Phospholipase A<inf>1</inf>-catalyzed hydrolysis of soy phosphatidylcholine to prepare l-α-glycerylphosphorylcholine in organic-aqueous media

Hyo Jeong Bang, In-Hwan Kim, Byung Hee Kim

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This study aimed to optimize the preparation of l-α-glycerylphosphorylcholine (l-α-GPC) via phospholipase A<inf>1</inf> (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.

Original languageEnglish
Pages (from-to)201-206
Number of pages6
JournalFood Chemistry
Publication statusPublished - 2016 May 26



  • Acyl migration
  • Hydrolysis
  • l-α-Glycerylphosphorylcholine
  • Phosphatidylcholine
  • Phospholipase A<inf>1</inf>
  • Response surface methodology

ASJC Scopus subject areas

  • Food Science
  • Analytical Chemistry

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