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.
Chen, Wei-Ming; Chen, Ching-San; and Jiang, Shann-Tzong
"PURIFICATION AND CHARACTERIZATION OF AN EXTRACELLULAR CHITINASE FROM RHIZOPUS ORYZAE,"
Journal of Marine Science and Technology: Vol. 21
, Article 15.
Available at: https://jmstt.ntou.edu.tw/journal/vol21/iss3/15