Exploring the interaction between lytic polysaccharide monooxygenases and its redox partner cellobiose dehydrogenases

• Grant number: 22/04713-0
• Support Opportunities: Scholarships in Brazil - Doctorate (Direct)
• Start date: June 01, 2022
• Status: Discontinued
• Field of knowledge: Biological Sciences - Genetics - Molecular Genetics and Genetics of Microorganisms
• Principal Investigator: Fernando Segato
• Grantee: Martha Inés Vélez Mercado
• Host Institution: Escola de Engenharia de Lorena (EEL). Universidade de São Paulo (USP). Lorena , SP, Brazil
• Associated research grant: 21/06679-1 - Enzymatic oxidation of sugarcane bagasse 2: exploring the interaction between LPMOs and its redox partner CDHs aiming for the development of more efficient enzymes for insertion into an engineered cell factory, AP.BIOEN.JP2
• Associated scholarship(s): 24/16094-9 - Assessment of the impact of reducing agent types on electron transfer and enzymatic activity of lytic polysaccharide monooxygenases (LPMOs) from Thermothelomyces thermophilus, BE.EP.DD 24/12476-4 - Exploring the interaction between Lytic Polysaccharide Monooxygenases and Cellobiose Dehydrogenase as their redox agent, BE.EP.DD

Abstract

Lignocellulose is an abundant source of polysaccharides that can be used as a renewable raw material for the production of biofuels and other compounds of interest. The conversion of lignocellulose into its subunits is a slow and costly process, therefore, more study is needed to make this process feasible. Until recently, the available enzymatic cocktails were composed of hydrolytic enzymes that act on the cellulose components of lignocellulose. These enzymes cocktails are low and inefficient. In recent years, oxidative proteins have been discovered that act directly on crystalline cellulose have been described, and are named LPMOs. Since the discovery, LPMOs have been added to the commercial cocktails improving their performance, as well as, have been the focus of many studies related to their mode of action, interaction with substrate and electron donors including the enzyme CDH. Through the analysis of amino acid sequence of LPMOs from different filamentous fungi an extra-region was found to the structure described so far. Previous molecular docking analysis of the interaction between CDHs and LPMOs provided evidenced that these extra-regions serve to anchor location of the CDH for electron transfer pathway. Since we have been developing a filamentous fungus for the enzymes production the current proposal aim to understanding the coupling mechanism between CDH and LPMO, as well as describing the electron transfer pathway to the copper active site. (AU)

Scientific publications

(References retrieved automatically from Web of Science and SciELO through information on FAPESP grants and their corresponding numbers as mentioned in the publications by the authors)

BARRIOS-GUTIERREZ, SOLANGE GRACE; VELEZ-MERCADO, MARTHA INES; ORTEGA, JULIA RODRIGUES; LIMA, AWANA DA SILVA; SARAIVA, ANA LUIZA DA ROCHA FORTES; BERTO, GABRIELA LEILA; SEGATO, FERNANDO. Oxidative Machinery of basidiomycetes as potential enhancers in lignocellulosic biorefineries: A lytic polysaccharide monooxygenases approach. Bioresource Technology, v. 386, p. 11-pg., 2023-10-01. (22/00539-6, 22/04227-9, 14/18714-2, 19/22284-7, 22/04713-0, 21/06679-1)