Abstract
The measurement of N-acetyl-β-glucosaminidase activity upon β-MAGA* was carried out in order to survey oligosaccharidase fraction in the chitinolytic enzymes of Aspergillus niger. N-Acetyl-β-glucosaminidase was purified in parallel with chitobiase activity, being separated from chitinase activity, and some properties of the enzyme in the hydrolysis of β-MAGA and DACB were investigated. The enzyme hydrolysed more rapidly β-glucosaminidic bonds in DACB than that in β-MAGA, but did not decompose α-MAGA.
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