Enzymatic synthesis of lysophosphatidylcholine containing CLA from sn-glycero-3-phosphatidylcholine (GPC) under vacuum

Seung In Hong, Yangha Kim, Chong Tai Kim, In-Hwan Kim

Research output: Contribution to journalArticle

18 Citations (Scopus)


Lysophosphatidylcholine (LPC) was successfully synthesised by enzyme-catalysed esterification of sn-glycero-3-phosphatidylcholine (GPC) with the acid form of conjugated linoleic acid (CLA), using a vacuum system. GPC was prepared from phosphatidylcholine (PC) by alkaline deacylation using a methanolic tetra-butylammonium hydroxide solution. Five enzymes were tested as biocatalysts for direct esterification, and lipases were found to be more effective than phospholipases for production of LPC. Amongst the enzymes tested, Novozym 435, from Candida antarctica, gave the highest yield of LPC. The optimal temperature, molar ratio of substrate, and vacuum were 40°C, 1:50 (GPC to CLA), and 1 mm Hg, respectively. The maximum yield (70 mol%) of LPC was obtained under optimal conditions after a 48 h reaction time.

Original languageEnglish
Pages (from-to)1-6
Number of pages6
JournalFood Chemistry
Issue number1
Publication statusPublished - 2011 Nov 1



  • Conjugated linoleic acid (CLA)
  • Lysophosphatidylcholine (LPC)
  • Novozym 435
  • Phosphatidylcholine (PC)
  • sn-Glycero-3-phosphatidylcholine (GPC)
  • Vacuum system

ASJC Scopus subject areas

  • Food Science
  • Analytical Chemistry

Cite this