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Novelβ-D-Galactofuranose-containing High-mannose Type Oligosaccharides in Ascorbate Oxidase fromAcremoniumsp. HI-25
Author(s) -
Masaya Ohta,
Emi Shinichi,
Hiroyuki Iwamoto,
Junzo Hirose,
Keitarō Hiromi,
Itoh Homare,
Shin Takashi,
Sawao Murao,
Fumito Matsuura
Publication year - 1996
Publication title -
bioscience biotechnology and biochemistry
Language(s) - Uncategorized
Resource type - Journals
SCImago Journal Rank - 0.509
H-Index - 116
eISSN - 1347-6947
pISSN - 0916-8451
DOI - 10.1271/bbb.60.1123
Subject(s) - exoglycosidase , chemistry , dehydroascorbic acid , mannose , hydrolysis , oligosaccharide , ascorbic acid , oxidase test , biochemistry , stereochemistry , enzyme , glycan , glycoprotein , food science
Ascorbate oxidase from the fungus Acremonium sp. HI-25 is a copper-containing glycoprotein that catalyzes the oxidation of ascorbic acid to dehydroascorbic acid. Monosaccharide composition analysis showed that the enzyme contains exclusively N-linked oligosaccharide chains. Following liberation by hydrazinolysis/re-N-acetylation, and fractionation by HPLC on anion exchange. Amide-80 and/or octadecyl silica columns after derivatization with p-aminobenzoic ethyl ester, the structures of the twelve major neutral oligosaccharides were identified by FAB-MS, 400 MHz 1H-NMR, methylation analysis, mild acid hydrolysis, and/or sequential exoglycosidase digestions. Acremonium sp. ascorbate oxidase was found to consist of high-mannose type oligosaccharides (76.3%) having 4 to 9 mannose residues and a series of novel D-galactofuranose-containing high-mannose type oligosaccharides (18.6%) with the following structure.

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