Dimarogona Maria, Topakas Evangelos, Christakopoulos Paul
BIOtechMASS Unit, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, 5 Iroon Polytechniou Str, Zografou Campus, 15700, Athens, Greece.
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.
Comput Struct Biotechnol J. 2012 Nov 9;2:e201209015. doi: 10.5936/csbj.201209015. eCollection 2012.
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.
酶促降解植物生物质已吸引了大量研究兴趣，旨在生产具有经济可行性的生物燃料。在此，我们概述了近期关于参与纤维素氧化裂解的生物催化剂的研究发现，包括多糖单加氧酶（PMO或LPMO，即裂解性PMO）、纤维二糖脱氢酶（CDH）以及碳水化合物结合模块家族33（CBM33）的成员。PMO是一类以前称为GH61的新型酶，可提高普通纤维素酶的效率，从而提高水解产率，同时降低所需的蛋白质负载量。它们通过产生氧化和未氧化的链端作用于纤维素的结晶部分。提高PMO的活性需要外部电子供体。我们讨论了有关其作用机制的近期发现，并确定了未来需要解决的问题。
