Synthesis of CLA ‐rich lysophosphatidylcholine by immobilized MAS1‐H108A‐catalyzed esterification: Effects of the parameters and monitoring of the reaction process

Abstract Conjugated linoleic acid (CLA)‐rich lysophosphatidylcholine (LPC) with many proven beneficial effects was successfully synthesized by an immobilized mutant lipase (MAS1‐H108A)‐catalyzed esterification of glycerophosphorylcholine (GPC) and CLA‐rich FAs. Under the optimized conditions (temperature of 55 °C, substrate molar ratio of CLA‐rich FAs to GPC of 40:1, and enzyme loading of 300 U/g), LPC content as high as 89.10 mol% was achieved, which was exceptionally higher than any ever‐reported value. By monitoring the esterification process, it was found that sn1‐LPC was easy to synthesize and was the predominant product, while sn2‐LPC and phosphatidylcholine (PC) were difficult to synthesize and were with lower content in the final product. The formed sn2‐LPC during esterification may mainly attribute to the acyl migration of sn1‐LPC and the ratio of sn1‐LPC to sn2‐LPC finally plateaued at approximately 7. Besides, our results also demonstrated that sn2‐LPC was the main template for the synthesis of PC. Finally, a complete reaction scheme for the synthesis of LPC by immobilized MAS1‐H108A‐catalyzed esterification of GPC and fatty acids was mapped out. Overall, the highest LPC content could be obtained by immobilized MAS1‐H108A‐catalyzed esterification and there is the first study for systematical studying the reaction process of CLA‐rich LPC synthesis.
Source: European Journal of Lipid Science and Technology - Category: Lipidology Authors: Tags: Research Article Source Type: research