ArticleApplied biochemistry and biotechnology2022
Immobilization of Eversa Lipases on Hydrophobic Supports for Ethanolysis of Sunflower Oil Solvent-Free.
Article in Applied biochemistry and biotechnology, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 29 citations in OpenAlex.
- Enzymatic Synthesis of Aroma Ester Catalyzed by Lipases Immobilized on Activated Carbon Derived from Fermented Cocoa Bean Shells.ACS omega · 2026Article
- A Review of Guerbet Alcohols and Their Esters: Synthesis, Applications, and Future Perspectives.Materials (Basel, Switzerland) · 2025Review
- Understanding the Enzymatic Synthesis of a New Biolubricant: Decane-1,10-diyl bis(2-methylpentanoate).Molecules (Basel, Switzerland) · 2024Article
- Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles.Langmuir : the ACS journal of surfaces and colloids · 2024Article
- Hydrolysis of Casein by Pepsin Immobilized on Heterofunctional Supports to Produce Antioxidant Peptides.Applied biochemistry and biotechnology · 2024Article
- A Lipase Gene ofInternational journal of molecular sciences · 2024Article
- Adsorption of extracellular lipase in a packed-bed reactor: an alternative immobilization approach.Bioprocess and biosystems engineering · 2024Article
- Solvent-Free Enzymatic Synthesis of Dietary Triacylglycerols from Cottonseed Oil in a Fluidized Bed Reactor.Molecules (Basel, Switzerland) · 2023Article
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Authors and funding
6 authors at 3 institutions in 2 countries.
Funding
Abstract
Lipases are an important group of biocatalysts for many industrial applications. Two new commercial low-cost lipases Eversa® Transform and Eversa® Transform 2.0 was immobilized on four different hydrophobic supports: Lewatit-DVB, Purolite-DVB, Sepabeads-C18, and Purolite-C18. The performance of immobilized lipases was investigated in the transesterification of sunflower oil solvent-free in an anhydrous medium. Interesting results were obtained for both lipases and the four supports, but with Sepabeads support the lipases Eversa showed high catalytic activity. However, the more stable and efficient derivative was Eversa® Transform immobilized on Sepabeads C-18. A 98 wt% of ethyl ester of fatty acid (FAEE) was obtained, in 3 h at 40ºC, ethanol/sunflower oil molar ratio of 3:1 and a 10 wt% of the immobilized biocatalyst. After 6 reaction cycles, the immobilized biocatalyst preserved 70 wt% of activity. Both lipases immobilized in Sepabeads C-18 were highly active and stable in the presence of ethanol. The immobilization of Eversa Transform and Eversa Transform 2.0 in hydrophobic supports described in this study appears to be a promising alternative to the immobilization and application of these news lipases still unexplored.
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