Pyranose oxidase, a major source of H sub(2)O sub(2) during wood degradation by Phanerochaete chrysosporium, Trametes versicolor, and Oudemansiella mucida

The production of the H sub(2)O sub(2)-generating enzyme pyranose oxidase (POD) (EC 1.1.3.10) (synonym, glucose 2-oxidase), two ligninolytic peroxidases, and laccase in wood decayed by three white rot fungi was investigated by correlated biochemical, immunological, and transmission electron microsco...

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Bibliographic Details
Published in:Applied and environmental microbiology 1994-01, Vol.60 (7), p.2524-2532
Main Authors: Daniel, G, Volc, J, Kubatova, E
Format: Article
Language:English
Subjects:
Phanerochaete chrysosporium
Trametes versicolor
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Summary:The production of the H sub(2)O sub(2)-generating enzyme pyranose oxidase (POD) (EC 1.1.3.10) (synonym, glucose 2-oxidase), two ligninolytic peroxidases, and laccase in wood decayed by three white rot fungi was investigated by correlated biochemical, immunological, and transmission electron microscopic techniques. Enzyme activities were assayed in extracts from decayed birch wood blocks obtained by a novel extraction procedure. By transmission electron microscopy-immunocytochemistry, POD was found to be preferentially localized in the hyphal periplasmic space of P. chrysosporium and O. mucida and associated with membranous materials in hyphae growing within the cell lumina or cell walls of partially and highly degraded birch fibers. The periplasmic distribution in hyphae and extracellular location of POD are consistent with the reported ultrastructural distribution of H sub(2)O sub(2)-dependent Mn-dependent peroxidases. This fact and the dominant presence of POD and Mn-dependent peroxidase in extracts from degraded wood suggest a cooperative role of the two enzymes during white rot decay by the test fungi.
ISSN:0099-2240