Purification of Chitosanase of Beta proteobacterium sp.T_1

Objective:Purification of Chitosanase of Beta proteobacterium sp.T1.Methods:The chitosanase of the strain is extracted by ammonium sulfate precipitation(20%-70%saturation),and purified by ion-exchange chromatography(DEAE Cellulose 52) and gel filtration(Sephadex G-100);SDS-PAGE is used to identify the purity and molecular weight of the chitosanase.Results: Chitosanase from Beta proteobacterium sp.T1 was purified about 13.19 fold by DEAE Cellulose 52 and was purified about 26.32 fold by Sephadex G-100.Conclusion: The purified enzyme is demonstrated by SDS-PAGE to be a hormogenous protein.The molecular is determined as about 29.5 kDa by SDS-PAGE.