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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Bibliographic Details
Published in:Biotechnology letters 2011-07, Vol.33 (7), p.1441-1447
Main Authors: Hung, Kuo-Sheng, Liu, Shiu-Mei, Fang, Tsuei-Yun, Tzou, Wen-Shyong, Lin, Fu-Pang, Sun, Kuang-Hui, Tang, Shye-Jye
Format: Article
Language:English
Subjects:
Applied Microbiology
Biochemistry
Biological and medical sciences
Biomedical and Life Sciences
Biotechnology
carbohydrate binding
Carbohydrates
Cloning, Molecular
DNA, Bacterial - chemistry
DNA, Bacterial - genetics
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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Summary: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.
ISSN:0141-5492
1573-6776
DOI:10.1007/s10529-011-0579-7