Abstract
We show that the N-terminal 'thermostabilizing domain' (TSD) of the xylanase, XynA, from the thermophilic bacterium Caldibacillus cellulovorans also acts as a xylan binding domain. Affinity electrophoresis experiments show that this TSD selectively binds soluble xylan and binds weakly to hydroxyethylcellulose. Based on this, and previously reported evidence, we propose that xylanase-associated TSDs are xylan binding domains.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Amino Acid Sequence
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Base Sequence
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Clostridium / enzymology*
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DNA Primers
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Electrophoresis, Polyacrylamide Gel / methods
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Endo-1,4-beta Xylanases
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Molecular Sequence Data
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Protein Binding
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Sequence Homology, Amino Acid
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Temperature
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Xylans / metabolism*
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Xylosidases / chemistry
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Xylosidases / isolation & purification
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Xylosidases / metabolism*
Substances
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DNA Primers
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Xylans
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Xylosidases
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Endo-1,4-beta Xylanases