抄録
Purification of chitinase was carried out from wheat-bran culture of black-koji mold, employing fractionation by ammonium sulfate, adsorption on calcium phosphate gel and column chromatography by hydroxylapatite. The enzyme preparation was obtained in a highly purified state and had a powerful property of decreasing the viscosity of glycol chitin solution, being accompanied wtih depolymerization of substrate molecule.
