Lytic xylan oxidases from wood-decay fungi unlock biomass degradation

Couturier, Marie; Ladev�ze, Simon; Sulzenbacher, Gerlind; Ciano, Luisa; Fanuel, Mathieu; Moreau, C�line; Villares, Ana; Cathala, Bernard; Chaspoul, Florence; Frandsen, Kristian E; Labourel, Aurore; Herpo�l-Gimbert, Isabelle; Grisel, Sacha; Haon, Mireille; Lenfant, Nicolas; Rogniaux, H�l�ne; Ropartz, David; Davies, Gideon J; Rosso, Marie-No�lle; Walton, Paul H; Henrissat, Bernard; Berrin, Jean-Guy

Abstract

Wood biomass is the most abundant feedstock envisioned for the development of modern biorefineries. However, the cost-effective conversion of this form of biomass into commodity products is limited by its resistance to enzymatic degradation. Here we describe a new family of fungal lytic polysaccharide monooxygenases (LPMOs) prevalent among white-rot and brown-rot basidiomycetes that is active on xylans - a recalcitrant polysaccharide abundant in wood biomass. Two AA14 LPMO members from the white-rot fungus Pycnoporus coccineus substantially increase the efficiency of wood saccharification through oxidative cleavage of highly refractory xylan-coated cellulose fibers. The discovery of this unique enzyme activity advances our knowledge on the degradation of woody biomass in nature and offers an innovative solution for improving enzyme cocktails for biorefinery applications.

Citation

Couturier, M., Ladevèze, S., Sulzenbacher, G., Ciano, L., Fanuel, M., Moreau, C., Villares, A., Cathala, B., Chaspoul, F., Frandsen, K. E., Labourel, A., Herpoël-Gimbert, I., Grisel, S., Haon, M., Lenfant, N., Rogniaux, H., Ropartz, D., Davies, G. J., Rosso, M.-N., Walton, P. H., …Berrin, J.-G. (2018). Lytic xylan oxidases from wood-decay fungi unlock biomass degradation. Nature Chemical Biology, 14(3), 306-310. https://doi.org/10.1038/nchembio.2558

• Journal Article Type: Article
• Acceptance Date: Dec 11, 2017
• Online Publication Date: Jan 29, 2018
• Publication Date: 2018-03
• Deposit Date: Feb 13, 2020
• Publicly Available Date: Feb 18, 2020
• Journal: Nature Chemical Biology
• Print ISSN: 1552-4450
• Electronic ISSN: 1552-4469
• Publisher: Nature Publishing Group
• Peer Reviewed: Peer Reviewed
• Volume: 14
• Issue: 3
• Pages: 306-310
• DOI: https://doi.org/10.1038/nchembio.2558
• Keywords: Cell Biology; Molecular Biology
• Public URL: https://nottingham-repository.worktribe.com/output/3829588
• Publisher URL: https://www.nature.com/articles/nchembio.2558
• Additional Information: Received: 7 May 2017; Accepted: 11 December 2017; First Online: 29 January 2018; : The authors declare no competing financial interests.