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Mode of action of beta-glucuronidase from Aspergillus niger on the sugar chains of arabinogalactan-protein.
- Source :
-
Bioscience, biotechnology, and biochemistry [Biosci Biotechnol Biochem] 2005 Nov; Vol. 69 (11), pp. 2170-7. - Publication Year :
- 2005
-
Abstract
- A beta-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 beta-galactosyl side chains of the carbohydrate portion of a radish arabinogalactan-protein (AGP) modified by treatment with fungal alpha-L-arabinosidase. Digestion of the alpha-L-arabinosidase-treated AGP with exo-beta-(1-->3)-galactanase released, by exo-fission of beta-(1-->3)-galactosidic bonds in the backbone chains of the AGP, neutral beta-(1-->6)-galactooligosaccharides with various chain lengths and their acidic derivatives substituted at their nonreducing terminals with 4-Me-beta-GlcA groups. In contrast, successive digestion of the alpha-L-arabinosidase-treated AGP with beta-glucuronidase followed by exo-beta-(1-->3)-galactanase liberated much higher amounts of beta-(1-->6)-galactooligomers together with a small portion of short acidic oligomers, mainly 4-Me-beta-GlcA-(1-->6)-Gal and 4-Me-beta-GlcA-(1-->6)-beta-Gal-(1-->6)-Gal. These results indicate that beta-glucuronidase acts upon 4-Me-beta-GlcA residues in long (1-->6)-linked beta-galactosyl side chains of the AGP, whereas short acidic side chains survive the attack of the enzyme.
Details
- Language :
- English
- ISSN :
- 0916-8451
- Volume :
- 69
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Bioscience, biotechnology, and biochemistry
- Publication Type :
- Academic Journal
- Accession number :
- 16306699
- Full Text :
- https://doi.org/10.1271/bbb.69.2170