Performance of Eversa Transform 2.0 Lipase in Ester Production Using Babassu Oil (Orbignya sp.) and Tucuman Oil (Astrocaryum vulgar): A Comparative Study between Liquid and Immobilized Forms in Fe3O4 Nanoparticles

• Published in: Catalysts Vol. 13; no. 3; p. 571
• Main Authors: Brandão Júnior, João, Andrade do Nascimento, Jean Gleison, França Silva, Michael Pablo, Lima Brandão, Eliane de Aquino, de Castro Bizerra, Viviane, dos Santos, Kaiany Moreira, Serpa, Juliana de França, Santos, José Cleiton Sousa dos, da Fonseca, Aluísio Marques, Vasconcelos de Oliveira, Diego Lomonaco, Souza, Maria Cristiane Martins de
• Format: Journal Article
• Language: English
• Published: Basel MDPI AG 01.03.2023
• Subjects: Alcohol; babassu; biodiesel; Biodiesel fuels; Biofuels; Catalysts; Chemical reactions; Chemical synthesis; Comparative studies; Coupling (molecular); Energy consumption; Enzymes; Esterification; Esters; Ethanol; Eversa Transform 2.0; Fatty acids; Free energy; Free form; Gas chromatography; Iron oxides; Lipase; Medical research; Methanol; Moisture content; Nanoparticles; Oils & fats; Soybeans; tucuman; Vegetable oils; Brazil; United States > US
• ISSN: 2073-4344; 2073-4344
• DOI: 10.3390/catal13030571

In this study, biodiesel was produced through the enzymatic esterification of vegetable oils from two common Brazilian palm trees: babassu and tucuman. The oils were hydrolyzed by a chemical route and their free fatty acids esterified with ethanol and methanol using the lipase enzyme Eversa® Transform 2.0 in free forms and supported in iron magnetic nanoparticles (Fe3O4) (enzymatic load: 80 UpNPBg−1). These enzymatic reactions were performed at an oil–alcohol molar ratio of 1:1, reaction temperature of 37 °C, agitation at 150 rpm, and reaction times of 2, 4, 6 and 8 h for the reactions catalyzed by the soluble enzyme and 8 h for the reactions using the biocatalyst. The conversions of fatty acids in ethyl and methyl esters obtained were monitored by gas chromatography (CG). The results obtained from ester synthesis using enzyme catalysts in free form were better: babassu 52.6% (methanol) and 57.5% (ethanol), and for tucuman 96.7% (methanol) and 93.4% (ethanol). In the case of immobilized enzymes, the results obtained ranged from 68.7% to 82.2% for babassu and from 32.5% to 86.0% for tucuman, with three cycles of reuse and without significant catalyst loss. Molecular coupling studies revealed the structures of lipase and that linoleic acid bonded near the active site of the enzyme with the best free energy of −6.5 Kcal/mol.