An actinobacteria lytic polysaccharide monooxygenase acts on both cellulose and xylan to boost biomass saccharification

• Published in: Biotechnology for biofuels 2019-05, Vol.12 (1), p.117-117, Article 117
• Main Authors: Corrêa, Thamy Lívia Ribeiro, Júnior, Atílio Tomazini, Wolf, Lúcia Daniela, Buckeridge, Marcos Silveira, Dos Santos, Leandro Vieira, Murakami, Mario Tyago
• Format: Article
• Language: English
• Subjects: AA10; Actinomycetes; Biomass; Catalysis; catalytic activity; Cellulose; Chitin; Crystal structure; Crystallinity; Crystallography; Deconstruction; E coli; endo-1,4-β-Xylanase; Enzymes; Escherichia coli; glycosidases; Glycoside hydrolase; Kitasatospora; LPMO; Monooxygenase; Oxidation; Peptides; Phylogenetics; Polysaccharides; Proteins; Saccharides; Saccharification; Substrates; synergism; Synergistic effect; Xylan; Xylanase
• ISSN: 1754-6834; 1754-6834
• DOI: 10.1186/s13068-019-1449-0

Lytic polysaccharide monooxygenases (LPMOs) opened a new horizon for biomass deconstruction. They use a redox mechanism not yet fully understood and the range of substrates initially envisaged to be the crystalline polysaccharides is steadily expanding to non-crystalline ones. The enzyme LPMO10A from the actinomycete was cloned and overexpressed in cells in the functional form with native N-terminal. The enzyme can release oxidized species from chitin (C1-type oxidation) and cellulose (C1/C4-type oxidation) similarly to other AA10 members from clade II (subclade A). Interestingly, LPMO10A also cleaves isolated xylan (not complexed with cellulose, C4-type oxidation), a rare activity among LPMOs not described yet for the AA10 family. The synergistic effect of LPMO10A with Celluclast and an endo-β-1,4-xylanase also supports this finding. The crystallographic elucidation of LPMO10A at 1.6 Å resolution along with extensive structural analyses did not indicate any evident difference with other characterized AA10 LPMOs at the catalytic interface, tempting us to suggest that these enzymes might also be active on xylan or that the ability to attack both crystalline and non-crystalline substrates involves yet obscure mechanisms of substrate recognition and binding. This work expands the spectrum of substrates recognized by AA10 family, opening a new perspective for the understanding of the synergistic effect of these enzymes with canonical glycoside hydrolases to deconstruct ligno(hemi)cellulosic biomass.