Characterization of a salt-tolerant xylanase from Thermoanaerobacterium saccharolyticum NTOU1

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...

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Veröffentlicht in:	Biotechnology letters 2011-07, Vol.33 (7), p.1441-1447
Hauptverfasser:	Hung, Kuo-Sheng, Liu, Shiu-Mei, Fang, Tsuei-Yun, Tzou, Wen-Shyong, Lin, Fu-Pang, Sun, Kuang-Hui, Tang, Shye-Jye
Format:	Artikel
Sprache:	eng
Schlagworte:	Applied Microbiology Biochemistry Biological and medical sciences Biomedical and Life Sciences Biotechnology carbohydrate binding Carbohydrates Cloning, Molecular DNA, Bacterial - chemistry DNA, Bacterial - genetics E coli Enzyme Activators - metabolism Enzyme Stability Enzymes Escherichia coli Escherichia coli - genetics Fundamental and applied biological sciences. Psychology Gene Expression Genes Glycosides Hydrogen-Ion Concentration industrial applications Life Sciences Microbiology Molecular Sequence Data Optimization Original Research Paper Peptides Protein Sorting Signals - genetics Protein Structure, Tertiary Salinity Salts - metabolism Sequence Analysis, DNA sequence homology signal peptide Sodium chloride Surface layer Temperature thermal stability Thermoanaerobacterium - enzymology Thermoanaerobacterium saccharolyticum Xylanase xylanases Xylosidases - chemistry Xylosidases - genetics Xylosidases - metabolism Yeast
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