ArticleMolecules (Basel, Switzerland)2018
Optimization of Transesterification Reactions with CLEA-Immobilized Feruloyl Esterases from
Article in Molecules (Basel, Switzerland), 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed, 16 citations in OpenAlex.
- Genomic Sequence Resource ofJournal of fungi (Basel, Switzerland) · 2023Article
- The Inhibitory Potential of Ferulic Acid Derivatives against the SARS-CoV-2 Main Protease: Molecular Docking, Molecular Dynamics, and ADMET Evaluation.Biomedicines · 2022Article
- Ferulic Acid From Plant Biomass: A Phytochemical With Promising Antiviral Properties.Frontiers in nutrition · 2021Review
- Crosslinked Enzyme Aggregates (CLEAs) of Laccases fromMolecules (Basel, Switzerland) · 2020Article
- Optimization of Transesterification Reactions with CLEA-Immobilized Feruloyl Esterases fromMolecules (Basel, Switzerland) · 2018Article
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
Abstract
Feruloyl esterases (FAEs, E.C. 3.1.1.73) are biotechnologically important enzymes with several applications in ferulic acid production from biomass, but also in synthesis of hydroxycinnamic acid derivatives. The use of such biocatalysts in commercial processes can become feasible by their immobilization, providing the advantages of isolation and recycling. In this work, eight feruloyl esterases, immobilized in cross-linked enzyme aggregates (CLEAs) were tested in regard to their transesterification performance, towards the production of prenyl ferulate (PFA) and arabinose ferulate (AFA). After solvent screening, comparison with the activity of respective soluble enzymes, and operational stability tests, FAE125 was selected as the most promising biocatalyst. A central composite design revealed the optimum conditions for each transesterification product, in terms of water content, time, and substrate ratio for both products, and temperature and enzyme load additionally for prenyl ferulate. The optimum product yields obtained were 83.7% for PFA and 58.1% for AFA. FAE125 CLEAs are stable in the optimum conditions of transesterification reactions, maintaining 70% residual activity after five consecutive reactions. Overall, FAE125 CLEAs seem to be able to perform as a robust biocatalyst, offering satisfactory yields and stability, and thus showing significant potential for industrial applications.
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