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(Reference retrieved automatically from Web of Science through information on FAPESP grant and its corresponding number as mentioned in the publication by the authors.)

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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Author(s):
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]
Total Authors: 6
Affiliation:
[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
Total Affiliations: 4
Document type: Journal article
Source: BIOFUEL RESEARCH JOURNAL-BRJ; v. 8, n. 3, p. 1454-1464, SUM 2021.
Web of Science Citations: 0
Abstract

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)

FAPESP's process: 18/22300-0 - Synergistic activities to boost enzymatic lignocellulose oxidation using light and LPMOs
Grantee:Igor Polikarpov
Support Opportunities: Regular Research Grants
FAPESP's process: 15/13684-0 - Structural and functional studies of enzymes that participate in complex carbohydrates synthesis and degradation
Grantee:Igor Polikarpov
Support Opportunities: Research Projects - Thematic Grants
FAPESP's process: 19/13569-8 - Study of the Mechanisms of Action in Photodynamic Therapy: From Photosensitizer to Practical Application
Grantee:Lucas Danilo Dias
Support Opportunities: Scholarships in Brazil - Post-Doctoral