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Cloning, Expression, and Characterization of a New Streptomyces sp. S27 Xylanase for Which Xylobiose is the Main Hydrolysis Product

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Abstract

A xylanase gene, xynBS27, was cloned from Streptomyces sp. S27 and consisted of 693 bp encoding a 230-residue protein, including a putative 41-residue signal peptide. Belonging to the glycoside hydrolase family 11, XynBS27 exhibits the maximum identity (75.9%) to the xylanase from Streptomyces sp. zxy19. Recombinant XynBS27 was overexpressed in Pichia pastoris, and the xylanase activity was 7624.0 U/ml after high-cell-density fermentation in 3.7-L fermenter. The purified recombinant XynBS27 had a high specific activity of 3272.0 U/mg. The optimum temperature and pH for XynBS27 activity was 65 °C and pH 6.5, respectively. XynBS27 showed good pH stability and retained more than 80% of the maximum activity after incubation in buffers with pH ranging between 4.0 and 12.0 at 37 °C for 1 h. The main hydrolysis product of xylan by XynBS27 was xylobiose (>75%), which was good for human health derived from its ability to modulate the intestinal function. The attractive biochemical characteristics of XynBS27 suggest that it may be a good candidate in a variety of industrial applications.

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Acknowledgments

This work was supported by National High Technology Research and Development Program of China (863 Program; no. 2007AA100601) and National Key Technology R&D Program of China (no. 2006BAD12B05-03).

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Authors and Affiliations

  1. Key Laboratory for Feed Biotechnology of the Ministry of Agriculture, Feed Research Institute, Chinese Academy of Agricultural Sciences, No. 12 Zhongguancun South Street, Beijing, 100081, People’s Republic of China

    Ning Li, Pengjun Shi, Peilong Yang, Yaru Wang, Huiying Luo, Yingguo Bai, Zhigang Zhou & Bin Yao

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  1. Ning Li
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  2. Pengjun Shi
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Correspondence to Bin Yao.

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Li, N., Shi, P., Yang, P. et al. Cloning, Expression, and Characterization of a New Streptomyces sp. S27 Xylanase for Which Xylobiose is the Main Hydrolysis Product. Appl Biochem Biotechnol 159, 521–531 (2009). https://doi.org/10.1007/s12010-008-8411-0

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