In this study, the enzymatic properties of the recombinant collagenase (ColM13) from engineering bacteria pET30a-ColM13/BL21 were analyzed after expression and purification.By studying the effects of temperature, pH and inhibitor, the optimal reaction temperature and pH for the ColM13 enzyme activity were determined as 50 ℃ and 8.0 respectively.The ColM13 enzyme was stable when the temperature was 20-55 ℃.The ColM13 enzyme activity was stable between pH 6.0-9.0.Metalloproteinase inhibitors EDTA and EGTA had a significant inhibitory effect on ColM13.The structural properties of bone collagen and its hydrolysate were characterized by ultraviolet (UV), differential scanning calorimetry (DSC), fluorescence and fourier transform infrared spectroscopy (FT-IR).The results showed that the enzymatic hydrolysis damaged the triple helical structure of collagen protein and released a large amount of free amino acids.The enzymolysis reduced the -NH2+- mutual exclusion on the collagen peptide chain and enhanced the hydrophobic amino acid residues.The collagen hydrolysate had higher thermal stability.Compared with the collagenase (BSC) isolated from B.cereus MBL13-U, the degradation of collagen treated by ColM13 was more significant.