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Lignin peroxidase of Phanerochaete chrysosporium
The production of ligninase in shallow stationary cultures and in agitated cultures is described, which give somewhat more reliable and reproducible results than the agitated cultures. Expand
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. Expand
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 HymenomycetePhanerochaeteExpand
Lignin-degrading enzyme from Phanerochaete chrysosporium: Purification, characterization, and catalytic properties of a unique H(2)O(2)-requiring oxygenase.
  • M. Tien, T. Kirk
  • Chemistry, Medicine
  • Proceedings of the National Academy of Sciences…
  • 1 April 1984
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). Expand
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 wellExpand
Oxidation of polycyclic aromatic hydrocarbons and dibenzo[p]-dioxins by Phanerochaete chrysosporium ligninase.
It is reported that this enzyme also catalyzes the oxidation of certain aromatic pollutants and compounds related to them, including polycyclic aromatic hydrocarbons with ionization potentials less than or equal to approximately 7.55 eV. Expand
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. Expand
Production of multiple ligninases by Phanerochaete chrysosporium: effect of selected growth conditions and use of a mutant strain
Two methods for increasing the production of ligninase by cultures of Phanerochaete chrysosporium grown in a nitrogen-limiting medium are described, indicating a high degree of homology between the lign inases within each strain in addition to homologybetween the corresponding lignInases of the two stains. Expand
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. Expand
Comparison of lignin peroxidase, horseradish peroxidase and laccase in the oxidation of methoxybenzenes.
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. Expand