ArticleACS sustainable chemistry & engineering2022
Enhancing the Thermostability of Engineered Laccases in Aqueous Betaine-Based Natural Deep Eutectic Solvents.
Article in ACS sustainable chemistry & engineering, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 40 citations in OpenAlex.
- Recent advances in AI-driven deep eutectic solvent design for biocatalysis: Co-design of extremozyme and reaction medium.Biodesign research · 2026Review
- Article
- Laccase-Catalyzed Dimerization of Honokiol and Magnolol for Multitarget Metabolic Enzyme Inhibitors.Chembiochem : a European journal of chemical biology · 2026Article
- Current Status and Future Perspectives of Betaine and Betaine-Based Natural Deep Eutectic Solvents: A Review.Foods (Basel, Switzerland) · 2025Review
- The Versatility of NADES Across Applications.Molecules (Basel, Switzerland) · 2025Review
- Advanced Solubilization of Brazilian Cerrado Byproduct Extracts Using Green Nanostructured Lipid Carriers and NaDESs for Enhanced Antioxidant Potentials.Antioxidants (Basel, Switzerland) · 2025Article
- Deep eutectic solvents assisted laccase pretreatment for improving enzymatic hydrolysis of corn stover.Bioprocess and biosystems engineering · 2025Article
- New Green Biorefinery Strategies to Valorize Bioactive Fractions fromMarine drugs · 2024Article
- Review
- Rational design of deep eutectic solvents for the stabilization of dehydrogenases: an artificial neural network prediction approach.Frontiers in chemistry · 2024Article
- Laccase-catalyzed lignin depolymerization in deep eutectic solvents: challenges and prospects.Bioresources and bioprocessing · 2023Review
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
In recent years, natural deep eutectic solvents (NADESs) have gained increasing attention as promising nontoxic solvents for biotechnological applications, due to their compatibility with enzymes and ability to enhance their activity. Betaine-based NADESs at a concentration of 25 wt % in a buffered aqueous solution were used as media to inhibit thermal inactivation of POXA1b laccase and its five variants when incubated at 70 and 90 °C. All the tested laccases showed higher residual activity when incubated in NADES solutions, with a further enhancement achieved also for the most thermostable variant. Furthermore, the residual activity of laccases in the presence of NADESs showed a clear advantage over the use of NADESs' individual components. Molecular docking simulations were performed to understand the role of NADESs in the stabilization of laccases toward thermal inactivation, evaluating the interaction between each enzyme and NADESs' individual components. A correlation within the binding energies between laccases and NADES components and the stabilization of the enzymes was demonstrated. These findings establish the possibility of preincubating enzymes in NADESs as a facile and cost-effective solution to inhibit thermal inactivation of enzymes when exposed to high temperatures. This computer-aided approach can assist the tailoring of NADES composition for every enzyme of interest.
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Registered trials
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