Partial characterization of digestive proteases in the river prawn Macrobrachium americanum () (Decapoda: Caridea: Palaemonidae) in Mexico

Abstract

Abstract We characterized the digestive enzymes in adults of Macrobrachium americanum (Spence Bate, 1868) in southeastern Mexico. The digestive enzyme extracts were made from the specimens’ hepatopancreas. Alkaline proteases, trypsin, chymotrypsin, carboxypeptidase A, leucine aminopeptidase, lipases, α-amylase and alkaline phosphatase activities were determined, as well as the percentage of inhibition, pH, and temperature stabilities through biochemical and electrophoretic techniques. The maximum digestive activity of proteases was at 35 °C and pH 11. Alkaline digestive proteases were highly stable at pHs 4, 9 and 11 at 55 °C after 30 min pre-incubation. PMSF inhibited two bands with proteolytic activity (35.1 and 23.2 kDa), and SBT1 inhibited all bands, including the one with the highest molecular weight (64.2 kDa). We concluded that enzymes in M. americanum coincide with those of omnivorous decapods with a tendency to carnivory.