The immobilization of lipase onto two lipophilic particulate supports, non-porous polystyrene latex and porous Accurel EP400 powder, for the enzymic hydrolysis of sunflower oil is described. The activity of the immobilized enzyme was compared to that in free enzyme hydrolyses and the immobilization efficiency of lipase on each of the supports determined. Results indicated that, although polystyrene latex exhibited a very high affinity for the adsorption of lipase, enzyme activities were very poor. Satisfactory immobilization of lipase onto EP400 particles was attained only at high enzyme loadings. However, under these conditions, rates of hydrolysis and equilibrium conversions obtained using lipase immobilized onto EP400 particles were comparable to those achieved in free enzyme systems. In addition, once bound to the EP400 support, the enzyme displayed good recycle potential.