Enzymatic synthesis of lysophosphatidylcholine with n−3 polyunsaturated fatty acid from sn-glycero-3-phosphatidylcholine in a solvent-free system

- Lipases TLIM was more effective than phospholipases and other lipases for esterification of GPC and n−3 PUFA.
- Optimal conditions were a temperature of 45 °C, a mole ratio of 1:20 (GPC to n−3 PUFA) under vacuum for 64 h.
- The 1-acyl-sn-glycero-3-lysophosphatidylcholine (2-LPC) was predominant in the reaction.

The n−3 polyunsaturated fatty acids (PUFA)-rich lysophosphatidylcholine (LPC) was successfully synthesized by Thermomyces lanuginosus lipase (TL IM)-catalyzed esterification of glycerylphosphorylcholine (GPC) and n−3 PUFA-rich fatty acids in a solvent-free system. Effects of reaction temperature, enzyme loading and substrate mole ratio on the yield of LPC and incorporation of n−3 PUFA were evaluated. The acyl-specificities of five enzymes were tested for direct esterification of n−3 PUFA, and Lipozyme TL IM was found to be more effective than others for production of LPC with n−3 PUFA. Substrate mole ratio and reaction temperature, however, had no significant effect on the incorporation. The maximal yield of LPC was obtained under the following conditions: temperature 45 °C, enzyme loading 15% by weight and substrate mole ratio (GPC/n−3 PUFA) 1:20. Furthermore, the composition of products were further investigated in the study. The 1-acyl-sn-glycero-3-lysophosphatidylcholine (2-LPC) was predominant in the mixtures at early stages of reaction, whereas less increment of 2-acyl-sn-glycero-3-lysophosphatidylcholine (1-LPC) and PC was observed at later stages.