Production of feruloylated lysophospholipids via a one-step enzymatic interesterification.

Incorporation of ferulic acid (FA) into egg-yolk phosphatidylcholine (PC) in a lipase-catalyzed acidolysis and interesterification process was studied using four commercially available immobilized lipases as catalysts and two acyl donors: ferulic acid (FA) and ethyl ferulate (EF). Novozym 435 and a binary solvent system of toluene/chloroform 9:1 (v/v) were found to be the most suitable biocatalyst and medium, respectively, and significantly increased the incorporation of FA into the phospholipid fraction. Subsequently response surface methodology (RSM) and Box-Behnken design were employed to evaluate the effects of substrate molar ratio, enzyme loading and time of the reaction on the process of interesterification. The selected optimized parameters were established as PC/EF molar ratio 1/15, enzyme load 30% (w/w) and incubation time 6 days. The process of interesterification at the optimized parameters carried out on a large scale afforded feruloylated lysophosphatidylcholine (FLPC) in high isolated yield of 62% (w/w).