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An extracellular chitinase of the selected strong antifungal microorganism, Serratia sp. 3095, was purified by salting out, affinity adsorption, Sepadex G-100 gel fitration, Sepadex G-75 gel fitration and DEAE Sepadex A-50 chromatography. The molecular weight of the purified chitinase was estimated to be 62,000 dalton by SDS-PAGE. Optimal pH and temperature of the chitinase were pH 7.5 and 45, respectively. The enzyme retained more than 80% of the activity between pH 5.5 and pH 10.5, and below 50℃ but was unstable above 60℃, below pH 5.0. The activity of the chitinase was inhibited about 60% by Sn^(2+), 40% by Hg^(2+) and Ag^+, 70% by AHA, 40% by iodoacetate, 35% by thiourea and p-CMB, but stabilized by SDS. K_m value of the purified chitinase was 3.68 ㎎/㎖ for colloidal chitin. The chitinase from Serratia sp. 3095 showed antifungal activity to Fusariurm solani.
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