Catalytic Stability of Aspartic Proteinases Recovered from Viscera of Merluccius hubbsi, Percophis brailiensis, Urophicis brasiliensis, and Cynoscion guatucupa

The present work aimed to extract and characterize aspartic proteinases from the viscera of Merluccius hubbsi (Mh), Percophis brasiliensis (Pb), Urophycis brasiliensis (Ub), and Cynoscion guatucupa (Cg). Proteainse activity of Pb extracts was enhanced by the presence of Mn²⁺, K⁺, and Ca^+ 2. Conversely, the enzyme activity of the other species was stable in the presence of those ions. The surfactant Tween 20 increased enzyme activity in all cases. However, Tween 80 had a positive effect only for proteinases from Mh, Pb, and Ub. The enzymes of all species were stable in the presence of hydrogen peroxide. Acetone increased the enzyme activity in Pb extracts. Interestingly, aspartic proteinases from Mh, Pb, and Cg were compatible with the tested commercial detergents. The information from this work contributes to increase the knowledge about enzymes from South Atlantic species that could be incorporated as bioactive and biodegradable ingredients in different industries.