Influence of Veratryl Alcohol and Hydrogen Peroxide on Ligninase Activity and Ligninase Production by Phanerochaete chrysosporium
- 1 February 1988
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 54 (2) , 466-472
- https://doi.org/10.1128/aem.54.2.466-472.1988
Abstract
Veratryl alcohol, added as a supplement to cultures of Phanerochaete chrysosporium , enhanced ligninase activity through protection of the ligninase against inactivation by hydrogen peroxide produced by this fungus in cultures. In the presence of veratryl alcohol, the loss of ligninase activity observed in non-protein-synthesizing cultures (cycloheximide-treated) equaled the extracellular protein turnover. When cultures were not supplemented with veratryl alcohol, inactivation of ligninase by hydrogen peroxide added to protein turnover, resulting in a more rapid loss of ligninase activity. Although all ligninase isoenzymes are sensitive to inactivation by hydrogen peroxide, only the isoenzyme of the highest specific activity (80.6 nkat · mg of protein −1 ; M r , 41,800; pI, 3.96) was found to be protected by veratryl alcohol. The concentration of veratryl alcohol necessary for full protection of ligninase activity varied according to the concentration of hydrogen peroxide present in the medium, which depended on the nature of the carbon source (glucose or glycerol). It is proposed that the nature of the carbon source influences the overall ligninase activity not only directly, by affecting the rate and the type of synthesized ligninase, but also by affecting the rate of hydrogen peroxide production, bringing about different rates of inactivation.This publication has 16 references indexed in Scilit:
- The ligninase of Phanerochaete chrysosporium generates cation radicals from methoxybenzenes.Published by Elsevier ,2021
- Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporiumJournal of Bacteriology, 1987
- Oxidation of benzo(a)pyrene by extracellular ligninases of Phanerochaete chrysosporium. Veratryl alcohol and stability of ligninase.Journal of Biological Chemistry, 1986
- Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporiumArchives of Biochemistry and Biophysics, 1985
- Lignin-degrading enzyme from Phanerochaete chrysosporium : Purification, characterization, and catalytic properties of a unique H 2 O 2 -requiring oxygenaseProceedings of the National Academy of Sciences, 1984
- Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium BurdsScience, 1983
- An extracellular H2O2-requiring enzyme preparation involved in lignin biodegradation by the white rot basidiomycete Phanerochaete chrysosporiumBiochemical and Biophysical Research Communications, 1983
- Ultrastructural Localization of Hydrogen Peroxide Production in Ligninolytic Phanerochaete chrysosporium CellsApplied and Environmental Microbiology, 1982
- Ligninolytic enzyme system of Phanaerochaete chrysosporium: synthesized in the absence of lignin in response to nitrogen starvationJournal of Bacteriology, 1978
- A Rapid and Sensitive Method for the Quantitation of Microgram Quantities of Protein Utilizing the Principle of Protein-Dye BindingAnalytical Biochemistry, 1976