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- Title
Purification and characterization of Thermobifida fusca xylanase 10B.
- Authors
Kim, Jeong H.; Irwin, Diana; Wilsor, David B.
- Abstract
Thermobifida fusca grows well on cellulose and xylan. and produces a number of cellulases and xylanases. The gene encoding a previously unstudied endoxylanase, .xyllOB, was overexpressed in E. coli, and the protein was purified and characterized. Mature XyllOB is a 43-kDa glycohydrolase with a short basic domain at the C-terminus. It has moderate thermostability, maintaining 50% of its activity after incubation for 16 h at 62°C, and is most active between pH 5 and 8, XyllOB is produced by growth of T. fusca on xylan or Solka Floe but not on pure cellulose. Mass spectroscopic analysis showed that XyllOB produces xylobiose as the major product from birchwood and oat spelts xylan and that its hydrolysis products differ from those of T. fusca XylllA, XyllOB hydrolyzes various p-nitrophenyl-sugars, including p-nitrophenyl α-D-arabinofuranoside, p-nitrophenyl-β-D-xylobioside, p-nitrophenyl-β-D-Dxyloside, and p-nitrophenyl-β-D-cellobioside, XylllA has higher activity on xylan ,substrates, but XyllOB produced more reducing sugars from corn fiber than did XylllA.
- Subjects
XYLANASES; GLYCOSIDASES; ESCHERICHIA coli; SPECTROSCOPIC imaging; GENES; HYDROLASES
- Publication
Canadian Journal of Microbiology, 2004, Vol 50, Issue 10, p835
- ISSN
0008-4166
- Publication type
Article
- DOI
10.1139/W04-077