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Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1
Kuo-Sheng Hung1, Shiu-Mei Liu, Tsuei-Yun Fang
1Institute of Bioscience and Biotechnology, National Taiwan Ocean University, No. 2 Pei-Ning Road, Keelung, Taiwan, People's Republic of China.
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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