A fungal metabolite mediates degradation of non-phenolic lignin structures and synthetic lignin by laccase

Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of lignin by white-rot fungi. However, some white-rot fungi lack lignin peroxidase. Instead, many produce laccase, even though the redox potentials of known laccases are two to directly oxidize non-phen...

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Bibliographic Details
Published in:FEBS letters 1996-08, Vol.391 (1), p.144-148
Main Authors: Eggert, Claudia, Temp, Ulrike, Dean, Jeffrey F.D., Eriksson, Karl-Erik L.
Format: Article
Language:English
Subjects:
2,2′-azino-bis-(3-ethylthiazoline-6-sulfonate)
3-HAA
3-Hydroxyanthranilate
ABTS
Benzyl Alcohols - metabolism
Chromatography, Gel
Chromatography, High Pressure Liquid
Cinnabarinic acid
dehydropolymerizate
DHP
Kinetics
Laccase
Lignin - metabolism
Lignin degradation
lignin peroxidase
LiP
manganese-dependent peroxidase
MnP
Molecular Structure
Oxidation-Reduction
Oxidoreductases - metabolism
Phenols
Polyporaceae - metabolism
Pycnoporus cinnabarinus
Redox mediator
White-rot
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Summary:Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of lignin by white-rot fungi. However, some white-rot fungi lack lignin peroxidase. Instead, many produce laccase, even though the redox potentials of known laccases are two to directly oxidize non-phenolic components of lignin. Pycnoporus cinnabarinus is one example of a laccase-producing fungus that degrades lignin very efficiently. To overcome the redox potential barrier, P. cinnabarinus produces a metabolite, 3-hydroxyanthranilate that can mediate the oxidation of non-phenolic substrates by laccase. This is the first description of how laccase might function in a biological system for the complete depolymerization of lignin.
ISSN:0014-5793
1873-3468
DOI:10.1016/0014-5793(96)00719-3