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  • Title: Purification and characterization of endo-beta-N-acetylglucosaminidase of Aspergillus oryzae.
    Author: Hitomi J, Murakami Y, Saitoh F, Shigemitsu N, Yamaguchi H.
    Journal: J Biochem; 1985 Aug; 98(2):527-33. PubMed ID: 3934149.
    Abstract:
    An endo-beta-N-acetylglucosaminidase which hydrolyzes the N,N'-diacetylchitobiosyl linkage in asparagine-linked oligosaccharides was purified from the enzyme product of Aspergillus oryzae. Its substrate specificity was similar to that of endo-beta-N-acetylglucosaminidase H from Streptomyces griseus with respect to the relative activities toward the glycopeptides obtained from ovalbumin and bovine IgG. The present endoglycosidase exhibited a broad optimum pH range and was relatively stable. Metal ions, chelating agents and D-mannose did not have a significant effect on the enzyme activity.
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