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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.