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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Cloning, Molecular
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DNA, Bacterial / chemistry
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DNA, Bacterial / genetics
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Enzyme Activators / metabolism
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Enzyme Stability
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Escherichia coli / genetics
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Gene Expression
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Hydrogen-Ion Concentration
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Molecular Sequence Data
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Protein Sorting Signals / genetics
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Protein Structure, Tertiary
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Salts / metabolism*
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Sequence Analysis, DNA
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Temperature
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Thermoanaerobacterium / enzymology*
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Xylosidases / chemistry
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Xylosidases / genetics*
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Xylosidases / metabolism*
Substances
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DNA, Bacterial
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Enzyme Activators
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Protein Sorting Signals
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Salts
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Xylosidases