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

Autor(es)

Sepulchro, V, Ana Gabriela ; Pellegrini, Vanessa O. A. ^[1] ; Dias, Lucas D. ^[1] ; Kadowaki, Marco A. S. ^{[2, 3, 4]} ; Cannella, David ^{[2, 3, 4]} ; Polikarpov, Igor ^[1]

Afiliação do(s) autor(es)

^[1] Sepulchro, Ana Gabriela, V, Univ Sao Paulo, Inst Fis Sao Carlos, Ave Trabalhador Sao Carlense 400, BR-13566590 Sao Carlos, SP - Brazil

^[2] Univ Libre Bruxelles, Intetfac Sch Bioengineers, PhotoBioCatalysis Unit, BioCat Dept, Campus Plaine, Acc 2, CP 245, B-1050 Brussels - Belgium

^[3] Univ Libre Bruxelles, Intetfac Sch Bioengineers, PhotoBioCatalysis Unit, CPBL Dept, Campus Plaine, Acc 2, CP 245, B-1050 Brussels - Belgium

^[4] Univ Libre Bruxelles, Intetfac Sch Bioengineers, PhotoBioCatalysis Unit, BTL Dept, Campus Plaine, Acc 2, CP 245, B-1050 Brussels - Belgium

• Tipo de documento: Artigo Científico
• Fonte: BIOFUEL RESEARCH JOURNAL-BRJ; v. 8, n. 3, p. 1454-1464, SUM 2021.
• Citações Web of Science: 0

Resumo

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, O-2(center dot-)). 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 (O-2) as co-substrates for cellulose catalytic oxidation. (C) 2021 BRTeam. All rights reserved. (AU)

• Processo FAPESP: 18/22300-0 - Aumento da oxidação enzimática de lignocelulose através de atividades sinérgicas usando luz e LPMOs
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Regular
• Processo FAPESP: 15/13684-0 - Estudos estruturais e funcionais de enzimas que participam na síntese e degradação de carboidratos complexos
• Beneficiário: Igor Polikarpov
• Modalidade de apoio: Auxílio à Pesquisa - Temático
• Processo FAPESP: 19/13569-8 - Estudo dos Mecanismos de Ação em Terapia Fotodinâmica: Do Fotossensibilizador à Aplicação Prática
• Beneficiário: Lucas Danilo Dias
• Modalidade de apoio: Bolsas no Brasil - Pós-Doutorado