Modeling and optimization of phospholipase A1-catalyzed hydrolysis of phosphatidylcholine using response surface methodology for lysophosphatidylcholine production

Chang Wan Lim, Byung Hee Kim, In Hwan Kim, Moon Won Lee

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

Modeling the phospholipase A1 (PLA1)-catalyzed partial hydrolysis of soy phosphatidylcholine (PC) in hexane for the production of lysophosphatidylcholine (LPC) and optimizing the reaction conditions using response surface methodology were described. The reaction was performed with 4 g of PC in a stirred batch reactor using a commercial PLA1 (Lecitase Ultra) as the biocatalyst. The effects of temperature, reaction time, water content, and enzyme loading on LPC and glycerylphosphorylcholine (GPC) content in the reaction products were elucidated using the models established. Optimal reaction conditions for maximizing the LPC content while suppressing acyl migration, which causes GPC formation, were as follows: temperature, 60°C; reaction time, 3 h; water content, 10% of PC; and enzyme loading, 1% of PC. When the reaction was conducted with 40 g of PC under these conditions, the reaction products contained 83.7 mol % LPC and were free of GPC. LPC had a higher total unsaturated fatty acid content than original PC had and was mainly composed of linoleic acid (78.0 mol % of the total fatty acids).

Original languageEnglish
Pages (from-to)35-41
Number of pages7
JournalBiotechnology Progress
Volume31
Issue number1
DOIs
Publication statusPublished - 2015 Jan 1

Keywords

  • Acyl migration
  • Hydrolysis
  • Lysophosphatidylcholine
  • Phospholipase A
  • Response surface methodology

ASJC Scopus subject areas

  • Biotechnology

Fingerprint Dive into the research topics of 'Modeling and optimization of phospholipase A<sub>1</sub>-catalyzed hydrolysis of phosphatidylcholine using response surface methodology for lysophosphatidylcholine production'. Together they form a unique fingerprint.

  • Cite this