Characterization of crude proteases derived from Bacillus licheniformis F11.1 and F11.4 obtained from crustacean shell originated from Palembang, Indonesia, was studied. Crude proteases showed optimum pH and temperature at 10.0 and 60 C, respectively. Addition of calcium, magnesium, and sodium ions (5 mM concentration) resulted in changes of relative activity of crude protease derived from F11.1 to 117.53%, 95.23%, and 83.63%, respectively; while in crude proteases from F11.4 to 125.01%, 102.37%, and 80.25%, respectively. Addition of EDTA (5mM) and SDS (0.1%) reduced relative activity down to 84.49% and 84.16%, respectively for crude protease of F11.1; while for crude protease of F11.4 it was 83.37% and 89.56%. Addition of 10% ethanol or 10% hexane reduced relative activity to 50.53% and 42.84% respectively for crude protease from F11.1; and 64.73% and 50.64% respectively for crude proteases from F11.4. In term of food product specificity, the best one to be utilized by crude protease derived from F11.1 and F11.4 were soy protein concentrate and casein respectively. The stability of crude protease derived from F11.1 and from F11.4 was higher at pH 10.0 rather than pH 7.0 within temperature of 60 C. The stability of crude protease derived from F11.1 and F11.4 was higher at 60 C rather than at 80 C within pH 10.0; and addition of calcium ions (5 mM) increased the temperature stability of crude proteases from both F11.1 and F11.4.