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

Authors
Bang, Hyo-JeongKim, In-HwanKim, Byung Hee
Issue Date
Jan-2016
Publisher
ELSEVIER SCI LTD
Keywords
Acyl migration; L-alpha-Glycerylphosphorylcholine; Hydrolysis; Phosphatidylcholine; Phospholipase A(1); Response surface methodology
Citation
FOOD CHEMISTRY, v.190, pp 201 - 206
Pages
6
Journal Title
FOOD CHEMISTRY
Volume
190
Start Page
201
End Page
206
URI
https://scholarworks.bwise.kr/cau/handle/2019.sw.cau/64343
DOI
10.1016/j.foodchem.2015.05.093
ISSN
0308-8146
1873-7072
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.
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