title: Cellulose degradation by oxidative enzymes.
abstract: Enzymatic degradation of plant biomass has attracted intensive research interest for the production of economically viable biofuels. Here we present an overview of the recent findings on biocatalysts implicated in the oxidative cleavage of cellulose, including polysaccharide monooxygenases (PMOs or LPMOs which stands for lytic PMOs), cellobiose dehydrogenases (CDHs) and members of carbohydrate-binding module family 33 (CBM33). PMOs, a novel class of enzymes previously termed GH61s, boost the efficiency of common cellulases resulting in increased hydrolysis yields while lowering the protein loading needed. They act on the crystalline part of cellulose by generating oxidized and non-oxidized chain ends. An external electron donor is required for boosting the activity of PMOs. We discuss recent findings concerning their mechanism of action and identify issues and questions to be addressed in the future.
authors.affiliation: BIOtechMASS Unit, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, 15700, Athens, Greece.
authors.forename: Maria
authors.initials: M
authors.lastname: Dimarogona
authors.affiliation: BIOtechMASS Unit, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, 15700, Athens, Greece.
authors.forename: Evangelos
authors.initials: E
authors.lastname: Topakas
authors.affiliation: Biochemical and Chemical Process Engineering, Division of Sustainable Process Engineering, Department of Civil, Environmental and Natural Resources Engineering, Luleå University of Technology,SE-97187Luleå, Sweden.
authors.forename: Paul
authors.initials: P
authors.lastname: Christakopoulos
keywords: CBM33; GH61; bioethanol; biofuels; cellulose; polysaccharide monooxygenases