Lignin peroxidase of Phanerochaete chrysosporium
Enzymatic "combustion": the microbial degradation of lignin.
This paper presents a meta-analyses of IGNIN as a stimulus and its applications in medicine and physiology, and discusses the role that IGNIN plays in the development of disease and its role in medicine.
Influence of culture parameters on lignin metabolism byPhanerochaete chrysosporium
Culture parameters influencing metabolism of synthetic14C-lignins to14CO2 in defined media have been studied in shallow batch cultures of the ligninolytic wood-destroying HymenomycetePhanerochaete…
Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H(2)O(2)-requiring oxygenase.
An extracellular lignin-degrading enzyme from the basidiomycete Phanerochaete chrysosporium Burdsall was purified to homogeneity by ion-exchange chromatography, finding that it is an oxygenase, unique in its requirement for H(2)O(2).
Lignin-Degrading Enzyme from the Hymenomycete Phanerochaete chrysosporium Burds
The extracellular fluid of ligninolytic cultures of the wood-decomposing basidiomycete Phanerochaete chrysosporium Burds. contains an enzyme that degrades lignin substructure model compounds as well…
Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase.
Production of multiple ligninases by Phanerochaete chrysosporium: effect of selected growth conditions and use of a mutant strain
Involvement of a new enzyme, glyoxal oxidase, in extracellular H2O2 production by Phanerochaete chrysosporium
A new H2O2-producing activity of Phanerochaete chrysosporium is described that involves extracellular oxidases able to use simple aldehyde, alpha-hydroxycarbonyl, or alpha-dicarbonyl compounds as substrates.
Lignification as a Mechanism of Disease Resistance
This review deals with the formation of lignin as a mechanism of resistance to plant disease and the possible specificity of lIGNin formation in disease resistance remains unresolved.
Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.
- P. Kersten, B. Kalyanaraman, K. Hammel, B. Reinhammar, T. Kirk
- Chemistry, BiologyBiochemical Journal
- 1 June 1990
The present study investigated the possibility that other peroxidative and oxidative enzymes known to catalyse one-electron oxidations may also oxidize non-phenolics to cation-radical intermediates and that this ability is related to the redox potential of the substrate.