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Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases

Lytic polysaccharide monooxygenases (LPMOs) have recently been shown to significantly enhance the degradation of recalcitrant polysaccharides and are of interest for the production of biochemicals and bioethanol from plant biomass. The copper-containing LPMOs utilize electrons, provided by reducing...

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Autores principales: Frommhagen, Matthias, Westphal, Adrie H., Hilgers, Roelant, Koetsier, Martijn J., Hinz, Sandra W. A., Visser, Jaap, Gruppen, Harry, van Berkel, Willem J. H., Kabel, Mirjam A.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Springer Berlin Heidelberg 2017
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778151/
https://www.ncbi.nlm.nih.gov/pubmed/29196788
http://dx.doi.org/10.1007/s00253-017-8541-9
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author Frommhagen, Matthias
Westphal, Adrie H.
Hilgers, Roelant
Koetsier, Martijn J.
Hinz, Sandra W. A.
Visser, Jaap
Gruppen, Harry
van Berkel, Willem J. H.
Kabel, Mirjam A.
author_facet Frommhagen, Matthias
Westphal, Adrie H.
Hilgers, Roelant
Koetsier, Martijn J.
Hinz, Sandra W. A.
Visser, Jaap
Gruppen, Harry
van Berkel, Willem J. H.
Kabel, Mirjam A.
author_sort Frommhagen, Matthias
collection PubMed
description Lytic polysaccharide monooxygenases (LPMOs) have recently been shown to significantly enhance the degradation of recalcitrant polysaccharides and are of interest for the production of biochemicals and bioethanol from plant biomass. The copper-containing LPMOs utilize electrons, provided by reducing agents, to oxidatively cleave polysaccharides. Here, we report the development of a β-glucosidase-assisted method to quantify the release of C1-oxidized gluco-oligosaccharides from cellulose by two C1-oxidizing LPMOs from Myceliophthora thermophila C1. Based on this quantification method, we demonstrate that the catalytic performance of both MtLPMOs is strongly dependent on pH and temperature. The obtained results indicate that the catalytic performance of LPMOs depends on the interaction of multiple factors, which are affected by both pH and temperature. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-017-8541-9) contains supplementary material, which is available to authorized users.
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spelling pubmed-57781512018-02-01 Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases Frommhagen, Matthias Westphal, Adrie H. Hilgers, Roelant Koetsier, Martijn J. Hinz, Sandra W. A. Visser, Jaap Gruppen, Harry van Berkel, Willem J. H. Kabel, Mirjam A. Appl Microbiol Biotechnol Biotechnologically Relevant Enzymes and Proteins Lytic polysaccharide monooxygenases (LPMOs) have recently been shown to significantly enhance the degradation of recalcitrant polysaccharides and are of interest for the production of biochemicals and bioethanol from plant biomass. The copper-containing LPMOs utilize electrons, provided by reducing agents, to oxidatively cleave polysaccharides. Here, we report the development of a β-glucosidase-assisted method to quantify the release of C1-oxidized gluco-oligosaccharides from cellulose by two C1-oxidizing LPMOs from Myceliophthora thermophila C1. Based on this quantification method, we demonstrate that the catalytic performance of both MtLPMOs is strongly dependent on pH and temperature. The obtained results indicate that the catalytic performance of LPMOs depends on the interaction of multiple factors, which are affected by both pH and temperature. ELECTRONIC SUPPLEMENTARY MATERIAL: The online version of this article (10.1007/s00253-017-8541-9) contains supplementary material, which is available to authorized users. Springer Berlin Heidelberg 2017-12-02 2018 /pmc/articles/PMC5778151/ /pubmed/29196788 http://dx.doi.org/10.1007/s00253-017-8541-9 Text en © The Author(s) 2017 Open Access This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.
spellingShingle Biotechnologically Relevant Enzymes and Proteins
Frommhagen, Matthias
Westphal, Adrie H.
Hilgers, Roelant
Koetsier, Martijn J.
Hinz, Sandra W. A.
Visser, Jaap
Gruppen, Harry
van Berkel, Willem J. H.
Kabel, Mirjam A.
Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title_full Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title_fullStr Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title_full_unstemmed Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title_short Quantification of the catalytic performance of C1-cellulose-specific lytic polysaccharide monooxygenases
title_sort quantification of the catalytic performance of c1-cellulose-specific lytic polysaccharide monooxygenases
topic Biotechnologically Relevant Enzymes and Proteins
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5778151/
https://www.ncbi.nlm.nih.gov/pubmed/29196788
http://dx.doi.org/10.1007/s00253-017-8541-9
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