Journal
BIOTECHNOLOGY LETTERS
Volume 32, Issue 12, Pages 1915-1920Publisher
SPRINGER
DOI: 10.1007/s10529-010-0372-z
Keywords
Bacillus sp.; Heterologous expression; Pichia pastoris; Thermostable xylanase
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Funding
- Ministry of Sciences and Technology of China [2007CB, 707801, 2006AA020201, 2007AA021306]
- Hubei Province Nature Science Foundation [2008CDB-058]
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A xylanase gene (xyn10) from alkaliphilic Bacillus sp. N16-5 was cloned and expressed in Pichia pastoris. The deduced amino acid sequence has 85% identity with xylanase xyn10A from B. halodurans and contains two potential N-glycosylation sites. The glycosylated Xyn10 with MW 48 kDa can hydrolyze birchwood and oatspelt xylan. The enzyme had optimum activity at pH 7 and 70 degrees C, with the specific activity of 92.5U/mg. The Xyn10 retained over 90% residual activity at 60 degrees C for 30 min but lost all activity at 80 degrees C over 15 min. Most tested ions showed no or slight inhibition effects on enzyme activity.
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