Lipase-catalyzed interesterification of butterfat blended with rapeseed oil (70/30, w/w) was investigated both in batch and in continuous reactions. Six commercially available immobilized lipases were screened in batch experiments, and the lipases, Lipozyme TL IM and Lipozyme RM IM, were chosen for further studies in a continuous packed bed reactor. TL IM gave a fast reaction and had almost reached equilibrium with a residence time of 30 min, whereas RM IM required 60 min. The effect of reaction temperature was more pronounced for RM IM. TL IM showed little effect on the interesterification degree when the temperature was raised from 60 degrees C to 90 degrees C, whereas RM IM had a positive effect when the temperature was increased from 40 degrees C to 80 degrees C. Even though TL IM is an sn-1,3 specific lipase, small changes in the sn-2 position of the triacylglycerol could be seen. The tendency was toward a reduction of the saturated fatty acid C14:0 and C16:0 and an increase of the long-chain saturated and unsaturated fatty acids (C18:0 and C18:1), especially at longer residence times (90 min). In prolonged continuous operation the activity of TL IM was high for the first 5 days, whereafter it dramatically decreased over the next 10 days to an activity level of 40%. In general, the study shows no significant difference for butterfat interesterification in terms of enzyme behavior from normal vegetable oils and fats even though it contains short-chain fatty acids and cholesterol. However, the release of short-chain fatty acids from enzymatic reactions makes the sensory quality unacceptable for direct edible applications.