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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...
Autores principales: | , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Springer Berlin Heidelberg
2017
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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. |
format | Online Article Text |
id | pubmed-5778151 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2017 |
publisher | Springer Berlin Heidelberg |
record_format | MEDLINE/PubMed |
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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