Lipase-catalyzed Synthesis of Oleoyl-lysophosphatidylcholine by Direct Esterification in Solvent-free Medium without Water Removal

Overview & Synopsis

In this work, the synthesis of oleoyl-lysophosphatidylcholine by lipase-catalyzed esterification of glycerophosphocholine (GPC) and free oleic acid in a reaction medium without solvent is presented. The complete solubilisation of GPC, which is a crucial issue in non-polar liquids such as melted free fatty acids, was reached by heating the GPC/oleic acid mixture at high temperature during a short time. The immobilized lipase from Rhizomucor miehei (Lipozyme RM-IM) was shown to catalyze the reaction more efficiently than the immobilized lipases from Thermomyces lanuginosus (Lipozyme TL-IM) and Candida antarctica (Novozym 435). The condition reactions leading to the highest yield were as follows: substrate ratio: 1/20 (GPC/oleic acid); amount of catalyst: 10% (w/w of substrates); temperature: 50°C. Under these conditions, a yield of 75% of oleoyl-lysophosphatidylcholine was achieved in 24 h under stirring and almost no dioleoyl-lysophosphatidylcholine was produced. Unlike other studies dealing with the esterification of GPC with free fatty acids, the removal of the water produced while the reaction proceeds was not necessary to reach high yields.