Mode of Action of β-Glucuronidase from Aspergillus niger on the Sugar Chains of Arabinogalactan-Protein

  • HAQUE Md. Ashraful
    Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University
  • KOTAKE Toshihisa
    Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University
  • TSUMURAYA Yoichi
    Department of Biochemistry and Molecular Biology, Faculty of Science, Saitama University

書誌事項

タイトル別名
  • Mode of Action of .BETA.-Glucuronidase from Aspergillus niger on the Sugar Chains of Arabinogalactan-Protein
  • Mode of Action of ベータ Glucuronidase from Aspergillus niger on the Sugar Chains of Arabinogalactan Protein
  • Mode of Action of β-Glucuronidase from<i>Aspergillus niger</i>on the Sugar Chains of Arabinogalactan-Protein

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A β-glucuronidase purified from a commercial pectolytic enzyme preparation of Aspergillus niger hydrolyzed about half of the 4-O-methyl-glucuronic acid (4-Me-GlcA) residues located at the nonreducing terminals of (1→6)-linked β-galactosyl side chains of the carbohydrate portion of a radish arabinogalactan-protein (AGP) modified by treatment with fungal α-L-arabinosidase. Digestion of the α-L-arabinosidase-treated AGP with exo-β-(1→3)-galactanase released, by exo-fission of β-(1→3)-galactosidic bonds in the backbone chains of the AGP, neutral β-(1→6)-galactooligosaccharides with various chain lengths and their acidic derivatives substituted at their nonreducing terminals with 4-Me-β-GlcA groups. In contrast, successive digestion of the α-L-arabinosidase-treated AGP with β-glucuronidase followed by exo-β-(1→3)-galactanase liberated much higher amounts of β-(1→6)-galactooligomers together with a small portion of short acidic oligomers, mainly 4-Me-β-GlcA-(1→6)-Gal and 4-Me-β-GlcA-(1→6)-β-Gal-(1→6)-Gal. These results indicate that β-glucuronidase acts upon 4-Me-β-GlcA residues in long (1→6)-linked β-galactosyl side chains of the AGP, whereas short acidic side chains survive the attack of the enzyme.

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