Chitosanase which catalyze the hydrolytic degradation of chitosan is regarded as an important enzyme for the extense carbon and nitrogen recycle which occurs in nature. A bifunctional enzyme with chitosanase and carboxymethyl cellulase (CMCase) activity was purified from commercial cellulose, which was produced by Trichoderma viride, through sequential steps of DEAE-Sepharose CL-6B, ion-exchange chromatography, phenyl Sepharose CL-4B hydrophobic chromatography and Sephacryl S-200 gel filtration. The purified hydrolase was homogeneous, as examined by SDS-PAGE and RP-HPLC. The molecular mass was 66 kD and 64 kD estimated by SDS-PAGE and gel filtration,respectively.
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