Green Enzymatic Synthesis of Geranyl Butyrate: Process Optimization and Mechanistic Insights
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...
| Autores: | , , , , , , , , , , , |
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| Tipo de recurso: | artículo |
| Fecha de publicación: | 2024 |
| País: | España |
| Institución: | Universidad Complutense de Madrid (UCM) |
| Repositorio: | Docta Complutense |
| Idioma: | inglés |
| OAI Identifier: | oai:docta.ucm.es:20.500.14352/118927 |
| Acceso en línea: | https://hdl.handle.net/20.500.14352/118927 |
| Access Level: | acceso abierto |
| Palabra clave: | 612.393 613.2 641.1 577.15 547 663/665 Chemical reactions Flavor Organic compounds Organic reactions Peptides and proteins Alimentación Bioquímica (Biología) Tecnología de los alimentos Química orgánica (Química) 3309 Tecnología de Los Alimentos 2302.90 Bioquímica de Alimentos 2302.09 Enzimología 2306 Química Orgánica 3309.10 Aroma y Sabor |
| Sumario: | 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. |
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