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Cellulose degradation by oxidative enzymes

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...

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Autores principales: Dimarogona, Maria, Topakas, Evangelos, Christakopoulos, Paul
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962083/
https://www.ncbi.nlm.nih.gov/pubmed/24688656
http://dx.doi.org/10.5936/csbj.201209015
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author Dimarogona, Maria
Topakas, Evangelos
Christakopoulos, Paul
author_facet Dimarogona, Maria
Topakas, Evangelos
Christakopoulos, Paul
author_sort Dimarogona, Maria
collection PubMed
description 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.
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spelling pubmed-39620832014-03-31 Cellulose degradation by oxidative enzymes Dimarogona, Maria Topakas, Evangelos Christakopoulos, Paul Comput Struct Biotechnol J Mini Review 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. Research Network of Computational and Structural Biotechnology (RNCSB) Organization 2012-11-09 /pmc/articles/PMC3962083/ /pubmed/24688656 http://dx.doi.org/10.5936/csbj.201209015 Text en © Dimarogona et al. http://creativecommons.org/licenses/by/3.0/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are properly cited.
spellingShingle Mini Review
Dimarogona, Maria
Topakas, Evangelos
Christakopoulos, Paul
Cellulose degradation by oxidative enzymes
title Cellulose degradation by oxidative enzymes
title_full Cellulose degradation by oxidative enzymes
title_fullStr Cellulose degradation by oxidative enzymes
title_full_unstemmed Cellulose degradation by oxidative enzymes
title_short Cellulose degradation by oxidative enzymes
title_sort cellulose degradation by oxidative enzymes
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3962083/
https://www.ncbi.nlm.nih.gov/pubmed/24688656
http://dx.doi.org/10.5936/csbj.201209015
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