Esterification of Short Chain Organic Acids with Alcohols by a Lipase Microencapsulated in Reversed Micelles

Abstract
A Mucor miehei lipase was used to catalyse the esterification reaction between propionic acid and oleyl alcohol in reversed micelles of AOT in isooctane. Small-scale model studies were performed to study the influence of various parameters on the formation of oleyl propionate by this lipase. The maximum synthetic activity was obtained at w0 = 4.0. At high temperatures (65°C) the enzyme displays a better stability for a low water content (w0 = 3.3). The specificity of lipase was influenced by the solubilized water in the reversed micelles.

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