Enzymatic Production of Decyl Acetate: Kinetic Study in n-Hexane and Comparison with Supercritical CO₂

Abstract

The kinetics of the lipase-catalyzed synthesis of decyl acetate, by the transesterification reaction of vinyl acetate with decanol, was investigated at 30 °C using n-hexane as the solvent. Novozym 435 was found to be the most active catalyst among the immobilized lipases tested. Given the nonideality of the reaction mixture, only a thermodynamic activity-based kinetics was found to be suitable to represent the experimental data in the entire range of compositions tested (0.1-1.4 M). The reaction follows a ping-pong bi-bi mechanism, in which inhibition only by excess of alcohol was identified. Although intraparticle diffusional limitations were detected, intrinsic kinetic parameters were obtained by crushing the catalyst particles. The results were compared to those obtained with supercritical CO 2 as the solvent. For the conditions tested, Candida antarctica lipase B showed higher activity in the organic medium.

Kinetics and optimization of lipase-catalyzed synthesis of rose fragrance 2-phenylethyl acetate through transesterification

“…However, the inhibition behavior by 2-PE was observed since the increase in 2-PE concentration did not increase the initial rate at any given VAc concentration; the initial rate decreasing at higher concentrations of 2-PE could be attributed to the high affinity of 2-PE to lipase and slowly removing it from the active site. Recently, high concentrations of alcohol-inhibited lipase catalyzed esterification or transesterification were also reported [28,29].…”