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Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching.
- 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.
- Subjects :
- Amino Acid Sequence
Bacillus subtilis genetics
Cloning, Molecular
Crystallography, X-Ray
Hot Temperature
Hydrogen Bonding
Models, Molecular
Molecular Sequence Data
Phylogeny
Protein Conformation
Xylan Endo-1,3-beta-Xylosidase genetics
Xylan Endo-1,3-beta-Xylosidase isolation & purification
Xylans chemistry
Bacillus subtilis enzymology
Industrial Microbiology
Industry
Paper
Xylan Endo-1,3-beta-Xylosidase chemistry
Subjects
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