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

  • Biocatalysis
  • Published:
Journal of Industrial Microbiology & Biotechnology

Abstract

A xylanase gene (thxyn11A) from the Thermobifida halotolerans strain YIM 90462T 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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Acknowledgments

We are grateful to Dr. Chao Huang for technological guidance on TLC and to Dr. Guang-Yu Yang for many useful discussions. This research was supported by the National Basic Research Program of China (No. 2010CB833801), the National Natural Science Foundation of China (No. 31070007), and the International Cooperation Research Program of Yunnan Province (No. 2009AC017). W-J Li was also supported by ‘Hundred Talents Program' of the Chinese Academy of Sciences.

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Correspondence to Wen-Jun Li.

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Zhang, F., Chen, JJ., Ren, WZ. et al. Cloning, expression, and characterization of an alkaline thermostable GH11 xylanase from Thermobifida halotolerans YIM 90462T . J Ind Microbiol Biotechnol 39, 1109–1116 (2012). https://doi.org/10.1007/s10295-012-1119-8

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  • DOI: https://doi.org/10.1007/s10295-012-1119-8

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