Comparison of the properties of native and pentaammineruthenium(III)-modified xylanase

Barbara R. Evans, Lynette M. Lane, Ruth Margalit, Gary M. Hathaway, Arthur Ragauskas, Jonathan Woodward

Research output: Contribution to journalArticlepeer-review

Abstract

Two xylanases, xynA of Bacillus pumilus and xyn II of Trichoderma reesei, were purified and then modified by the attachment of pentaammineruthenium, thereby resulting in the generation of a xylanase with veratryl alcohol oxidase activity. Hydrolytic activity of T. reesei xyn II on soluble xylans was unchanged by modification with pentaammineruthenium; however, modification of B. pumilus xynA greatly reduced xylan hydrolysis unless the active site of the xylanase was protected with xylose during the modification. The presence of histidine, cysteine, or reduced glutathione during xylan hydrolysis greatly increased the xylanase activity of the pentaammineru-thenium-modified B. pumilus xylanase. Glycine, glutamic acid, methionine, or oxidized glutathione had no effect on xylanase activity.

Original languageEnglish
Pages (from-to)367-373
Number of pages7
JournalEnzyme and Microbial Technology
Volume19
Issue number5
DOIs
StatePublished - Oct 1996

Funding

This research was sponsored by the Laboratory Directed Researcha nd Development Program at Oak Ridge National Laboratory which is managedb y Lockheed Martin Energy Systems, Inc., for the U.S. Department of Energy under contract number DE-AC05840R21400. B. R. Evans is a postdoctoral research associated at Oak Ridge National Laboratories through the Oak Ridge Institute for Science and Education at Oak Ridge Associated Universities. The Jet Propulsion Laboratory is an operating division of the California Institute of Technology under contract NAS7-918 with the National Aeronautics and Space Administration. Address reprint requests to Dr. Barbara R. Evans, Senior Biochemist, Oak Ridge National Laboratory, MS6194, Rm. A-5, 4500 N. Bethel Valley Road, Oak Ridge. TN 3783 1 ‘Managed by Lockheed Martin Energy Systems, Inc., for the U.S. Department of Energy under contract DE-AC05-840R21400 ‘Operating Division of California Institute of Technology under contract NAS7-918 with the National Aeronautics and Space Administration “The submitted manuscript has been authored by a contractor of the U.S. Government under contract No. DE-AC05-840R21400. Accordingly, the U.S. Government retains a nonexclusive, royalty-free license to publish or reproduce the published form of this contribution, or allow others to do so, for U.S. Government purposes.” Received 9 October 1995; revised 7 December 1995; accepted 17 December 1995

FundersFunder number
Laboratory Directed Researcha
Lockheed Martin Energy Systems, Inc.
U.S. Government
U.S. Department of EnergyDE-AC05-840R21400
National Aeronautics and Space Administration
Oak Ridge National Laboratory
California Institute of TechnologyNAS7-918

    Keywords

    • Chemical modification
    • Oxidase
    • Ruthenium
    • Xylanase

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