Abstract: A fungium-producing chitinase was isolated from the dead body of Anisopliae. A chitinase was isolated from the culture of Metarhizium anisopliae and purified to electrophoretic homogeneity by the steps of ammonium sulfate precipitation,DEAE-cellulose and hydrophobic interaction column chromatography. Its molecular mass was estimated to be about 61.5 kD by SDS-PAGE,and 57.14 kD by mass spectroscopy.The isoelectric temperature and pH of the enzyme activity were 55 ℃ and 6.0 respectively.The isoelectric point was 4.02.Its N-terminal sequence was VIGPAAPL. The carbohydrate content was 56.2% by the phenol-sulfuric acid method. Michaelis constant of the enzyme was 14.5 μmol•L^-1.The enzyme activity was stable under 45 ℃ and in the pH range of 3.0—9.5. The activity was enhanced by Zn²⁺、Ca²⁺、Ba²⁺ and Mn²⁺,and was strongly inhibited by Hg²⁺、Co²⁺ and Fe²⁺.EDTA also inhibited the activity.Ser was the possible essential residue for enzyme activity.