Chitobiase from Aeromonas salmonicida YA7-625 was purified from culture broth through ammonium sulfate precipitation, chitin affinity adsorption, hydroxylapatite column chromatography and gel filtration, with 47.2% yield and 31.5 fold purity. The molecular weight of purified chitobiase was 15,000 daltons, and the chitobiase showes maximum activity at the condition of at 40¡É and pH 6.0. The effects of various metal ions and inhibitors show thatcystein, glutamic acid, serine, tryptophan, and tyrosine residues seem to be cencerned in chitobiase activity.
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