Role of Veratryl Alcohol in Regulating Ligninase Activity in Phanerochaete chrysosporium
Authors:
- 1 August 1986
- journal article
- research article
- Published by American Society for Microbiology in Applied and Environmental Microbiology
- Vol. 52 (2) , 251-254
Abstract
Ligninase activity in Phanerochaete chrysosporium is stimulated by incubating cultures with various substrates for the enzyme, including veratryl (3,4-dimethoxybenzyl) alcohol, which is a secondary metabolite of this fungus. This study was designed to provide insight into the mechanism involved in this stimulation. Ligninase activity increased 2 to 4 h after the addition of exogenous veratryl alcohol to ligninolytic cultures. This increase was prevented by inhibitors of protein synthesis. Analysis of the extracellular proteins by high-performance anion-exchange liquid chromatography revealed increases in the amounts of some, but not all, ligninase species. The normal rapid decrease in ligninase activity in aging cultures was not prevented or retarded by veratryl alcohol, indicating that veratryl alcohol does not increase ligninase activity by protecting extant enzyme. We conclude that veratryl alcohol probably functions via an induction type of mechanism, affecting only certain ligninase species. Results with an isolated lignin indicate that lignin (or its biodegradation products) functions in the same way that veratryl alcohol does.Keywords
This publication has 14 references indexed in Scilit:
- Multiple molecular forms of diarylpropane oxygenase, an H2O2-requiring, lignin-degrading enzyme from Phanerochaete chrysosporiumArchives of Biochemistry and Biophysics, 1985
- Phenotypic classes of phenoloxidase-negative mutants of the lignin-degrading fungus Phanerochaete chrysosporiumJournal of Bacteriology, 1985
- Factors Involved in the Regulation of a Ligninase Activity in Phanerochaete chrysosporiumApplied and Environmental Microbiology, 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
- Incorporation of 18O2 and absence of stereospecificity in primary product formation during fungal metabolism of a lignin model compoundBiochimica et Biophysica Acta (BBA) - General Subjects, 1982
- Ligninolytic activity of Phanerochaete chrysosporium: Physiology of suppression by NH 4 + and l-glutamateArchives of Microbiology, 1981
- Relationship of nitrogen to the onset and suppression of ligninolytic activity and secondary metabolism in Phanerochaete chrysosporiumArchives of Microbiology, 1981
- Biosynthesis of the secondary metabolite veratryl alcohol in relation to lignin degradation in Phanerochaete chrysosporiumArchives of Microbiology, 1981