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241127s2024 xx |||||o 00| ||eng c |
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|a 10.1021/acs.langmuir.4c02542
|2 doi
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|a pubmed24n1641.xml
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|a (DE-627)NLM380778408
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|a (NLM)39591534
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|a DE-627
|b ger
|c DE-627
|e rakwb
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| 041 |
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|a eng
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|a Dos Santos, Kaiany Moreira
|e verfasserin
|4 aut
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| 245 |
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|a Enhanced Biodiesel Production with Eversa Transform 2.0 Lipase on Magnetic Nanoparticles
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|c 2024
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|a Text
|b txt
|2 rdacontent
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|a ƒaComputermedien
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|2 rdamedia
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|a ƒa Online-Ressource
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|2 rdacarrier
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|a Date Completed 24.12.2024
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|a Date Revised 24.12.2024
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|a published: Print-Electronic
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|a Citation Status MEDLINE
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|a This research investigated the usefulness of magnetic iron oxide nanoparticles (Fe3O4) 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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|a Journal Article
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|a Biofuels
|2 NLM
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|a Lipase
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|a EC 3.1.1.3
|2 NLM
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|a Enzymes, Immobilized
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|a Magnetite Nanoparticles
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|a Oleic Acids
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|a Oleic Acid
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|a 2UMI9U37CP
|2 NLM
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|a ethyl oleate
|2 NLM
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|a Z2Z439864Y
|2 NLM
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|a de França Serpa, Juliana
|e verfasserin
|4 aut
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|a de Castro Bizerra, Viviane
|e verfasserin
|4 aut
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|a Melo, Rafael Leandro Fernandes
|e verfasserin
|4 aut
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|a Sousa Junior, Paulo Gonçalves de
|e verfasserin
|4 aut
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|a Santos Alexandre, Valdilane
|e verfasserin
|4 aut
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|a da Fonseca, Aluísio Marques
|e verfasserin
|4 aut
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|a Fechine, Pierre Basílio Almeida
|e verfasserin
|4 aut
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|a Lomonaco, Diego
|e verfasserin
|4 aut
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|a Sousa Dos Santos, José Cleiton
|e verfasserin
|4 aut
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|a Martins de Souza, Maria Cristiane
|e verfasserin
|4 aut
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| 773 |
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|i Enthalten in
|t Langmuir : the ACS journal of surfaces and colloids
|d 1999
|g 40(2024), 51 vom: 24. Dez., Seite 26835-26851
|w (DE-627)NLM098181009
|x 1520-5827
|7 nnns
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| 773 |
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|g volume:40
|g year:2024
|g number:51
|g day:24
|g month:12
|g pages:26835-26851
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|u http://dx.doi.org/10.1021/acs.langmuir.4c02542
|3 Volltext
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|h 26835-26851
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