RRC ID 7012
Author Miwa M, Horimoto T, Kiyohara M, Katayama T, Kitaoka M, Ashida H, Yamamoto K.
Title Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.
Journal Glycobiology
Abstract Bifidobacteria are predominant in the intestines of breast-fed infants and offer health benefits to the host. Human milk oligosaccharides (HMOs) are considered to be one of the most important growth factors for intestinal bifidobacteria. HMOs contain two major structures of core tetrasaccharide: lacto-N-tetraose (Galβ1-3GlcNAcβ1-3Galβ1-4Glc; type 1 chain) and lacto-N-neotetraose (Galβ1-4GlcNAcβ1-3Galβ1-4Glc; type 2 chain). We previously identified the unique metabolic pathway for lacto-N-tetraose in Bifidobacterium bifidum. Here, we clarified the degradation pathway for lacto-N-neotetraose in the same bifidobacteria. We cloned one β-galactosidase (BbgIII) and two β-N-acetylhexosaminidases (BbhI and BbhII), all of which are extracellular membrane-bound enzymes. The recombinant BbgIII hydrolyzed lacto-N-neotetraose into Gal and lacto-N-triose II, and furthermore the recombinant BbhI, but not BbhII, catalyzed the hydrolysis of lacto-N-triose II to GlcNAc and lactose. Since BbgIII and BbhI were highly specific for lacto-N-neotetraose and lacto-N-triose II, respectively, they may play essential roles in degrading the type 2 oligosaccharides in HMOs.
Volume 20(11)
Pages 1402-9
Published 2010-11
DOI 10.1093/glycob/cwq101
PII cwq101
PMID 20581010
MeSH Bifidobacterium / enzymology* Carbohydrate Conformation Cloning, Molecular Humans Hydrolysis Milk, Human / metabolism* Oligosaccharides / chemistry Oligosaccharides / metabolism* Substrate Specificity beta-Galactosidase / metabolism* beta-N-Acetylhexosaminidases / genetics beta-N-Acetylhexosaminidases / metabolism*
IF 3.664
Times Cited 43
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