Enzyme‐catalysed hydrolysis of phosphatidylcholine for the production of lysophosphatidylcholine

[Background] Production of lysophosphatidylcholine (LPC) via enzyme-catalysed hydrolysis was studied. Three enzymeswereemployed to conduct the reactions at different temperatures. The starting material, phosphatidylcholine (PC), was dispersed inwater (system A) and in ethanol (system B) to define the reaction mixture to carry out the trials.[Results] It was found that themedia 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 PLA1 and Novozym 435 were able to convert PC into LPC in ethanol, with yields of 50% and 58.51%, respectively, after 48 h at 50 ¿C. The highest degree of hydrolysis (70%) was reached with Lipase PS after 48 h at 60 ¿C in water.[Conclusions] Both 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.We thank Professor Garcia's team for the support given during the present work, and the National Council for Science and Technology of Mexico (CONACyT) for financial support through the grant 129334. The authors acknowledge the financial support of the National Plan of Materials of the Spanish Ministry of Science and Education (ref. MAT2007‐6662‐C02‐02), to the CSIC (Spain) for the JAE pre‐doctoral fellowship to author Baeza, and to the Spanish Ministry of Science and Education for a sabbatical grant for author Garcia.Peer Reviewe