Portal de Periódicos da CAPES

Artigo Acesso aberto Produção Nacional Revisado por pares

BIBTEX RIS

Green Enzymatic Synthesis of Geranyl Butyrate: Process Optimization and Mechanistic Insights

2024; American Chemical Society; Linguagem: Inglês

10.1021/acsomega.3c08483

2470-1343

Francisco Simão Neto, Paulo Gonçalves de Sousa, Carlos José Alves da Silva Filho, Lucas Pinheiro Coutinho, Rafael Leandro Fernandes Melo, Javier Rocha‐Martín, Maria Alexsandra de Sousa Rios, Ada Amélia Sanders Lopes, Norberto de Kássio Vieira Monteiro, Marcos Carlos de Mattos, Leonardo F. Serafim, José Cleiton Sousa dos Santos,

Microbial Metabolic Engineering and Bioproduction

Flavor esters are organic compounds widely used in the food industry to enhance the aroma and taste of products. However, most chemical processes for the production of these flavoring compounds use toxic organic solvents. Some organic solvents derived from petroleum can leave behind residual traces in food products, which may raise concerns about potential health risks and contamination. In this study, we employ Eversa Transform 2.0, a commercial lipase derived from the lipase from Thermomyces lanuginosus, to produce geranyl butyrate in aqueous media. The chemical process was optimized using the Taguchi method, and a conversion of 93% was obtained at the optimal reaction conditions of: 1:5 molar ratio (v/v), 15% biocatalyst load (w/w), at 50 °C, in 6 h. Classic (molecular dynamics) and quantum (density functional theory) simulations unveiled amino acid residues involved in the stabilization of the enzyme–substrate complex. Detailed QM/MM mechanistic studies identified the nucleophilic attack of the deacylation reaction as the rate-limiting step of the entire mechanism, which has a free energy barrier of 14.0 kcal/mol.