Phospholipase A1-catalyzed hydrolysis of soy phosphatidylcholine to prepare l-α-glycerylphosphorylcholine in organic-aqueous media

Abstract

This study aimed to optimize the preparation of l-α-glycerylphosphorylcholine (l-α-GPC) via phospholipase A1 (Lecitase Ultra)-catalyzed hydrolysis of soy phosphatidylcholine (PC). The reaction was performed in n-hexane–water biphasic media in a stirred batch reactor, and modeling and optimization were conducted using response surface methodology. Optimal conditions to completely hydrolyze PC to l-α-GPC were: temperature, 50°C; reaction time, 30h; water content, 69g/100g of PC weight; and enzyme loading, 13g/100g of PC weight. The optimal n-hexane-to-water ratio in the medium was 5.8:1 (v/v), and 21.3g of PC was treated as the substrate in 100mL of the medium. l-α-GPC with purity 99.3g/100g was obtained from the reaction products after diethyl ether extraction and silica column chromatography. These findings suggest that the use of n-hexane–water media increases the productivity of l-α-GPC compared to the aqueous media used in enzymatic reaction systems in other published studies.