Lignin-degrading enzyme activities

Yi Ru Chen, Simo Sarkanen, Yun Yan Wang

Research output: Chapter in Book/Report/Conference proceedingChapter

32 Scopus citations


Over the past three decades, the activities of four kinds of enzyme have been purported to furnish the mechanistic foundations for macromolecular lignin depolymerization in decaying plant cell walls. The pertinent fungal enzymes comprise lignin peroxidase (with a relatively high redox potential), manganese peroxidase, an alkyl aryl etherase, and laccase. The peroxidases and laccase, but not the etherase, are expressed extracellularly by white-rot fungi. A number of these microorganisms exhibit a marked preference toward lignin in their degradation of lignocellulose. Interestingly, some white-rot fungi secrete both kinds of peroxidase but no laccase, while others that are equally effective express extracellular laccase activity but no peroxidases. Actually, none of these enzymes has been reported to possess significant depolymerase activity toward macromolecular lignin substrates that are derived with little chemical modification from the native biopolymer. Here, the assays commonly employed for monitoring the traditional fungal peroxidases, alkyl aryl etherase, and laccase are described in their respective contexts. A soluble native polymeric substrate that can be isolated directly from a conventional milled-wood lignin preparation is characterized in relation to its utility in next-generation lignin-depolymerase assays.

Original languageEnglish (US)
Title of host publicationBiomass Conversion
Subtitle of host publicationMethods and Protocols
EditorsMichael Himmel
Number of pages18
StatePublished - 2012

Publication series

NameMethods in Molecular Biology
ISSN (Print)1064-3745


  • Alkyl aryl etherase
  • Laccase
  • Laccase mediator
  • Light scattering
  • Lignin
  • Lignin depolymerase
  • Lignin peroxidase
  • Manganese peroxidase
  • Reactive oxygen species
  • Versatile peroxidase
  • White-rot fungi


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