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

页码：1441 / 1447

页数：7

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