Hybrid QM/MM simulations of feruloyl esterases: cleavage mechanism of lignin-carbohydrate complexes in plant cell walls

• Grant number: 16/22956-7
• Support Opportunities: Scholarships abroad - Research Internship - Post-doctor
• Start date: February 01, 2017
• End date: January 31, 2018
• Field of knowledge: Physical Sciences and Mathematics - Chemistry - Physical-Chemistry
• Principal Investigator: Munir Salomao Skaf
• Grantee: Rodrigo Leandro Silveira
• Supervisor: Gregg Beckham
• Host Institution: Instituto de Química (IQ). Universidade Estadual de Campinas (UNICAMP). Campinas , SP, Brazil
• Institution abroad: National Renewable Energy Laboratory (NREL), United States
• Associated to the scholarship: 14/10448-1 - Molecular aspects of plant cell wall architecture, BP.PD

Abstract

Lignocellulosic biomass constitutes an enormous source of biopolymers that can be used for producing biofuels and valuable chemicals. Due to the plant cell walls' natural resistance against degradation (recalcitrance), enzymatic cocktails currently employed to depolymerize its components are not effective on broad-scale applications. Lignin-carbohydrate complexes (LCC) - covalent links between hemicellulose and lignin - are major contributors to lignocellulosic biomass recalcitrance. The presence of LCCs in biomass severely decreases its digestibility. Feruloyl esterases (FAE), secreted by cellulolytic fungi, cleave LCC ester bonds and release lignin from the hemicellulose. FAEs act as accessory enzymes, which, by disrupting LCCs, help glycoside hydrolases and oxidative enzymes to get in contact with their target substrates, leading to enhanced biomass degradation. Here, we propose to apply modern hybrid QM/MM (quantum mechanics/molecular mechanics) computer simulation techniques to elucidate the enzymatic mechanism of FAEs on LCCs. The proposed studies will help constructing a rational basis for enzyme engineering aimed at enhancing biomass conversion rates. The project will be conducted at the National Renewable Energy Laboratory/USA (NREL), whose outstanding team of researchers has long been making efforts to fully understand mechanisms of cell wall active enzymes by means of state-of-the-art computational chemistry techniques. Currently, there is already ongoing collaboration between our group at Unicamp and NREL, and we aim to further strengthen joint efforts towards elucidating molecular aspects of biomass conversion in the ambit of the Center for Computational Engineering & Sciences (CEPID, 2013/08293-7). (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)

MALLINSON, SAM J. B.; MACHOVINA, MELODIE M.; SILVEIRA, RODRIGO L.; GARCIA-BORRAS, MARC; GALLUP, NATHAN; JOHNSON, CHRISTOPHER W.; ALLEN, MARK D.; SKAF, MUNIR S.; CROWLEY, MICHAEL F.; NEIDLE, ELLEN L.; et al. A promiscuous cytochrome P450 aromatic O-demethylase for lignin bioconversion. NATURE COMMUNICATIONS, v. 9, JUN 27 2018. (13/08293-7, 14/10448-1, 16/22956-7)

SILVEIRA, RODRIGO L.; KNOTT, BRANDON C.; PEREIRA, CAROLINE S.; CROWLEY, MICHAEL F.; SKAF, MUNIR S.; BECKHAM, GREGG T.. Transition Path Sampling Study of the Feruloyl Esterase Mechanism. Journal of Physical Chemistry B, v. 125, n. 8, p. 2018-2030, MAR 4 2021. (15/25031-1, 17/01151-3, 16/22956-7, 13/08293-7, 14/10448-1)

AUSTIN, HARRY P.; ALLEN, MARK D.; DONOHOE, BRYON S.; RORRER, NICHOLAS A.; KEARNS, FIONA L.; SILVEIRA, RODRIGO L.; POLLARD, BENJAMIN C.; DOMINICK, GRAHAM; DUMAN, RAMONA; EL OMARI, KAMEL; et al. Characterization and engineering of a plastic-degrading aromatic polyesterase. PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, v. 115, n. 19, p. E4350-E4357, MAY 8 2018. (13/08293-7, 14/10448-1, 16/22956-7)