Structural studies on the O-glycosidically linked carbohydrate chains of glucoamylase G1 from Aspergillus niger

A. Gunnarsson, Birte Svensson, B. Nilsson, S. Svendsson

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Glucoamylase G1 from Aspergillus niger contains an unusual type of carbohydrate-protein linkage, involving mannose O-glycosidically linked to serine and threonine. The majority of the neutral oligosaccharides of glucoamylase G1 are located in a region of about 70 amino acid residues which carries about 35 oligosaccharide units [(1983) Carlsberg Res. Commun. 48, 517-527]. Structural analysis was performed on the O-linked carbohydrates of a tryptic fragment from glucoamylase G1 comprising the segment characterized by a high degree of glycosylation. The carbohydrate structures released by trifluoroacetolysis were elucidated using sugar analysis, methylation analysis, mass spectrometry, chromium trioxide oxidation, digestion with alpha-mannosidase and 1H-NMR spectroscopy. The following structures could be identified.
Original languageEnglish
JournalEuropean Journal of Biochemistry
Volume145
Pages (from-to)463-467
ISSN0014-2956
Publication statusPublished - 1984
Externally publishedYes

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