ArticleMolecules (Basel, Switzerland)2015
Exploring the Oxidation of Lignin-Derived Phenols by a Library of Laccase Mutants.
Article in Molecules (Basel, Switzerland), 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 20 citations in OpenAlex.
- Improving the Properties of Laccase Through Heterologous Expression and Protein Engineering.Microorganisms · 2025Review
- Synthesis and application of a phenazine class substrate for high-throughput screening of laccase activity.Applied microbiology and biotechnology · 2024Article
- Recent Theoretical Insights into the Oxidative Degradation of Biopolymers and Plastics by Metalloenzymes.International journal of molecular sciences · 2023Review
- Multicopper oxidases with laccase-ferroxidase activity: Classification and study of ferroxidase activity determinants in a member fromComputational and structural biotechnology journal · 2023Article
- Depolymerization of biorefinery lignin by improved laccases of the white-rot fungus Obba rivulosa.Microbial biotechnology · 2021Article
- Evolved Fusarium oxysporum laccase expressed in Saccharomyces cerevisiae.Scientific reports · 2020Article
- Laccases: structure, function, and potential application in water bioremediation.Microbial cell factories · 2019Review
- A highly stable laccase obtained by swapping the second cupredoxin domain.Scientific reports · 2018Article
- Laccase-mediator system produced by3 Biotech · 2018Article
- High-Throughput Screening Assay for Laccase Engineering toward Lignosulfonate Valorization.International journal of molecular sciences · 2017Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Saturation mutagenesis was performed over six residues delimiting the substrate binding pocket of a fungal laccase previously engineered in the lab. Mutant libraries were screened using sinapic acid as a model substrate, and those mutants presenting increased activity were selected for exploring the oxidation of lignin-derived phenols. The latter comprised a battery of phenolic compounds of interest due to their use as redox mediators or precursors of added-value products and their biological activity. The new laccase variants were investigated in a multi-screening assay and the structural determinants, at both the substrate and the protein level, for the oxidation of the different phenols are discussed. Laccase activity greatly varied only by changing one or two residues of the enzyme pocket. Our results suggest that once the redox potential threshold is surpassed, the contribution of the residues of the enzymatic pocket for substrate recognition and binding strongly influence the overall rate of the catalytic reaction.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.