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

Author:

Brandão Júnior João1,Andrade do Nascimento Jean Gleison1,França Silva Michael Pablo1,Lima Brandão Eliane de Aquino2,de Castro Bizerra Viviane1,dos Santos Kaiany Moreira1,Serpa Juliana de França1,Santos José Cleiton Sousa dos1ORCID,da Fonseca Aluísio Marques1ORCID,Vasconcelos de Oliveira Diego Lomonaco3ORCID,Souza Maria Cristiane Martins de1ORCID

Affiliation:

1. Institute of Engineering and Sustainable Development—IEDS, Campus das Auroras, University of International Integration of Afro-Brazilian Lusofonia—UNILAB, Rua José Franco de Oliveira, s/n—Rural Zone, Redenção 62790-970, CE, Brazil

2. Chemical Engineering Postgraduate Program—Technology Center, Campus Universitário—Lagoa Nova, Federal University of Rio Grande do Norte—UFRN, Natal 59078-970, RN, Brazil

3. Laboratory of Products and Technology in Processes (LPT), Federal University of Ceará—UFC, Fortaleza 60440-900, CE, Brazil

Abstract

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.

Publisher

MDPI AG

Subject

Physical and Theoretical Chemistry,Catalysis,General Environmental Science

Reference82 articles.

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