期刊
GLYCOCONJUGATE JOURNAL
卷 27, 期 1, 页码 125-132出版社
SPRINGER
DOI: 10.1007/s10719-009-9247-8
关键词
Bifidobacteria; Endoglycosidase; GH101; Mucin; O-glycan; Prebiotics
资金
- Promotion of Basic Research Activities for Innovative Biosciences (PROBRAIN)
- Ajinomoto Co., Inc.
Endo-alpha-N-acetylgalactosaminidase catalyzes the release of Gal beta 1-3GalNAc from the core 1-type O-glycan (Gal beta 1-3GalNAc alpha 1-Ser/Thr) of mucin glycoproteins and synthetic p-nitrophenyl (pNP) alpha-linked substrates. Here, we report the enzymatic syntheses of core 1 disaccharide-containing glycopeptides using the transglycosylation activity of endo-alpha-N-acetylgalactosaminidase (EngBF) from Bifidobacterium longum. The enzyme directly transferred Gal beta 1-3GalNAc to serine or threonine residues of bioactive peptides such as PAMP-12, bradykinin, peptide-T and MUC1a when Gal beta 1-3GalNAc alpha 1-pNP was used as a donor substrate. The enzyme was also found to catalyze the reverse-hydrolysis reaction. EngBF synthesized the core 1 disaccharide-containing oligosaccharides when the enzyme was incubated with either glucose or lactose and Gal beta 1-3GalNAc prepared from porcine gastric mucin using bifidobacterial cells expressing endo-alpha-N-acetylgalactosaminidase. Synthesized oligosaccharides are promising prebiotics for bifidobacteria.
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