Lignocellulose degradation mechanisms across the Tree of Life

Simon M. Cragg*, Gregg T. Beckham, Neil C. Bruce, Timothy D H Bugg, Daniel L. Distel, Paul Dupree, Amaia Green Etxabe, Barry S. Goodell, Jody Jellison, John E. McGeehan, Simon J. McQueen-Mason, Kirk Schnorr, Paul H. Walton, Joy E M Watts, Martin Zimmer

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

Abstract

Organisms use diverse mechanisms involving multiple complementary enzymes, particularly glycoside hydrolases (GHs), to deconstruct lignocellulose. Lytic polysaccharide monooxygenases (LPMOs) produced by bacteria and fungi facilitate deconstruction as does the Fenton chemistry of brown-rot fungi. Lignin depolymerisation is achieved by white-rot fungi and certain bacteria, using peroxidases and laccases. Meta-omics is now revealing the complexity of prokaryotic degradative activity in lignocellulose-rich environments. Protists from termite guts and some oomycetes produce multiple lignocellulolytic enzymes. Lignocellulose-consuming animals secrete some GHs, but most harbour a diverse enzyme-secreting gut microflora in a mutualism that is particularly complex in termites. Shipworms however, house GH-secreting and LPMO-secreting bacteria separate from the site of digestion and the isopod Limnoria relies on endogenous enzymes alone. The omics revolution is identifying many novel enzymes and paradigms for biomass deconstruction, but more emphasis on function is required, particularly for enzyme cocktails, in which LPMOs may play an important role.

Original languageEnglish
Pages (from-to)108-119
Number of pages12
JournalCurrent Opinion in Chemical Biology
Volume29
DOIs
Publication statusPublished - Dec 2015

Cite this