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American lobster Cathepsin D, an aspartic peptidase resistant to proteolysis and active in organic solvents, non-ionic detergents and salts

Rodriguez-Siordia, Ivan, Rojo-Arreola, Liliana, Navarrete del Toro, María de los Angeles, García-Carreño, Fernando
International journal of biological macromolecules 2018 v.107 pp. 1501-1509
Homarus americanus, additives, cathepsin D, chromatography, detergents, enzyme activity, ethanol, fluorescence, gastric juice, isopropyl alcohol, lobsters, methanol, models, octoxynol, pH, papain, polysorbates, proteolysis, renin, salts, solvents, temperature, urea
Suitable peptidases for biotechnological applications are those active at low temperature, in organic solvents, detergents or proteolytic additives. American lobster cathepsin D1 (CD1) is an enzyme highly efficient at 5–50°C and at pH 2.5–5.5. We assessed the effect of common industrial additives on CD1 activity. CD1 was isolated from lobster gastric fluid by chromatography. The proteolytic activity was measured using a fluorogenic specific substrate and the conformation by intrinsic fluorescence. Non-ionic detergents Tween-20 and Triton X-100 stabilize the peptidase activity. Ethanol, methanol and isopropanol [5–15% (v/v)] increased the enzyme activity up to 80%. The enzyme is active until 2.5M urea and is resistant to proteolysis by papain and renin. In this work, a crustacean peptidase that remains active when exposed to different chemical and proteolytic additives is reported, evincing that crustaceans are a good model for discovery of novel stable peptidases for future pharmaceutical, cosmetic and alimentary applications.