Revisiting the AA14 family of lytic polysaccharide monooxygenases and their catalytic activity
Tina R. Tuveng, Heidi Østby, Ketty C. Tamburrini, Bastien Bissaro, Olav A. Hegnar, Anton A. Stepnov, Anikó Várnai, Jean‐Guy Berrin, Vincent G. H. Eijsink
Abstract
Lytic polysaccharide monooxygenases (LPMOs) belonging to the AA14 family are believed to contribute to the enzymatic degradation of lignocellulosic biomass by specifically acting on xylan in recalcitrant cellulose-xylan complexes. Functional characterization of an AA14 LPMO from Trichoderma reesei, TrAA14A, and a re-evaluation of the properties of the previously described AA14 from Pycnoporus coccineus, PcoAA14A, showed that these proteins have oxidase and peroxidase activities that are common for LPMOs. However, we were not able to detect activity on cellulose-associated xylan or any other tested polysaccharide substrate, meaning that the substrate of these enzymes remains unknown. Next to raising questions regarding the true nature of AA14 LPMOs, the present data illustrate possible pitfalls in the functional characterization of these intriguing enzymes.