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

Authors :
Oakley AJ
Heinrich T
Thompson CA
Wilce MC
Source :
Acta crystallographica. Section D, Biological crystallography [Acta Crystallogr D Biol Crystallogr] 2003 Apr; Vol. 59 (Pt 4), pp. 627-36. Date of Electronic Publication: 2003 Mar 25.
Publication Year :
2003

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.

Details

Language :
English
ISSN :
0907-4449
Volume :
59
Issue :
Pt 4
Database :
MEDLINE
Journal :
Acta crystallographica. Section D, Biological crystallography
Publication Type :
Academic Journal
Accession number :
12657781
Full Text :
https://doi.org/10.1107/s0907444903001227