Scholarship 24/12476-4 - Biologia computacional, Biomassa - BV FAPESP
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Exploring the interaction between Lytic Polysaccharide Monooxygenases and Cellobiose Dehydrogenase as their redox agent

Grant number: 24/12476-4
Support Opportunities:Scholarships abroad - Research Internship - Doctorate (Direct)
Start date until: October 01, 2024
End date until: February 28, 2025
Field of knowledge:Biological Sciences - Biochemistry - Molecular Biology
Principal Investigator:Fernando Segato
Grantee:Martha Inés Vélez Mercado
Supervisor: Sam Hay
Host Institution: Escola de Engenharia de Lorena (EEL). Universidade de São Paulo (USP). Lorena , SP, Brazil
Institution abroad: University of Manchester, England  
Associated to the scholarship:22/04713-0 - Exploring the interaction between lytic polysaccharide monooxygenases and its redox partner cellobiose dehydrogenases, BP.DD

Abstract

In recent years, oxidative proteins known as lytic polysaccharide monooxygenases (LPMOs) have been discovered, which act directly on crystalline cellulose. The incorporation of LPMOs into commercial enzyme cocktails has substantially enhanced their performance. Moreover, LPMOs have been the subject of numerous studies focusing on their mode of action, substrate interactions, and electron donors, including the enzyme cellobiose dehydrogenase (CDH). In the preliminary analyses from the current PhD project, different monooxygenase activity of MtAA9s was observed when CDH was added as electron donor. Additionally, our previous results obtained in collaboration with Prof. Sam Hay (during FAPESP SPRINT, 2022/00539-6) indicate that redox potential of LPMOs is pH-dependent. In this research proposal (BEPE), the interaction between LPMOs and CDH will be assessed using molecular dynamics simulations and Förster resonance energy transfer (FRET), as well as electrochemical analysis of LPMOs to better understand LPMOs electron transfer. We will use recombinant LPMOs from Thermothelomyces thermophilus (MtAA9E, MtAA9H, MtAA9J, MtAA9W and MtAA16B) and the recombinant MtCDHB, also from T. thermophilus. The purified LPMOs will be characterized in presence of MtCDHB to elucidate the different interactions between them. These assays will provide information about the interaction between LPMOs and CDH, which will help to identify patterns of LPMOs that can interact with CDH and outline strategies to improve the interaction between both enzymes.

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