A chitinase with about 50 kDa of molecular mass from Rhizopus oryzae was purified to electrophoretical homogeneity after DEAE Sepharose and Sephacryl S-200 chromatographs, with specific activity of 165.2 U/mg, 19.7% recovery and 4.3-fold of purification. It had optimal pH and temperature at 5.5-6.0 and 60°C, respectively, and was stable at pH 5.0-8.5 and below 50°C. Ca2+, Sr2+, Ba2+, Mn2+, Co2+ and β-Me enhanced chitinase activity by 10-48% ,whereas Hg2+ and SDS strongly inhibited enzyme activity. This enzyme was identified that might be with both chitinolytic and amylolytic activity. According to the result of LC-MS/MS analysis, 4 identified amino acid sequences did not hit the same protein supposing that this enzyme is the first time reported.

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