@article{65c3c46704224d0e96f7311b772fc2c7,
title = "Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1",
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.",
keywords = "Salt tolerance, Thermoanaerobacterium saccharolyticum, Thermophile, Xylanase",
author = "Hung, {Kuo Sheng} and Liu, {Shiu Mei} and Fang, {Tsuei Yun} and Tzou, {Wen Shyong} and Lin, {Fu Pang} and Sun, {Kuang Hui} and Tang, {Shye Jye}",
note = "Funding Information: Acknowledgments This work was financially supported by the Center for Marine Bioscience and Biotechnology (CMBB). We thank Dr. Tze-Tze Liu for the consultation on whole genomic DNA sequencing.",
year = "2011",
month = jul,
doi = "10.1007/s10529-011-0579-7",
language = "English",
volume = "33",
pages = "1441--1447",
journal = "Biotechnology Letters",
issn = "0141-5492",
publisher = "Springer Netherlands",
number = "7",
}