Evaluation of Biochemical Properties of Digestive Lipolytic Enzymes from the Marine Snail (Hexaplex trunculus)

Unlike classical digestive lipolytic enzymes, the marine snail digestive lipase (mSDL) and marine snail digestive phospholipase A2 (mSDPLA2) showed maximal activities at a high temperature (50°C) and at pH 8.5. Both lipase and phospholipase A2 activities were remained stable in the presence of organic solvents. Phospholipase activity was calcium dependent, since no significant activities were detected in the presence of ion chelators like EDTA. Nevertheless, Mg2+, Mn2+ and Cu2+ inhibited the phospholipase activity. Otherwise, Hg2+ and Cu2+ ions act as strong inhibitors of mSDL activity when using tributyrin as a substrate. The digestive phospholipase cleaved efficiently fatty acids from phosphatidylcholine, phosphatidylglycerol, phosphatidylethanolamine and phosphatidylserine. Stability of lipase and phospholipase in the presence of organic solvents, as well as at high temperatures, makes them good candidates for application in non-aqueous catalysis.