Snail Hepatopancreatic Lipase: A New Member of Invertebrates Lipases' Group Sawsan Amara & Ahmed Fendri & Nadia Ben Salem & Youssef Gargouri & Nabil Miled Received: 29 July 2009 / Accepted: 25 October 2009 / Published online: 20 November 2009 # Humana Press 2009 Abstract 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 NH 2 -terminal sequence of the SnDL shows 66% of identity with the 17 NH 2 -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. Keywords Hepatopancreas . Snail . Invertebrate . Digestive lipase . Purification . Characterization Abbreviations AG Arabic gum BSA Bovine serum albumin DEAE Diethylaminoethyl FPLC Fast protein liquid chromatography NaDC Sodium deoxycholate NaTDC Sodium taurodeoxycholate SDS Sodium dodecyl sulfate SDS-PAGE Sodium dodecyl sulfate-polyacrylamide gel electrophoresis SnDL Snail digestive lipase Appl Biochem Biotechnol (2010) 162:942–952 DOI 10.1007/s12010-009-8837-z S. Amara : A. Fendri : N. Ben Salem : Y. Gargouri : N. Miled (*) Laboratoire de Biochimie et de Génie Enzymatique des Lipases, ENIS route de Soukra, BPW 3038 Sfax, Tunisia e-mail: nmiled@yahoo.com