Abstract
The synthesis of decyl acetate, by the transesterification of vinyl acetate with decanol, was studied using supercritical CO 2 as solvent and immobilized Candida antarctica lipase B as catalyst (Novozym ® 435). The enzymatic content was determined for each particle size of the catalyst, indicating that the enzyme is located in an external shell of the particle, following an “egg-shell” distribution, with an estimated thickness of ca. 60 μm, independent of the particle size. The reaction was enhanced by increasing the enzyme loading, the concentration of vinyl acetate and the temperature; it was inhibited by excess of decanol and by increasing the pressure. A simplified model, based on the Ping-pong bi-bi mechanism with competitive inhibition by the alcohol, was proposed for the transesterification of vinyl acetate with decanol at 35 °C and 100 bar, and it was found to be suitable to represent the kinetic data.
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