Affiliation:
1. Forest Products Laboratory, Forest Service, U.S. Department of Agriculture, Madison, Wisconsin
Abstract
ABSTRACT
Pyranose 2-oxidase (POX) was recovered from
Phanerochaete chrysosporium
BKM-F-1767 solid substrate culture using mild extraction conditions and was purified.
13
C-nuclear magnetic resonance confirmed production of
d
-
arabino
-hexos-2-ulose (glucosone) from
d
-glucose with the oxidase. Peptide fingerprints generated by liquid chromatography-tandem mass spectrometry of tryptic digests and analysis of the corresponding cDNA revealed a structurally unusual sequence for the
P. chrysosporium
POX. Relatively high levels of
pox
transcript were detected under carbon-starved culture conditions but not under nutrient sufficiency. This regulation pattern is similar to that observed for lignin peroxidases, manganese peroxidases, and glyoxal oxidase of
P. chrysosporium
, supporting evidence that POX has a role in lignocellulose degradation.
Publisher
American Society for Microbiology
Subject
Ecology,Applied Microbiology and Biotechnology,Food Science,Biotechnology
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