Acidic and antacid proteases from instinctive misuse of Labeo rohita (Hamilton et. al., 1822) were confined, incompletely sanitized by ammonium sulfate precipitation followed by dialysis, their energy and attributes considered. The purging fold expanded from 1.24 to 2.49 and 1.19 to 1.55 in acidic and soluble protease individually along with the cleaning steps. The atomic weight was found in the scope of 15-35 kDa and 25-63 kDa individually in acidic and basic proteases. The pH and temperature optima for acidic and basic proteases were 3 and 10, at 40°C and 60°C individually. The Protease action was diminished by 40% and 60% when hatched at 90°C for 30 min. Both the proteases demonstrated a diminished movement of over half after brooding with NaCl centralization of 0.5%. The level of hydrolysis (DH) of the proteases on muscle protein expanded with an increment of chemical fixations. Both soybean trypsin inhibitor and EDTA displayed a high level of hindrance when proteases were hatched with 50 mM of both the inhibitors. The investigation demonstrated that proteases from Rohu instinctive misuse could discover use in applications where the greatest movement at moderate temperature and low NaCl fixation is wanted.