Analysis of Four Chitin-Active Lytic Polysaccharide Monooxygenases from Reveals Functional Variation.

Lytic polysaccharide monooxygenases (LPMOs) are redox-active enzymes that cleave insoluble polysaccharides by an oxidative reaction. In the present study, we have characterized four recombinant putative chitin-active LPMOs from (LPMO10B, -C, -D, and -F) and evaluated their potential in enhancing hydrolysis of α- and β-chitin by three families of 18 chitinases of , ChiA, -B, and -C. All four recombinant LPMO10s showed oxidative activity toward both α- and β-chitin but exhibited different abilities to promote the release of chitobiose from chitin by chitinases depending on both the chitinase and the chitin type.