Abstract
Lipase-catalyzed esterification of caffeic acid with 1-propanol, to form caffeic acid propyl ester (CAPE), was investigated in ionic liquid using immobilized lipase. Ten ILs were used as the reaction medium; three types of lipases were selected as biocatalysts, and the lipase-catalyzed synthesis properties of CAPE were measured systematically in order to enhance the yield of CAPE. The results indicated that when [Bmim][Tf2N] was selected as reaction media, Novozym 435 was used as catalyst, the molar ratio of 1-propanol to CA was 10:1, the reaction temperature was 80 °C, and the mass ratio of catalyst to CA was 18:1, the highst yield of CAPE attained 41.0 %.
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