Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1 |
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| Authors: | Hung Kuo-Sheng Liu Shiu-Mei Fang Tsuei-Yun Tzou Wen-Shyong Lin Fu-Pang Sun Kuang-Hui Tang Shye-Jye |
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| Institution: | (1) Institute of Bioscience and Biotechnology, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China;(2) Institute of Marine Biology, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China;(3) Department of Food Science, National Taiwan Ocean University, No. 2 Pei-Ning Rd, Keelung, Taiwan, People’s Republic of China;(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; |
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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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