Modification of a xylanase from bacillus pumilus with pentaammineruthenium(III)
Conference
·
OSTI ID:370061
- Oak Ridge National Lab., TN (United States)
A xylanase, xynA of Bacillus pumilus, was purified, and then modified by the attachment of pentaammineruthenium, resulting in the generation of a xylanase with veratryl alcohol oxidase activity. Modification of B. pumilus xyn A was found to greatly reduce xylan hydrolysis unless the active site of the xylanase was protected with xylose during the modification. Addition of histidine, cysteine, or reduced glutathione during xylan hydrolysis greatly increased xylanase activity of the modified xylanase. Glycine, glutamic acid, methionine, or oxidized glutathione had no effect on xylanase activity. The site of attachment of pentaammineruthenium, was identified as His-160 by mass spectroscopy and sequence determination of tryptic peptides from modified and native xylanase.
- OSTI ID:
- 370061
- Report Number(s):
- CONF-960376--
- Country of Publication:
- United States
- Language:
- English
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