Fernándo López-Gallego

ORCID: 0000-0003-0031-1880
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About
Contact & Profiles
Research Areas
  • Enzyme Catalysis and Immobilization
  • Microbial Metabolic Engineering and Bioproduction
  • Electrochemical sensors and biosensors
  • Protein purification and stability
  • Chemical Synthesis and Analysis
  • Amino Acid Enzymes and Metabolism
  • Innovative Microfluidic and Catalytic Techniques Innovation
  • Biochemical and Molecular Research
  • Click Chemistry and Applications
  • Enzyme Structure and Function
  • Enzyme Production and Characterization
  • Monoclonal and Polyclonal Antibodies Research
  • Microbial Natural Products and Biosynthesis
  • Polymer Surface Interaction Studies
  • Biofuel production and bioconversion
  • Biotin and Related Studies
  • Glycosylation and Glycoproteins Research
  • Carbohydrate Chemistry and Synthesis
  • Plant biochemistry and biosynthesis
  • Peptidase Inhibition and Analysis
  • Microfluidic and Capillary Electrophoresis Applications
  • Catalysis for Biomass Conversion
  • Pancreatic function and diabetes
  • biodegradable polymer synthesis and properties
  • Advanced biosensing and bioanalysis techniques

CIC biomaGUNE
2016-2025

Ikerbasque
2016-2025

University of Copenhagen
2025

Université Paris-Saclay
2024

Thales (France)
2024

Centre National de la Recherche Scientifique
2024

University of Bern
2023-2024

Universidad de Zaragoza
2018-2023

Instituto de Síntesis Química y Catálisis Homogénea
2018-2021

Centro Médico Sanitas Zaragoza
2020-2021

Enzyme cofactors play a major role in biocatalysis, as many enzymes require them to catalyze highly valuable reactions organic synthesis. However, the cofactor recycling is often hurdle implement at industrial level. The fabrication of heterogeneous biocatalysts co-immobilizing phosphorylated (PLP, FAD+ , and NAD+ ) onto same solid material reported perform chemical without exogeneous addition aqueous media. In these self-sufficient biocatalysts, immobilized are catalytically active...

10.1002/anie.201609758 article EN cc-by Angewandte Chemie International Edition 2016-12-21

Biocatalysis is a key technology enabling plastic recycling. However, despite advances done in the development of plastic-degrading enzymes, molecular mechanisms that govern their catalytic performance are poorly understood, hampering engineering more efficient enzyme-based technologies. In this work, we study hydrolysis PET-derived diesters and PET trimers catalyzed by highly promiscuous lipase B from Candida antarctica (CALB) through QM/MM dynamics simulations supported experimental...

10.1038/s41467-023-39201-1 article EN cc-by Nature Communications 2023-06-15

The properties of a new commercially available amino-epoxy support (amino-epoxy-Sepabeads) for immobilizing enzymes have been compared to those conventional epoxy supports. has layer groups over ethylenediamine that is covalently bound the support. Thus, this great anionic exchanger power and high number groups. We found advantages heterofunctional Immobilization proceeds at low ionic strength using amino Sepabeads while requiring monofunctional much more rapid supports than employing...

10.1021/bm0257661 article EN Biomacromolecules 2003-04-10

Summary Fungi are a rich source of bioactive secondary metabolites, and mushroom‐forming fungi ( Agaricomycetes ) especially known for the synthesis numerous often cytotoxic sesquiterpenoid metabolites. Compared with large number sesquiterpene synthases identified in plants, less than handful unique have been described from fungi. Here we describe functional characterization six (Cop1 to Cop6) two terpene‐oxidizing cytochrome P450 monooxygenases (Cox1 Cox2) Coprinus cinereus. The genes were...

