Abstract
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°C, with the specific activity of 92.5U/mg. The Xyn10 retained over 90% residual activity at 60°C for 30 min but lost all activity at 80°C over 15 min. Most tested ions showed no or slight inhibition effects on enzyme activity.
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Acknowledgments
This study was supported by the Ministry of Sciences and Technology of China (973 programs 2007CB707801, 863 programs 2006AA020201 and 2007AA021306) and Hubei Province Nature Science Foundation (2008CDB058).
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Zhang, G., Mao, L., Zhao, Y. et al. Characterization of a thermostable xylanase from an alkaliphilic Bacillus sp.. Biotechnol Lett 32, 1915–1920 (2010). https://doi.org/10.1007/s10529-010-0372-z
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DOI: https://doi.org/10.1007/s10529-010-0372-z