Phospholipase A(1)-catalyzed hydrolysis of soy phosphatidylcholine to prepare L-alpha-glycerylphosphorylcholine in organic-aqueous media

Abstract

This study aimed to optimize the preparation of L-alpha-glycerylphosphorylcholine (L-alpha-GPC) via phospholipase A(1) (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-alpha-GPC were: temperature, 50 degrees C; reaction time, 30 h; water content, 69 g/100 g of PC weight; and enzyme loading, 13 g/100 g of PC weight. The optimal n-hexane-to-water ratio in the medium was 5.8:1 (v/v), and 21.3 g of PC was treated as the substrate in 100 mL of the medium. L-alpha-GPC with purity 99.3 g/100 g 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-alpha-GPC compared to the aqueous media used in enzymatic reaction systems in other published studies. (C) 2015 Elsevier Ltd. All rights reserved.