Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1

被引：31
|
作者：
Hung, Kuo-Sheng [1 ]
Liu, Shiu-Mei [2 ]
Fang, Tsuei-Yun [3 ]
Tzou, Wen-Shyong [1 ]
Lin, Fu-Pang [1 ]
Sun, Kuang-Hui [4 ]
Tang, Shye-Jye [1 ]
机构：
[1] Natl Taiwan Ocean Univ, Inst Biosci & Biotechnol, Keelung, Taiwan
[2] Natl Taiwan Ocean Univ, Inst Marine Biol, Keelung, Taiwan
[3] Natl Taiwan Ocean Univ, Dept Food Sci, Keelung, Taiwan
[4] Natl Yang Ming Univ, Dept Biotechnol & Lab Sci Med, Taipei 112, Taiwan
来源：
BIOTECHNOLOGY LETTERS | 2011年 / 33卷 / 07期
关键词：
Salt tolerance; Thermoanaerobacterium saccharolyticum; Thermophile; Xylanase; ENDOXYLANASE; DIVERSITY; ENZYMES; CLONING; B6A-RI;
D O I：
10.1007/s10529-011-0579-7
中图分类号：
Q81 [生物工程学（生物技术）]; Q93 [微生物学];
学科分类号：
071005 ; 0836 ; 090102 ; 100705 ;
摘要：
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 70-73A degrees 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.
引用
收藏
页码：1441 / 1447
页数：7
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