Pablo Aza

ORCID: 0000-0002-8703-8399
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Research Areas
  • Enzyme-mediated dye degradation
  • Microbial Metabolism and Applications
  • Electrochemical sensors and biosensors
  • melanin and skin pigmentation
  • Biotin and Related Studies
  • Fungal and yeast genetics research
  • Lignin and Wood Chemistry
  • Chromium effects and bioremediation
  • Dye analysis and toxicity
  • Fungal Biology and Applications
  • Electrochemical Analysis and Applications
  • Conducting polymers and applications
  • Mycorrhizal Fungi and Plant Interactions

Centro de Investigaciones Biológicas Margarita Salas
2016-2025

Consejo Superior de Investigaciones Científicas
2023-2025

Multicopper oxidases (MCOs) share a common catalytic mechanism of activation by oxygen and cupredoxin-like folding, along with some structural determinants. Laccases constitute the largest group MCOs, fungal laccases having greatest biotechnological applicability due to their superior ability oxidize wide range aromatic compounds lignin, which is enhanced in presence redox mediators. The adaptation these versatile enzymes specific application processes can be achieved through directed...

10.3390/biom13121716 article EN cc-by Biomolecules 2023-11-28

From laccase design to application of the overexpressed biocatalyst in an industrial environment for eco-friendly synthesis polyaniline and dyes.

10.1039/c9gc02475a article EN cc-by-nc Green Chemistry 2019-01-01

Laccases secreted by saprotrophic basidiomycete fungi are versatile biocatalysts able to oxidize a wide range of aromatic compounds using oxygen as the sole requirement. Saccharomyces cerevisiae is preferred host for engineering fungal laccases. To assist difficult secretion active enzymes yeast, native signal peptide usually replaced preproleader S. alfa mating factor (MFα1). However, in most cases, only basal enzyme levels obtained. During directed evolution laccases fused α-factor...

10.3390/ijms22031157 article EN International Journal of Molecular Sciences 2021-01-25

Abstract Saccharomyces cerevisiae plays an important role in the heterologous expression of array proteins due to its easy manipulation, low requirements and ability for protein post-translational modifications. The implementation preproleader secretion signal α-factor mating pheromone from this yeast contributes increase production yields by targeting foreign extracellular environment. use peptide combined with enzyme-directed evolution allowed us achieve otherwise difficult functional...

10.1007/s00018-021-03793-y article EN cc-by Cellular and Molecular Life Sciences 2021-03-09

Multicopper oxidases (MCOs) comprise different types of enzymes widely distributed in nature with quite diverse functions. Laccases are the most interesting MCOs from a biotechnological point view, particularly those secreted by ligninolytic Basidiomycota fungi due to their versatility oxidize lignin and variety aromatic substrates. The term "laccase" has been broadly (but sometimes erroneously) applied low sequence homology some overlapping activities other MCO groups. We examined...

10.1016/j.ympev.2025.108310 article EN cc-by Molecular Phylogenetics and Evolution 2025-02-01

Polyaniline is a conductive polymer with distinctive optical and electrical properties. Its enzymatic synthesis an environmentally friendly alternative to the use of harsh oxidants extremely acidic conditions. 7D5L, high-redox potential laccase developed in our lab, biocatalyst choice for green polyaniline (emeraldine salt) due its superior ability oxidize aniline kinetic stability at required polymerization conditions (pH 3 presence anionic surfactants) as compared other fungal laccases....

10.1371/journal.pone.0164958 article EN cc-by PLoS ONE 2016-10-14

The robustness of a high-redox potential laccase has been enhanced by swapping its second cupredoxin domain with that from another fungal laccase, which introduced pool neutral mutations in the protein sequence without affecting enzyme functionality. new showed outstanding stability to temperature, pH (2-9) and organic solvents, while maintaining ability oxidize substrates. By engineering signal peptide, secretion levels Saccharomyces cerevisiae were increased, allowed purify engineered for...

10.1038/s41598-018-34008-3 article EN cc-by Scientific Reports 2018-10-17

Multi-copper oxidases (MCO) share a common molecular architecture and the use of copper ions as cofactors to reduce O2 H2O, but show high sequence heterogeneity functional diversity. Many new emerging MCO genes are wrongly annotated laccases, largest group MCOs, with widest range biotechnological applications (particularly those from basidiomycete fungi) due their ability oxidise aromatic compounds lignin. Thus, comprehensive studies for better classification structure-function...

10.1016/j.csbj.2023.01.030 article EN cc-by-nc-nd Computational and Structural Biotechnology Journal 2023-01-01

During the kraft process to obtain cellulosic pulp from wood, most of lignin is removed by high-temperature alkaline cooking, released in black liquors and usually incinerated for energy. However, lignins are a valuable source phenolic compounds that can be valorized new bio-based products. The aim this work develop laccases capable working under extreme conditions high temperature pH, typical industrial conversion wood into fibreboard, order provide extremophilic biocatalysts depolymerising...

10.1186/s13068-022-02247-2 article EN cc-by Biotechnology for Biofuels and Bioproducts 2022-12-29

Agaricomycetes fungi responsible for decay of wood and other lignocellulosic substrates constitute a valuable source lignin-degrading enzymes. Among these enzymes, laccases (multi-copper oxidases) present remarkable biotechnological potential as environmentally friendly biocatalysts able to oxidize wide range aromatic compounds using oxygen the only requirement. Laccases from saprotrophic Agaricales species have been much less studied than Polyporales, despite fact that former are excellent...

10.3390/jof7050359 article EN cc-by Journal of Fungi 2021-05-04

Abstract Unlike laccases sensu stricto, which are usually monomeric enzymes, laccase‐like enzymes recently re‐classified as Novel Laccases (NLACs) characterized by the formation of heterodimers with small proteins (subunits) unknown function. Here NLAC from Pleurotus eryngii (PeNL) and a protein selected fungal genome, that is homologous to reported POXA3 ostreatus, were produced in Aspergillus oryzae separately or together. The two interacted regardless whether subunit was co‐expressed...

10.1002/pro.4734 article EN cc-by-nc Protein Science 2023-07-23
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