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J. Biochem, 1970, Vol. 68, No. 1 109-117
© 1970 Japanese Biochemical Society

research-article

Studies on N-Acetyl-ß-D-glucosaminidase of Aspergillus oryzae

1. Purification and Characterization of N-Acety-ß-D-glucosaminidase Obtained from Takadiastase

Tomohiro MEGA, Tokuji IKENAKA and Yoshio MATSUSHIMA

The Department of Chemistry, Osaka University College of Science Toyonaka

1. N-Acetyl-ß-D-glucosaminidase [EC 3.2.1.30 [EC] ] was isolated from Takadiastase Sankyo by means of several purificastion methods.

2. The purified enzyme was shown to be homogeneous by disc electrophoresis and ultracentrifugation.

3. The molecular weight of the enzyme was determined to be 140,00–146.000 by equilibrium ultracentrifugation.

4. The enzyme was a glycoprotein, and the amino acid and sugar composition of this enzyme was determined.

5. N-Acetyl-ß-D-galactosaminidase activity was found in water extract of Takadiastase and the two activities were not sparated from each other.

6. The Km and pH optimum of the enzyme were determined by using I-nitrophenyl and phenyl N-acetyl-ß-D-glucosaminides and phenyl N-acetyl-ß-D-galactosaminide as substrates.


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