Journal
APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 76, Issue 21, Pages 7363-7366Publisher
AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.01326-10
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Funding
- Chevron Technology Ventures [RSO21]
- University of California, Davis, Committee on Research New Funding Initiative
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We cloned and purified the major family 10 xylanase (Xyn10A) from Acidothermus cellulolyticus 11B. Xyn10A was active on oat spelt and birchwood xylans between 60 degrees C and 100 degrees C and between pH 4 and pH 8. The optimal activity was at 90 degrees C and pH 6; specific activity and K-m for oat spelt xylan were 350 mu mol xylose produced min(-1) mg of protein(-1) and 0.53 mg ml(-1), respectively. Based on xylan cleavage patterns, Xyn10A is an endoxylanase, and its half-life at 90 degrees C was approximately 1.5 h in the presence of xylan.
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