Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A

Cost-efficient plant biomass conversion using biochemical and/or chemical routes is essential for transitioning to sustainable chemical technologies and renewable biofuels. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that make part of modern hydrolytic cocktails destined...

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Autores principales:	Ana Gabriela Sepulchro, Vanessa Pellegrini, Lucas Dias, Marco Kadowaki, David Cannella, Igor Polikarpov
Formato:	article
Lenguaje:	EN
Publicado:	Green Wave Publishing of Canada 2021
Materias:	lytic polysaccharide monooxygenases chlorophyllin light co-substrates utilization Fuel TP315-360 Energy industries. Energy policy. Fuel trade HD9502-9502.5
Acceso en línea:	https://doaj.org/article/079764d604a44a068fe5b8e9ca04bfc1
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spelling	oai:doaj.org-article:079764d604a44a068fe5b8e9ca04bfc12021-11-30T13:24:37ZCombining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A2292-878210.18331/BRJ2021.8.3.5https://doaj.org/article/079764d604a44a068fe5b8e9ca04bfc12021-09-01T00:00:00Zhttps://www.biofueljournal.com/article_135752_d83020ca75fecb89b861d22bcec7b282.pdfhttps://doaj.org/toc/2292-8782Cost-efficient plant biomass conversion using biochemical and/or chemical routes is essential for transitioning to sustainable chemical technologies and renewable biofuels. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that make part of modern hydrolytic cocktails destined for plant biomass degradation. Here, we characterized MtLPMO9A from Thermothelomyces thermophilus M77 (formerly Myceliophthora thermophila) and demonstrated that it could be efficiently driven by chlorophyllin excited by light in the presence of a reductant agent. However, in the absence of chemical reductant, chlorophyllin and light alone do not lead to a significant release of the reaction products by the LPMO, indicating a low capacity of MtLPMO9A reduction (either via direct electron transfer or via superoxide ion, O2•-). We showed that photocatalysis could significantly increase the LPMO activity against highly crystalline and recalcitrant cellulosic substrates, which are poorly degraded in the absence of chlorophyllin and light. We also evaluated the use of co-substrates by MtLPMO9A, revealing that the enzyme can use both hydrogen peroxide (H2O2) and molecular oxygen (O2) as co-substrates for cellulose catalytic oxidation.Ana Gabriela SepulchroVanessa PellegriniLucas DiasMarco KadowakiDavid CannellaIgor PolikarpovGreen Wave Publishing of Canadaarticlelytic polysaccharide monooxygenaseschlorophyllinlightco-substrates utilizationFuelTP315-360Energy industries. Energy policy. Fuel tradeHD9502-9502.5ENBiofuel Research Journal, Vol 8, Iss 3, Pp 1454-1464 (2021)
institution	DOAJ
collection	DOAJ
language	EN
topic	lytic polysaccharide monooxygenases chlorophyllin light co-substrates utilization Fuel TP315-360 Energy industries. Energy policy. Fuel trade HD9502-9502.5
spellingShingle	lytic polysaccharide monooxygenases chlorophyllin light co-substrates utilization Fuel TP315-360 Energy industries. Energy policy. Fuel trade HD9502-9502.5 Ana Gabriela Sepulchro Vanessa Pellegrini Lucas Dias Marco Kadowaki David Cannella Igor Polikarpov Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
description	Cost-efficient plant biomass conversion using biochemical and/or chemical routes is essential for transitioning to sustainable chemical technologies and renewable biofuels. Lytic polysaccharide monooxygenases (LPMOs) are copper-dependent enzymes that make part of modern hydrolytic cocktails destined for plant biomass degradation. Here, we characterized MtLPMO9A from Thermothelomyces thermophilus M77 (formerly Myceliophthora thermophila) and demonstrated that it could be efficiently driven by chlorophyllin excited by light in the presence of a reductant agent. However, in the absence of chemical reductant, chlorophyllin and light alone do not lead to a significant release of the reaction products by the LPMO, indicating a low capacity of MtLPMO9A reduction (either via direct electron transfer or via superoxide ion, O2•-). We showed that photocatalysis could significantly increase the LPMO activity against highly crystalline and recalcitrant cellulosic substrates, which are poorly degraded in the absence of chlorophyllin and light. We also evaluated the use of co-substrates by MtLPMO9A, revealing that the enzyme can use both hydrogen peroxide (H2O2) and molecular oxygen (O2) as co-substrates for cellulose catalytic oxidation.
format	article
author	Ana Gabriela Sepulchro Vanessa Pellegrini Lucas Dias Marco Kadowaki David Cannella Igor Polikarpov
author_facet	Ana Gabriela Sepulchro Vanessa Pellegrini Lucas Dias Marco Kadowaki David Cannella Igor Polikarpov
author_sort	Ana Gabriela Sepulchro
title	Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
title_short	Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
title_full	Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
title_fullStr	Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
title_full_unstemmed	Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A
title_sort	combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase mtlpmo9a
publisher	Green Wave Publishing of Canada
publishDate	2021
url	https://doaj.org/article/079764d604a44a068fe5b8e9ca04bfc1
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Combining pieces: a thorough analysis of light activation boosting power and co-substrate preferences for the catalytic efficiency of lytic polysaccharide monooxygenase MtLPMO9A

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