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Authors = Aluísio Marques da Fonseca ORCID = 0000-0002-8112-9513

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19 pages, 7730 KiB  
Article
Ester Production Using the Lipid Composition of Coffee Ground Oil (Coffea arabica): A Theoretical Study of Eversa® Transform 2.0 Lipase as an Enzymatic Biocatalyst
by Millena Mara Rabelo Nobre, Ananias Freire da Silva, Amanda Maria Menezes, Francisco Lennon Barbosa da Silva, Iesa Matos Lima, Regilany Paulo Colares, Maria Cristiane Martins de Souza, Emmanuel Silva Marinho, Rafael Leandro Fernandes Melo, José Cleiton Sousa dos Santos and Aluísio Marques da Fonseca
Compounds 2023, 3(3), 411-429; https://doi.org/10.3390/compounds3030031 - 28 Jul 2023
Cited by 4 | Viewed by 2638
Abstract
The scientific community recognizes coffee grounds (Coffea arabica) as an important biological residue, which led to using the Eversa® Transform 2.0 lipase as an in silico enzymatic catalyst for coffee grounds’ free fatty acids (FFA). Molecular modeling studies, including molecular [...] Read more.
The scientific community recognizes coffee grounds (Coffea arabica) as an important biological residue, which led to using the Eversa® Transform 2.0 lipase as an in silico enzymatic catalyst for coffee grounds’ free fatty acids (FFA). Molecular modeling studies, including molecular docking, were performed, which revealed the structures of the lipase and showed the primary interactions between the ligands and the amino acid residues in the active site of the enzyme. Of the ligands tested, 6,9-methyl octadienoate had the best free energy of −6.1 kcal/mol, while methyl octadecenoate and methyl eicosanoate had energies of −5.7 kcal/mol. Molecular dynamics confirmed the stability of the bonds with low Root Mean Square Deviation (RMSD) values. The MMGBSA study showed that methyl octadecenoate had the best free energy estimate, and CASTp identified key active sites for potential enzyme immobilization in experimental studies. Overall, this study provides efficient and promising results for future experimental investigations, showing a classification of oils present in coffee grounds and their binding affinity with Eversa. Full article
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37 pages, 7084 KiB  
Review
Lipase from Yarrowia lipolytica: Prospects as an Industrial Biocatalyst for Biotechnological Applications
by Jessica Lopes da Silva, Misael Bessa Sales, Viviane de Castro Bizerra, Millena Mara Rabelo Nobre, Ana Kátia de Sousa Braz, Patrick da Silva Sousa, Antônio L. G. Cavalcante, Rafael L. F. Melo, Paulo Gonçalves De Sousa Junior, Francisco S. Neto, Aluísio Marques da Fonseca and José Cleiton Sousa dos Santos
Fermentation 2023, 9(7), 581; https://doi.org/10.3390/fermentation9070581 - 21 Jun 2023
Cited by 31 | Viewed by 6036
Abstract
This paper aims to present the advances related to the biotechnological application of lipases Y. lipolytica, presenting their properties and more efficient ways to use them in different industrial applications. Waste treatment and bioremediation highlight recent studies and advances and the interest [...] Read more.
This paper aims to present the advances related to the biotechnological application of lipases Y. lipolytica, presenting their properties and more efficient ways to use them in different industrial applications. Waste treatment and bioremediation highlight recent studies and advances and the interest in large-scale applications in the food sector and biofuel production. The USA and China, two major world powers in industy, are of utmost importance in the search for the improvement in the development and properties of a controlled system for the large-scale production of a significant number of applications of lipase from Y. lipolytica. Full article
(This article belongs to the Special Issue Yarrowia lipolytica: A Beneficial Yeast as a Biofactory for Biotechnological Applications)
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19 pages, 3610 KiB  
Article
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
by João Brandão Júnior, Jean Gleison Andrade do Nascimento, Michael Pablo França Silva, Eliane de Aquino Lima Brandão, Viviane de Castro Bizerra, Kaiany Moreira dos Santos, Juliana de França Serpa, José Cleiton Sousa dos Santos, Aluísio Marques da Fonseca, Diego Lomonaco Vasconcelos de Oliveira and Maria Cristiane Martins de Souza
Catalysts 2023, 13(3), 571; https://doi.org/10.3390/catal13030571 - 11 Mar 2023
Cited by 20 | Viewed by 4446
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 [...] Read more.
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. Full article
(This article belongs to the Special Issue Immobilized Biocatalysts II)
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20 pages, 3630 KiB  
Article
A Theoretical and Experimental Study for Enzymatic Biodiesel Production from Babassu Oil (Orbignya sp.) Using Eversa Lipase
by Jeferson Yves Nunes Holanda Alexandre, Francisco Thálysson Tavares Cavalcante, Lara Matias Freitas, Alyne Prudêncio Castro, Pedro Tavares Borges, Paulo Gonçalves de Sousa Junior, Manoel Nazareno Ribeiro Filho, Ada Amelia Sanders Lopes, Aluisio Marques da Fonseca, Diego Lomonaco, Maria Alexsandra de Sousa Rios and José Cleiton Sousa dos Santos
Catalysts 2022, 12(11), 1322; https://doi.org/10.3390/catal12111322 - 27 Oct 2022
Cited by 31 | Viewed by 3242
Abstract
A theoretical and experimental study was carried out on the biocatalytic production of babassu biodiesel through enzymatic hydroesterification. The complete hydrolysis of babassu oil was carried out using a 1:1 mass solution at 40 °C for 4 h using 0.4% of lipase from [...] Read more.
A theoretical and experimental study was carried out on the biocatalytic production of babassu biodiesel through enzymatic hydroesterification. The complete hydrolysis of babassu oil was carried out using a 1:1 mass solution at 40 °C for 4 h using 0.4% of lipase from Thermomyces lanuginosus (TLL). Then, with the use of Eversa® Transform 2.0 lipase in the esterification step, a statistical design was used, varying the temperature (25–55 °C), the molar ratio between free fatty acids (FFAs) and methanol (1:1 to 1:9), the percentage of biocatalyst (0.1% to 0.9%), and the reaction time (1–5 h) using the Taguchi method. The ideal reaction levels obtained after the statistical treatment were 5 h of reaction at 40 °C at a molar ratio of 1:5 (FFAs/methanol) using 0.9% of the biocatalyst. These optimal conditions were validated by chromatographic analysis; following the EN 14103 standard, the sample showed an ester concentration of 95.76%. A theoretical study was carried out to evaluate the stability of Eversa with FFAs. It was observed in the molecular docking results that the ligands interacted directly with the catalytic site. Through molecular dynamics studies, it was verified that there were no significant conformational changes in the studied complexes. Theoretical and experimental results show the feasibility of this process. Full article
(This article belongs to the Special Issue Catalysts for Biofuel and Bioenergy Production)
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