| Literature DB >> 20851989 |
Ravi D Barabote1, Juanito V Parales, Ying-Yi Guo, John M Labavitch, Rebecca E Parales, Alison M Berry.
Abstract
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°C and 100°C and between pH 4 and pH 8. The optimal activity was at 90°C and pH 6; specific activity and K(m) for oat spelt xylan were 350 μmol 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°C was approximately 1.5 h in the presence of xylan.Entities:
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Year: 2010 PMID: 20851989 PMCID: PMC2976246 DOI: 10.1128/AEM.01326-10
Source DB: PubMed Journal: Appl Environ Microbiol ISSN: 0099-2240 Impact factor: 4.792