Ligninolysis by a purified lignin peroxidase

Kenneth E. Hammel, Kenneth A. Jensen, Michael D. Mozuch, Lawrence L. Landucci, Ming Tien, Elizabeth A. Pease

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243 Scopus citations


The lignin peroxidases (LiPs) of white-rot basidiomycetes are generally thought to catalyze the oxidative cleavage of polymeric lignin in vivo. However, direct evidence for such a role has been lacking. In this investigation, 14C- and 13C-labeled synthetic lignins were oxidized with a purified isozyme of Phanerochaete chrysosporium LiP. Gel permeation chromatography of the radiolabeled polymers showed that LiP catalyzed their cleavage to give soluble lower-Mr products. To a lesser extent, the enzyme also polymerized the lignins to give soluble higher-Mr products. This result is attributable to the fact that purified LiP, unlike the intact fungus, provides no mechanism for the removal of lignin fragments that are susceptible to repolymerization. LiP catalysis also gave small quantities of insoluble, perhaps polymerized, lignin, but in lower yield than intact P. chrysosporium does. 13C NMR experiments with 13C-labeled polymer showed that LiP cleaved it between Cα and Cβ of the propyl side chain to give benzylic aldehydes at Cα, in agreement with the cleavage mechanism hypothesized earlier. The data show that LiP catalysis accounts adequately for the initial steps of ligninolysis by P. chrysosporium in vivo.

Original languageEnglish (US)
Pages (from-to)12274-12281
Number of pages8
JournalJournal of Biological Chemistry
Issue number17
StatePublished - Jun 15 1993

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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