Isolation and Purification of Chitinase from Shellfish of Procambarus clarkii

In this study,chitinase(EC 3.2.1.14)was purified from the shell membrane of Procambarus clarkii by ammonium sulfate fractionation and column chromatographies with Sephadex G-100,Phenyl Sepharose 6-Fast Flow and DEAE Sepharose-Fast Flow. The specific activity the chitinase of 44.93 U/mg and the purification multiple the enzyme was about 16.28 times. which was a single subunit protein. The molecular weight of the chitinase was 37.7 kDa with SDS-PAGE and flight mass spectrometry. This purification method of the experiment is feasible and provides a basis for the study of subsequent enzymatic properties.