Solvent-free Lipase-Catalyzed Preparation of Long-Chain Alkyl Phenylpropanoates and Phenylpropyl Alkanoates

Abstract

An enzymatic method was developed for the preparation of medium- or long-chain alkyl 3-phenylpropenoates (alkyl cinnamates), particularly alkyl hydroxy- and methoxy-substituted cinnamates such as oleyl p-coumarate and oleyl ferulate. The various alkyl cinnamates were formed in high to moderate yield by lipase-catalyzed esterification of cinnamic acid and its analogues with fatty alcohols in vacuo at moderate temperatures in the absence of drying agents and solvents. Immobilized Candida antarctica lipase B was the most effective biocatalyst for the various esterification reactions. The relative esterification activities were of the following order: dihydrocinnamic > cinnamic > 3-methoxycinnamic > dihydrocaffeic approximately 3-hydroxycinnamic > 4-methoxycinnamic > 2-methoxycinnamic > 4-hydroxycinnamic > ferulic approximately 3,4-dimethoxycinnamic > 2-hydroxycinnamic acid. With respect to the position of the substituents at the phenyl moiety, the esterification activity increased in the order meta > para > ortho. Rhizomucor miehei lipase demonstrated moderate esterification activity. Compounds with inverse chemical structure, that is, 3-phenylpropyl alkanoates such as 3-(4-hydroxyphenyl)propyl oleate, were also obtained in high yield by esterification of fatty acids with the corresponding 3-phenylpropan-1-ols.