Enzyme-catalysed hydrolysis of phosphatidylcholine for the production of lysophosphatidylcholine

Abstract

BackgroundProduction of lysophosphatidylcholine (LPC) via enzyme-catalysed hydrolysis was studied. Three enzymes were employed to conduct the reactions at different temperatures. The starting material, phosphatidylcholine (PC), was dispersed in water (system A) and in ethanol (system B) to define the reaction mixture to carry out the trials. ResultsIt was found that the media employed and the type of biocatalyst (free or immobilized), clearly determine the kinetics of the reactions. PC was well dissolved in ethanol but an opaque emulsion was obtained when it was dissolved in water. Immobilized PLA(1) and Novozym 435 were able to convert PC into LPC in ethanol, with yields of 50% and 58.51%, respectively, after 48h at 50 degrees C. The highest degree of hydrolysis (70%) was reached with Lipase PS after 48h at 60 degrees C in water. ConclusionsBoth reaction media enabled fairly good yields but water was better. The present work proposes a simple reaction scheme compared with other reports in the literature where different substrates, additives and polar solvents have been employed. LPC has interesting properties as a bioemulsifier, which led us to develop new methods for its production. (c) 2013 Society of Chemical Industry