Microbial degradation of lignin: Role of lignin peroxidase, manganese peroxidase, and laccase

By T. Higuchi. Proceedings of the Japan Academy. Series B, Physical and biological sciences, 2004

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Lignin peroxidase (LiP), laccase (LA) and manganese peroxidase (MnP) of white-rot basidiomycetes such as Phanerochaete chrysosporium, Coliorus versicolor, Phlebia radiata and Pleurotus eryngii catalyze oxidative degradation of lignin substructure model compounds and synthetic lignins (DHPs). Side chain- and aromatic ring cleavage products of both phenolic and non-phenolic substrates oxidized by LiP were isolated and characterized by NMR and MS. The cleavage mechanism was elucidated by using 18O, 2H, and 13C labeled lignin substructure dimers with 18O2 and H2 18O. Recent studies suggested that LiP is capable of oxidizing lignin directly at the protein surface via a long-range electron transfer process. LA and MnP, which oxidize phenolic but not non-phenolic moieties, generally degrade lignin stepwise from phenolic moieties. However, recent studies indicated that MnP and LA can degrade both phenolic and non-phenolic aromatic moieties of lignin with some special mediators.

Subfields: Biomedical Engineering, Biotechnology, Plant Science

View Paper: https://www.semanticscholar.org/paper/824725ca7ad07cab5170e934405fb0a828f5d806

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