Collagenase is a kind of enzymes thatspecificallyhydrolyze natural collagen or gelatin. In order to prepare a new type of collagen protease and explore its ability to degrade collagen,a novelbone specific collagenase (BSC) was obtained fromBacillus cereuscrude enzyme liquid throughthe purification steps of ammonium sulfate precipitation, DEAE-Sepharose Fast Flow ion exchange chromatography and Sephadex G-100 gel chromatography. Furthermore, itsmolecular weight of the purified enzyme, substrate specificity and degradation ability were analyzed. What’s more, we derived the kinetic model of hydrolyzing bovine bone collagen. The results showed that the specific activity of BSC was 5.57×103U/mg, the purification times was up to 42.85 times, and its molecular weight was about 52.0 kDa. The specificity analysis showed that the substrate was a bone collagen enzyme, and its ability to hydrolyze type I collagen was significant.The comparative test indicated that the hydrolysis capacity of BSC was higher than that of other proteases.The dynamic model of the enzymatic degradation of collagen was:the degradation rate，degree of hydrolysis，Enzyme inactivation constant K4=64.1157 h-1. Theresults provided a novel collagenolytic protease for the development of animal bone collagen industrial.