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Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1

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Abstract

A xylanase gene was PCR-cloned from Thermoanaerobacterium saccharolyticum and expressed in Escherichia coli. The xylanase (XynA) consisted of a signal peptide, glycoside hydrolase family 10 domains, carbohydrate-binding modules, and surface layer homology domains. It was optimally active at 70–73°C and at pH 5–7. It had enhanced activity with NaCl with optimal activity at 0.4 M but was tolerant up to 2 M NaCl. The thermostable and salt-tolerant properties of this xylanase suggest that it may be useful for industrial applications.

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Acknowledgments

This work was financially supported by the Center for Marine Bioscience and Biotechnology (CMBB). We thank Dr. Tze-Tze Liu for the consultation on whole genomic DNA sequencing.

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Authors and Affiliations

  1. Institute of Bioscience and Biotechnology, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China

    Kuo-Sheng Hung, Wen-Shyong Tzou, Fu-Pang Lin & Shye-Jye Tang

  2. Institute of Marine Biology, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China

    Shiu-Mei Liu

  3. Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China

    Tsuei-Yun Fang

  4. Department of Biotechnology and Laboratory Science in Medicine, National Yang-Ming University, No. 155, Sec. 2, Linong Street, Taipei, Taiwan, People’s Republic of China

    Kuang-Hui Sun

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  1. Kuo-Sheng Hung
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  2. Shiu-Mei Liu
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  3. Tsuei-Yun Fang
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  4. Wen-Shyong Tzou
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  5. Fu-Pang Lin
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  6. Kuang-Hui Sun
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  7. Shye-Jye Tang
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Correspondence to Shye-Jye Tang.

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Hung, KS., Liu, SM., Fang, TY. et al. Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1. Biotechnol Lett 33, 1441–1447 (2011). https://doi.org/10.1007/s10529-011-0579-7

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  • DOI: https://doi.org/10.1007/s10529-011-0579-7

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