Gustavo Avelar Molina

ORCID: 0000-0002-4301-9049
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About
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Research Areas
  • Biofuel production and bioconversion
  • Enzyme Catalysis and Immobilization
  • Protein Structure and Dynamics
  • Microbial Metabolic Engineering and Bioproduction
  • Enzyme Structure and Function
  • Botany and Geology in Latin America and Caribbean
  • Advanced Cellulose Research Studies
  • Enzyme Production and Characterization
  • Mosquito-borne diseases and control
  • Enzyme-mediated dye degradation
  • Phytoplasmas and Hemiptera pathogens

Novo Nordisk Foundation
2022-2024

Technical University of Denmark
2020-2024

Universidade de São Paulo
2024

Universidade de Ribeirão Preto
2024

Abstract Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions interfacial enzyme catalysis remain sparse, this is partly due to a shortage coherent experimental data guide assess such work. In work, we produced kinetically characterized 83 cellulases, which revealed conspicuous linear free energy relationship (LFER) between substrate binding strength activation barrier. The scaling occurred...

10.1038/s41467-021-24075-y article EN cc-by Nature Communications 2021-06-22

Deposition of enzyme sequences greatly outruns any possibility thorough experimental characterization. There seems to be a particular shortage quantitative kinetic data, and this limits both structure–function analyses the selection biocatalysts for technical use. In study, we present virtual screening approach, which takes advantage empirical scaling relations interfacial enzymes in order predict parameters from sequences. As an example, analyzed industrially important group enzymes,...

10.1021/acscatal.2c02305 article EN ACS Catalysis 2022-06-08

Xylanases are of significant interest for biomass conversion technologies. Here, we investigated the allosteric regulation xylan hydrolysis by Bacillus subtilis GH11 endoxylanase. Molecular dynamics simulations (MDS) in presence xylobiose identified binding to active site and two potential secondary sites (SBS) around surface residues Asn54 Asn151. Arabinoxylan titration experiments with single cysteine mutants N54C N151C labeled thiol‐reactive fluorophore acrylodan or ESR spin‐label MTSSL...

10.1002/1873-3468.14799 article EN FEBS Letters 2024-01-22

While heterogeneous enzyme reactions play an essential role in both nature and green industries, computational predictions of their catalytic properties remain scarce. Recent experimental work demonstrated the applicability Sabatier principle for biocatalysis. This provides a simple relationship between binding strength rate potentially opens new way inexpensive determination kinetic parameters. However, broader implementation this approach will require fast reliable prediction free energies...

10.1021/acsomega.0c05361 article EN cc-by-nc-nd ACS Omega 2021-01-06

Enzymatic degradation of cellulosic biomass is a well-established route for the sustainable production biofuels, chemicals, and materials. A strategy employed by nature industry to achieve an efficient cellulose that cellobiohydrolases (or exocellulases), such as Cel7A, work synergistically with endoglucanases, Cel7B, complete cellulose. However, mechanistic understanding this exo–endo synergy still lacking. Here, we used single-molecule fluorescence microscopy quantify binding kinetics...

10.1021/acs.jpcb.3c05697 article EN cc-by The Journal of Physical Chemistry B 2024-01-16

Abstract Structural polysaccharides are difficult to degrade due their crystalline structure. Hence, industrial conversion of biomass has focused on both substrate pretreatment and enzyme engineering improve the biochemical into fuels chemicals. However, few studies have explored interrelationship between crystallinity cellulase activity. Here, we systematically investigated kinetics structurally diverse cellulases five cellulosic substrates with varying crystallinity. Regardless structure...

10.1101/2024.08.20.607150 preprint EN cc-by bioRxiv (Cold Spring Harbor Laboratory) 2024-08-20

Abstract Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions interfacial enzyme catalysis remain sparse, this is partly due to a shortage coherent experimental data guide assess such work. We have produced kinetically characterized 83 cellulases, which revealed conspicuous linear free energy relationship (LFER) between strength substrate binding activation barrier. This common scaling occurred...

10.1101/2020.05.20.105569 preprint EN bioRxiv (Cold Spring Harbor Laboratory) 2020-05-23
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