Characterization of a family 11 xylanase from Bacillus subtillis B230 used for paper bleaching.
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.
Oakley
Aaron J
AJ
School of Biomedical and Chemical Sciences, School of Medicine and Pharmacology, University of Western Australia, Nedlands, Australia.
Heinrich
Tatjana
T
Thompson
Colin A
CA
Wilce
Matthew C J
MC
D000595:Amino Acid Sequence; D001412:Bacillus subtilis / Q000201:enzymology* / Q000235:genetics; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D006358:Hot Temperature; D006860:Hydrogen Bonding; D007218:Industrial Microbiology; D007221:Industry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010209:Paper; D010802:Phylogeny; D011487:Protein Conformation; D043325:Xylan Endo-1,3-beta-Xylosidase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D014990:Xylans / Q000737:chemistry
D014990:Xylans; D043325:Xylan Endo-1,3-beta-Xylosidase