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Advisor(s)
Abstract(s)
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 CO2 as the solvent. For the conditions tested, Candida antarctica lipase B showed higher activity in the organic medium.
Description
Keywords
Enzymztic catalysis Supercritical CO2
Citation
Ribeiro, Adriano S.; Oliveira, Manuela V.; Rebocho, Sílvia F.; Ferreira, Olga; Vidinha, Pedro; Barreiros, Susana; Macedo, Eugénia A.; Loureiro, José M. (2010). Enzymatic production of decyl acetate: kinetic study in n-hexane and comparison with supercritical CO2. Industrial & Engineering Chemistry Research. ISSN 0888-5885. 49:16, p. 7168-7175.
Publisher
American Chemical Society