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Identification of glucose oxidase activity as the primary source of hydrogen peroxide production in ligninolytic cultures of Phanerochaete chrysosporium

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Abstract

The primary enzymatic activity involved in hydrogen peroxide (H2O2) production by extracts of ligninolytic cultures of Phanerochaete chrysosporium was investigated. Glucose supported the highest level of oxygen-dependent H2O2 production by cell extracts compared to a number of other substrates tested. No H2O2 production was observed anaerobically under N2. Polyacrylamide gel electrophoresis of extracts from ligninolytic cultures followed by diaminobenzidine/horseradish peroxidase staining procedure showed that only one protein band exhibited glucose-dependent H2O2 production. This protein band was not seen in extracts of non-ligninolytic cultures or in the extracellular fluid of ligninolytic cultures. Extracts of cells grown with either xylose, succinate or cellobiose showed the presence of only one glucose-dependent H2O2-producing band, with electrophoretic mobility similar to that observed in extracts of glucose-grown cells. Both glucose oxidase activity and lignin degradation were triggered in response to nitrogen (N) or carbohydrate starvation, and were repressed in media containing high levels of N (24 mM) or carbohydrate (56 mM), or on addition of exogenous N sources such as glutamate to the low N medium (2.4 mM N). The results indicate that glucose oxidase activity is the primary source of H2O2 in ligninolytic cultures of P. chrysosporium and that nutritional parameters which affect lignin degradation have a parallel effect on glucose oxidase activity.

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Journal article no. 10679 from the Michigan Agricultural Experiment Station

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Kelley, R.L., Reddy, C.A. Identification of glucose oxidase activity as the primary source of hydrogen peroxide production in ligninolytic cultures of Phanerochaete chrysosporium . Arch. Microbiol. 144, 248–253 (1986). https://doi.org/10.1007/BF00410957

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