키틴 분해 효소활성이 높은 균주로 분리동정한 Aeromonas salmonicida YA7-625의 chitobiase를 ammonium sulfate침전, affinity adsorption, DEAE-cellulose chromatography, hydroxylapatite chromatography, gel filtration 과정을 통해 수율 47.2% 및 정제도 31.5로 분리, 정제 하였다. 정제된 chitobiase는 pH6.0, $40^{circ}C$에서 최대의 활성을 나타내었고 분자량은 15,000 daltons로 추정되었다. 금속이온과 저해제들의 효과를 검토결과 효소의 활성에는 cystein, glutamic acid, aspartic acid, serine, tryptophan 및 tyrposine 잔기 등이 관여하는 것으로 유추되었다.
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 $40^{circ}C$ and pH 6.0. The effects of various metal ions and inhibitors show thatcystein, glutamic acid, serine, tryptophan, and tyrosine residues seem to be concerned in chitobiase activity.
