Studies on the Chitinolytic Enzymes of Black-koji Mold

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  • Part IV. Action of the Liquefying Chitinase on Glycol Chitin

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The mode of degradation of glycol chitin by the liquefying chitinase of Aspergillus niger was invetsigated. Glycol chitin was rapidly cleaved to glycol chitodextrin and oligosaccharides, without formation of detectable amounts of monosaccharide. The enzyme attacked glycol chitodextrin as well as glycol chitin, but the rate of degradation was slower in the former than in the latter. Glycol chitosan, deacetylated compound, was not splitted. Activity of this enzyme preparation on N, N'-diacetylchitobiose and β-methyl-N-acetylglucosaminide was weak. Therefore, it is presumed that the liquefying chitinase degrade the glucosaminidic bonds at random in the interior of the polysaccharide chain.

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