Lipase‐catalyzed synthesis of designer acylglycerols rich in residues of eicosapentaenoic, docosahexaenoic, conjugated linoleic, and/or stearic acids

Abstract

AbstractLipase‐catalyzed glycerolysis of a commercial acylglycerol (TG500), rich in eicosapentaenoic residues, and subsequent reaction of the product acylglycerols via esterification and/or transesterification reactions were investigated for the purpose of preparing acylglycerols enriched in particular fatty acid residues. An immobilized lipase from Candida antarctica (fraction B) was employed as biocatalyst for these reactions. The effects of enzyme loading, molar ratio of substrates, type of acyl donor, and use of a continuous purge stream of nitrogen were evaluated. The transesterification reactions were carried out using the ethyl esters of 3 different fatty acids, namely stearic, conjugated linoleic, and docosahexaenoic acids. Final yields of triacylglycerols of 75‐80% were obtained for the transesterification reactions with the 3 different types of fatty acid ethyl esters.