Enhanced in situ H₂O₂ production explains synergy between an LPMO with a cellulose-binding domain and a single-domain LPMO.

ABSTRACT: Lytic polysaccharide monooxygenases (LPMOs) are mono-copper enzymes that catalyze oxidative depolymerization of recalcitrant substrates such as chitin or cellulose. Recent work has shown that LPMOs catalyze fast peroxygenase reactions and that, under commonly used reaction set-ups, access to in situ generated H₂O₂ likely limits catalysis. Based on a hypothesis that the impact of a cellulose-binding module (CBM) on LPMO activity could relate to changes in in situ H₂O₂ production, we have assessed the interplay between CBM-containing ScLPMO10C and its truncated form comprising the catalytic domain only (ScLPMO10C_TR). The results show that truncation of the linker and CBM leads to elevated H₂O₂ production and decreas

SUBMITTER: Stepnov AA 

PROVIDER: S-EPMC9005612 | biostudies-literature | 2022 Apr

REPOSITORIES: biostudies-literature