10.1111/j.1365-2958.2009.06717.x article EN Molecular Microbiology 2009-04-28

Abstract In bio‐redox cascade reactions that are immobilized on porous supports, mass‐transfer limitations may impede the effective concentration of cofactor around corresponding dehydrogenases. This main drawback has been addressed by co‐immobilization both and recycling Herein, we report tailor‐made procedures to assemble three different orthogonal cascades in vitro (two selective reductions one oxidation) with situ cofactor‐regeneration. However, itself does not guarantee success...

10.1002/cctc.201200146 article EN ChemCatChem 2012-06-15

We expanded the application of self-sufficient heterogeneous biocatalysts containing coimmobilized ω-transaminases and pyridoxal 5′-phosphate (PLP) to efficiently operate packed-bed reactors in continuous flow. Using a ω-transaminase from Halomonas elongata with PLP onto porous methacrylate-based carriers coated polyethylenimine, we operated reactor continuously for up 50 column volumes at 1.45 mL × min–1 enantioselective deamination model amines (α-methylbenzyl amine), yielding >90%...

10.1021/acssuschemeng.8b02672 article EN ACS Sustainable Chemistry & Engineering 2018-08-26

Multi-enzymatic cascades with enzymes arranged in close-proximity through a protein scaffold can trigger substrate channeling effect, allowing for efficient cofactor reuse industrial potential. However, precise nanometric organization of challenges the design scaffolds. In this study, we create nanometrically organized multi-enzymatic system exploiting engineered Tetrapeptide Repeat Affinity Proteins (TRAPs) as scaffolding biocatalysis. We genetically fuse TRAP domains and program them to...

10.1038/s41467-023-38304-z article EN cc-by Nature Communications 2023-05-04

ABSTRACT Cyanobacteria are a rich source of natural products and known to produce terpenoids. These bacteria the major musty-smelling terpenes geosmin 2-methylisoborneol, which found in many water supplies; however, no terpene synthases have been characterized from these organisms date. Here, we describe characterization three sesquiterpene identified Nostoc sp. strain PCC 7120 (terpene synthase NS1) punctiforme 73102 NP1 NP2). The second N. (NP2) is homologous fusion-type Streptomyces spp....

10.1128/jb.00759-08 article EN Journal of Bacteriology 2008-07-26

In this paper, the stabilization of a lipase from Bacillus thermocatenulatus (BTL2) by new strategy is described. First, selectively adsorbed on hydrophobic supports. Second, carboxylic residues enzyme are modified with ethylenediamine, generating having 4-fold more amino groups than native enzyme. The chemical amination did not present significant effect activity and only reduced half-life 3−4-fold factor in inactivations promoted heat or organic solvents. Next, aminated purified desorbed...

10.1021/bm800609g article EN Biomacromolecules 2008-08-15

Abstract Sesquiterpene synthases catalyze with different catalytic fidelity the cyclization of farnesyl pyrophosphate (FPP) into hundreds known compounds diverse structures and stereochemistries. Two sesquiterpene synthases, Cop4 Cop6, were previously isolated from Coprinus cinereus as part a fungal genome survey. This study investigates reaction mechanism two enzymes. Cyclization all‐ trans ‐FPP (( E , ) ‐ FPP) was compared to cis – isomer FPP Z )‐FPP) surrogate for secondary cisoid neryl...

10.1002/cbic.200900671 article EN ChemBioChem 2010-04-23

Recent advances in bioorthogonal catalysis promise to deliver new chemical tools for performing chemoselective transformations complex biological environments. Herein, we report how FAD (flavin adenine dinucleotide), FMN mononucleotide), and four flavoproteins act as unconventional photocatalysts capable of converting PtIV RuII complexes into potentially toxic PtII or -OH2 species. In the presence electron donors low doses visible light, mini singlet oxygen generator (miniSOG) NADH oxidase...

10.1002/anie.201800288 article EN cc-by-nc-nd Angewandte Chemie International Edition 2018-01-23

Riboflavin acts as bioorthogonal photocatalyst to activate a Pt<sup>IV</sup> anticancer prodrug in the biological environment.

10.1039/c7sc01109a article EN cc-by-nc Chemical Science 2017-01-01
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