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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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Detalles Bibliográficos
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
Descripción
Sumario: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.