Higher animal's lipases are well characterized; however, much less is known about lipases from mollusks. A lipolytic activity was located in the land snail (Eobania vermiculata) digestive glands (hepatopancreas), from which a snail digestive lipase (SnDL) was purified. Pure SnDL has a molecular mass of 60 kDa; it does not present the interfacial activation phenomenon. It was found to be more active on short-chain triacylglycerols than on long-chain triacylglycerols. The NH2-terminal sequence of the SnDL shows 66% of identity with the 17 NH2-terminal amino acids of a putative lipase from sea urchin (Strongylocentrotus purpuratus). No sequence identity was found with known lipases. Interestingly, neither colipase nor bile salts were detected in the snail hepatopancreas. This suggests that colipase evolved in vertebrates simultaneously with the appearance of an exocrine pancreas and a true liver which produces bile salts. Altogether, these results suggest that SnDL is a member of a new group of digestive lipases belonging to invertebrates.