Cloning, expression, and characterization of an alkaline thermostable GH11 xylanase from Thermobifida halotolerans YIM 90462T |
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Authors: | Feng Zhang Jiu-Jiu Chen Wan-Zeng Ren Lian-Bing Lin Yu Zhou Xiao-Yang Zhi Shu-Kun Tang Wen-Jun Li |
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Affiliation: | Key Laboratory of Microbial Diversity in Southwest China, Ministry of Education and Laboratory for Conservation and Utilization of Bio-Resources, Yunnan Institute of Microbiology, Yunnan University, Kunming, 650091, People's Republic of China. |
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Abstract: | 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 °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. |
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