Phospholipase A(1)-catalyzed hydrolysis of soy phosphatidylcholine to prepare L-alpha-glycerylphosphorylcholine in organic-aqueous media
- Authors
- Bang, Hyo-Jeong; Kim, In-Hwan; Kim, Byung Hee
- Issue Date
- Jan-2016
- Publisher
- Elsevier BV
- Keywords
- Acyl migration; l-α-Glycerylphosphorylcholine; Hydrolysis; Phosphatidylcholine; Phospholipase A1; 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.sookmyung.ac.kr/handle/2020.sw.sookmyung/147081
- DOI
- 10.1016/j.foodchem.2015.05.093
- ISSN
- 0308-8146
1873-7072
- 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, 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-α-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-α-GPC compared to the aqueous media used in enzymatic reaction systems in other published studies.
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