Immobilized lipase from Candida antarctica lipase B (Novozym 435) was effective in the synthesis of lysophosphatidylcholine (LPC). The transesterification of L-alpha-glycerophosphorylcholine (GPC) and vinyl laurate was carried out in a solvent free system or in the presence of 50% (v/v) t-butanol. High conversions (>95%) were easily achieved. The lipase was selective for the sn-1 position of the glycerol backbone, and almost no phosphatidylcholine was produced in the first 24 hours of the reaction. However, and probably due to acyl migration, the formation of phosphatidylcholine (PC) increased slowly if the reactions were incubated over a long period of time. The synthetic reaction was only possible with a high excess of vinyl laurate over glycerophosphorylcholine (>10 times). High purity products could be produced by a decrease of the reaction temperature to induce precipitation of the product. The temperature needed depended on the fatty acid chain length. Thus, only lysophosphatidylcholine was produced with palmitic acid vinyl ester at 45 degrees C, whereas for the vinyl esters of lauric acid, capric acid, and caprylic acid, a lower reaction temperature (25 degrees C) was necessary to obtain solely the lysophospholipid products. (C) 2000 Elsevier Science Inc. All rights reserved.