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Acidic and alkaline proteases from visceral waste of Labeo rohita (Hamilton, 1822) were isolated, partially purified by ammonium sulphate precipitation followed by dialysis, their kinetics and characteristics studied. The purification fold increased from 1.24 to 2.49 and 1.19 to 1.55 in acidic and alkaline protease respectively along the purification steps. The molecular weight was found in the range of 15-35 kDa and 25-63 kDa respectively in acidic and alkaline proteases. The pH and temperature optima for acidic and alkaline proteases were 3 and 10, at 40°C and 60°C respectively. The Protease activity was decreased by 40% and 60%, when incubated at 90°C for 30 min. Both the proteases showed a decreased activity of more than 50% after incubation with NaCl concentration of 0.5%. Degree of hydrolysis (DH) of the proteases on muscle protein increased with increase of enzyme concentrations. Both soybean trypsin inhibitor and EDTA exhibited high percentage of inhibition, when proteases were incubated with 50 mM of both the inhibitors. The study showed that proteases from Rohu visceral waste of could find use in applications where maximum activity at moderate temperature and low NaCl concentration is desired.