Cloning, expression, and characterization of an alkaline thermostable GH11 xylanase from Thermobifida halotolerans YIM 90462(T)

文献类型: 外文期刊

第一作者: Zhang, Feng

作者: Zhang, Feng;Chen, Jiu-Jiu;Ren, Wan-Zeng;Zhi, Xiao-Yang;Tang, Shu-Kun;Li, Wen-Jun;Zhang, Feng;Chen, Jiu-Jiu;Ren, Wan-Zeng;Zhi, Xiao-Yang;Tang, Shu-Kun;Li, Wen-Jun;Chen, Jiu-Jiu;Lin, Lian-Bing;Zhou, Yu;Li, Wen-Jun

作者机构:

关键词: Thermobifida halotolerans YIM 90462T;Xylanase;Thermostable;Industrial application

期刊名称:JOURNAL OF INDUSTRIAL MICROBIOLOGY & BIOTECHNOLOGY ( 影响因子:3.346; 五年影响因子:3.426 )

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收录情况: SCI

摘要: A xylanase gene (thxyn11A) from the Thermobifida halotolerans strain YIM 90462(T) was cloned and expressed in Escherichia coli. The open reading frame (ORF) of thxyn11A has 1,008 bp encoding a mature xylanase with a high degree of similarity (80 %) to the xylanase from Nocardiopsis dassonvillei subsp. dassonvillei DSM 43111. This enzyme (Thxyn11A) also possesses a glycosyl hydrolases family 11 (GH11) domain and a high isoelectric point (pI = 9.1). However, Thxyn11A varies from most GH11 xylanases, due to its large molecular mass (34 kDa). Recombinant Thxyn11A demonstrated a strong pH and temperature tolerance with a maximum activity at pH 9.0 and 70 A degrees C. Xylotriose, the end-product of xylan hydrolysis by Thxyn11A, serves as a catalyst for hemicellulose pretreatment in industrial applications and can also function as a food source or supplement for enterobacteria. Due to its attractive biochemical properties, Thxyn11A may have potential value in many commercial applications.

分类号: Q81

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