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Please use this identifier to cite or link to this item: http://ntour.ntou.edu.tw:8080/ir/handle/987654321/27406

Title: Characterization of a novel GH10 thermostable, halophilic xylanase from the marine bacterium Thermoanaerobacterium saccharolyticum NTOU1
Authors: Kuo-Sheng Hung;Shiu-Mei Liu;Wen-Shyong Tzou;Fu-Pang Lin;Chorng-Liang Pan;Tsuei-Yun Fang;Kuang-Hui Sun;Shye-Jye Tang
Contributors: NTOU:Department of Food Science
國立臺灣海洋大學:食品科學系
Keywords: GH10 xylanases;Thermoanaerobacterium saccharolyticum NTOU1;Pyrosequencing;Thermostable xylanase;Halophilism
Date: 2011-06
Issue Date: 2011-10-21T02:25:12Z
Publisher: Process Biochemistry
Abstract: Abstract:The thermophilic bacterium Thermoanaerobacterium saccharolyticum NTOU1 was isolated from a hydrothermal vent near Taiwan. A complete gene, xynFCB, encoding 413 amino acids and belonging to the glycosyl hydrolyase family 10 (GH10) of xylanases was identified from the genome sequence of strain NTOU1. This gene was cloned and expressed in Escherichia coli BL21(DE3)pLys. The enzyme was purified by Nickel affinity chromatography and had a molecular mass of 50 kDa. XynFCB hydrolyzed xylan with optimal activity at 63 °C and pH 6.4, and preferentially hydrolyzed oat spelt xylan. The enzyme retained more 70% of its activity between the pH values of 5.5–8.0, and its half-life was 55 min at 65 °C. XynFCB displayed enhanced activity in a dose-dependent manner in 0–12.5% (w/v) NaCl. Optimal activity was observed in 12.5% (w/v) NaCl, while 67% of its activity was retained in 15% (w/v) NaCl after a 48-h incubation. This is the first report describing the cloning, expression and characterization of a thermostable, halophilic xylanase from T. saccharolyticum.
Relation: 46(6), pp.1257–1263
URI: http://ntour.ntou.edu.tw/handle/987654321/27406
Appears in Collections:[食品科學系] 期刊論文

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