI: 10.1107/s0907444903001227
Source DB: PubMed Journal: Acta Crystallogr D Biol Crystallogr ISSN: 0907-4449