Crude porcine lipase (triacylglycerol lipase, EC 3.1.1.3) was purified in a single-stage chromatographic process. The purification was accomplished in a batch, as well as in a continuous system. Two types of size-exclusion packing materials (Sephadex and Sephacryl) were used. The average x-fold increase in purity, and the average recovered activity in the batch Sephadex and Sephacryl experiments were 13.6 and 89.7%, and 34.2 and 98.8%, respectively. The average x-fold increase in purity and the average activity recovered in the continuous Sephadex and Sephacryl experiments were 27.1 and 82.5% and 16.2 and 89%, respectively. Flow visualization experiments were carried out by tagging the protein to be separated with a fluorescent dye The results from these experiments are also reported in this article.