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  • Title: Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1.
    Author: Hung KS, Liu SM, Fang TY, Tzou WS, Lin FP, Sun KH, Tang SJ.
    Journal: Biotechnol Lett; 2011 Jul; 33(7):1441-7. PubMed ID: 21380775.
    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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