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 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.

Enhancing biocatalyst performance through immobilization of lipase (Eversa® Transform 2.0) on hybrid amine-epoxy core-shell magnetic nanoparticles.

Magnetic nanoparticles were functionalized with polyethylenimine (PEI) and activated with epoxy. This support was used to immobilize Lipase (Eversa® Transform 2.0) (EVS), optimization using the Taguchi method. XRF, SEM, TEM, XRD, FTIR, TGA, and VSM performed the characterizations. The optimal conditions were immobilization yield (I.Y.) of 95.04 ± 0.79 %, time of 15 h, ionic load of 95 mM, protein load of 5 mg/g, and temperature of 25 °C. The maximum loading capacity was 25 mg/g, and its stability in 60 days of storage showed a negligible loss of only 9.53 % of its activity. The biocatalyst demonstrated better stability at varying temperatures than free EVS, maintaining 28 % of its activity at 70 °C. It was feasible to esterify free fatty acids (FFA) from babassu oil with the best reaction of 97.91 % and ten cycles having an efficiency above 50 %. The esterification of produced biolubricant was confirmed by NMR, and it displayed kinematic viscosity and density of 6.052 mm2/s and 0.832 g/cm3, respectively, at 40 °C. The in-silico study showed a binding affinity of -5.8 kcal/mol between EVS and oleic acid, suggesting a stable substrate-lipase combination suitable for esterification.

A comprehensive review on enzyme-based biosensors: Advanced analysis and emerging applications in nanomaterial-enzyme linkage.

Biosensors with nanomaterials and enzymes detect and quantify specific targets in samples, converting recognition into measurable signals. The study explores the intrinsic synergy between these elements for detecting and quantifying particular targets in biological and environmental samples, with results demonstrated through bibliometric analysis and a comprehensive review of enzyme-based biosensors. Using WoS, 57,331 articles were analyzed and refined to 880. Key journals, countries, institutions, and relevant authors were identified. The main areas highlighted the multidisciplinary nature of the field, and critical keywords identified five thematic clusters, revealing the primary nanoparticles used (CNTs, graphene, AuNPs), major application fields, basic application themes, and niche topics such as sensitive detection, peroxidase activity, and quantum dot utilization. The biosensor overview covered nanomaterials and their primary applications, addressing recent advances and inherent challenges. Patent analysis emphasized the U.S. leadership in the industrial sector, contrasting with China's academic prominence. Future studies should focus on enhancing biosensor portability and analysis speed, with challenges encompassing efficient integration with recent technologies and improving stability and reproducibility in the nanomaterial-enzyme interaction.

Recent applications and future prospects of magnetic biocatalysts.

Magnetic biocatalysts combine magnetic properties with the catalytic activity of enzymes, achieving easy recovery and reuse in biotechnological processes. Lipases immobilized by magnetic nanoparticles dominate. This review covers an advanced bibliometric analysis and an overview of the area, elucidating research advances. Using WoS, 34,949 publications were analyzed and refined to 450. The prominent journals, countries, institutions, and authors that published the most were identified. The most cited articles showed research hotspots. The analysis of the themes and keywords identified five clusters and showed that the main field of research is associated with obtaining biofuels derived from different types of sustainable vegetable oils. The overview of magnetic biocatalysts showed that these materials are also employed in biosensors, photothermal therapy, environmental remediation, and medical applications. The industry shows a significant interest, with the number of patents increasing. Future studies should focus on immobilizing new lipases in unique materials with magnetic profiles, aiming to improve the efficiency for various biotechnological applications.