Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles

This research investigated the usefulness of magnetic iron oxide nanoparticles (Fe<sub>3</sub>O<sub>4</sub>) as a support to immobilize the lipase Eversa Transform 2.0 (ET 2.0) to obtain an active and stable biocatalyst, easily recoverable from the reaction medium for applications in the production of biodiesel. Biodiesel was an alternative fuel composed mainly of fatty acid esters with strong transesterification and esterification capabilities. The study focused on the esterification of oleic acid with ethanol to synthesize ethyl oleate. Magnetic nanoparticles were prepared by coprecipitation, then activated with glutaraldehyde and functionalized with γ-aminopropyltriethoxysilane (APTES). The optimal conditions for immobilizing ET 2.0 were pH 10, 25 mM sodium carbonate buffer, an enzymatic load of 200 U/g, and 1 h of contact time, obtaining 78% yield and enzymatic activity of 205.9 U/g. Postimmobilization evaluation showed that the immobilized enzyme performed better than its free form. Kinetic studies were conducted under these optimized conditions (2-96 h at 150 rpm and 37 °C). The biocatalyst was tested for the synthesis of ethyl oleate using oleic acid as the substrate and ethanol, achieving a conversion of 88.1%. Subsequent recirculation tests maintained approximately 80% conversion until the fourth cycle, confirming the sustainability of ester production. Molecular docking studies revealed that the binding affinity for the enzyme-docked oil composition was estimated at -5.8 kcal/mol, suggesting that the combination of the substrate and lipase was stable and suitable for esterification.

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Publication Details

Journal
Langmuir
Published
2024-11-26
DOI
https://doi.org/10.1021/acs.langmuir.4c02542
Citations
23
Primary Topic
Enzyme Catalysis and Immobilization
Type
article
Field-Weighted Citation Impact
5.38

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article

Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles

Paulo Gonçalves de Sousa, Rafael Leandro Fernandes Melo, Pierre Basílio Almeida Fechine, José Cleiton Sousa dos Santos et al.
23 citations
Langmuir
Enzyme Catalysis and Immobilization
5.38
article

Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles

Paulo Gonçalves de Sousa, Rafael Leandro Fernandes Melo, Pierre Basílio Almeida Fechine, José Cleiton Sousa dos Santos, Viviane de Castro Bizerra, Juliana de França Serpa, Diego Lomonaco, Aluísio Marques da Fonseca, Kaiany Moreira dos Santos, Valdilane Santos Alexandre, Maria Cristiane Martins de Souza
article en
23 citations

Abstract

This research investigated the usefulness of magnetic iron oxide nanoparticles (Fe<sub>3</sub>O<sub>4</sub>) as a support to immobilize the lipase Eversa Transform 2.0 (ET 2.0) to obtain an active and stable biocatalyst, easily recoverable from the reaction medium for applications in the production of biodiesel. Biodiesel was an alternative fuel composed mainly of fatty acid esters with strong transesterification and esterification capabilities. The study focused on the esterification of oleic acid with ethanol to synthesize ethyl oleate. Magnetic nanoparticles were prepared by coprecipitation, then activated with glutaraldehyde and functionalized with γ-aminopropyltriethoxysilane (APTES). The optimal conditions for immobilizing ET 2.0 were pH 10, 25 mM sodium carbonate buffer, an enzymatic load of 200 U/g, and 1 h of contact time, obtaining 78% yield and enzymatic activity of 205.9 U/g. Postimmobilization evaluation showed that the immobilized enzyme performed better than its free form. Kinetic studies were conducted under these optimized conditions (2-96 h at 150 rpm and 37 °C). The biocatalyst was tested for the synthesis of ethyl oleate using oleic acid as the substrate and ethanol, achieving a conversion of 88.1%. Subsequent recirculation tests maintained approximately 80% conversion until the fourth cycle, confirming the sustainability of ester production. Molecular docking studies revealed that the binding affinity for the enzyme-docked oil composition was estimated at -5.8 kcal/mol, suggesting that the combination of the substrate and lipase was stable and suitable for esterification.

LangmuirVol. 40(51)
Universidade Federal do Ceará (BR), University for International Integration of the Afro-Brazilian Lusophony (BR)
Coordenação de Aperfeiçoamento de Pessoal de Nível Superior, Conselho Nacional de Desenvolvimento Científico e Tecnológico, Fundação Cearense de Apoio ao Desenvolvimento Científico e Tecnológico
Openalex Percentile: Top 3%
Enzyme Catalysis and Immobilization
5.38
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