Studies on the Chitinolytic Enzymes of Black-koji Mold

Part V. Participation of Two Different Enzymes in the Decomposition of Glycol Chitin to Constituent Aminosugar

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In an attempt to separate the enzyme system participating in the decomposition of glycol chitin to constituent aminosugar, the purification of chitinase of Aspergillus niger was carried out by detemining both liquefying and saccharifying activities. Using fractionation with ammonium sulfate and column chromatography by hydroxylapatite, the chitinase system of the mold was separated into different enzyme fractions, which were required for the complete hydrolysis of glycol chitin. It was found that one of these enzymes caused a rapid decrease in viscosity of glycol chitin solution, another enzyme possessed N-acetyl-β-glucosaminidase activity upon N, N'-diacetylchitobiose and β-methyl-N-acetylglucosaminide. and that glycol chitin was decomposed to constituent aminosugar by a successive action of the two different enzymes.