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

Tipo de material: TextoTextoSeries ; Febs Letters, 391, p.144-148, 1996Trabajos contenidos:
  • Eggert, C
  • Temp, U
  • Dean, J.F.D
  • Eriksson, K.E
Tema(s): Recursos en línea: Resumen: Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of fignin 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 too low to directly oxidize the 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 nowphenolic substrates by laccase. This is the first description of how laccase might function in a biological system for the complete depolymerization of lignin.
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Lignin peroxidase is generally considered to be a primary catalyst for oxidative depolymerization of fignin 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 too low to directly oxidize the 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 nowphenolic substrates by laccase. This is the first description of how laccase might function in a biological system for the complete depolymerization of lignin.

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