The fatty layer obtained by centrifuging a homogenate of oil palm fruit mesocarp contains an active lipase. The lipase which was partially purified using a combination of ammonium sulphate fractionation, ion exchange and gel filtration chromatography, indicated an optimum activity at pH 4.5 and a temperature of 30°C. The enzyme exhibited good activity towards its natural substrate, palm oil as well as glycerol trioleate and glycerol tripalmitate. It also showed a linear reaction rate for the first 20 min of incubation. Sodium cyanide, resorcinol, cholesterol, lecithin and glycylglycine strongly inhibited its activity while phenol, L-cysteine and EDTA enhanced its activity. It is suggested that the lipase is associated with the membrane of the oil droplets.

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