• Home
  • Search Results
  • Bifidobacterial α-galactosidase with unique carbohydrate-binding module specifically acts on blood group B antigen.

Bifidobacterial α-galactosidase with unique carbohydrate-binding module specifically acts on blood group B antigen.

Glycobiology (2012-10-24)
Takura Wakinaka, Masashi Kiyohara, Shin Kurihara, Akiko Hirata, Thida Chaiwangsri, Takayuki Ohnuma, Tamo Fukamizo, Takane Katayama, Hisashi Ashida, Kenji Yamamoto
ABSTRACT

Bifidobacterium bifidum is one of the most frequently found bifidobacteria in the intestines of newborn infants. We previously reported that B. bifidum possesses unique metabolic pathways for O-linked glycans on gastrointestinal mucin (Yoshida E, Sakurama H, Kiyohara M, Nakajima M, Kitaoka M, Ashida H, Hirose J, Katayama T, Yamamoto K, Kumagai H. 2012. Bifidobacterium longum subsp. infantis uses two different β-galactosidases for selectively degrading type-1 and type-2 human milk oligosaccharides. Glycobiology. 22:361-368). The nonreducing termini of O-linked glycans on mucin are frequently covered with histo-blood group antigens. Here, we identified a gene agabb from B. bifidum JCM 1254, which encodes glycoside hydrolase (GH) family 110 α-galactosidase. AgaBb is a 1289-amino acid polypeptide containing an N-terminal signal sequence, a GH110 domain, a carbohydrate-binding module (CBM) 51 domain, a bacterial Ig-like (Big) 2 domain and a C-terminal transmembrane region, in this order. The recombinant enzyme expressed in Escherichia coli hydrolyzed α1,3-linked Gal in branched blood group B antigen [Galα1-3(Fucα1-2)Galβ1-R], but not in a linear xenotransplantation antigen (Galα1-3Galβ1-R). The enzyme also acted on group B human salivary mucin and erythrocytes. We also revealed that CBM51 specifically bound blood group B antigen using both isothermal titration calorimetry and a solid-phase binding assay, and it enhanced the affinity of the enzyme toward substrates with multivalent B antigens. We suggest that this enzyme plays an important role in degrading B antigens to acquire nutrients from mucin oligosaccharides in the gastrointestinal tracts.

MATERIALS
Product Number
Brand
Product Description

Sigma-Aldrich
α-Galactosidase from green coffee beans, ammonium sulfate suspension, ≥9 units/mg protein
Sigma-Aldrich
α-Galactosidase, positionally specific from Escherichia coli, recombinant, expressed in E. coli, buffered aqueous solution
Sigma-Aldrich
α-Galactosidase I, Alkaline from Cucumis melo

Social Media

LinkedIn icon
Twitter icon
Facebook Icon
Instagram Icon

MilliporeSigma

Research. Development. Production.

We are a leading supplier to the global Life Science industry with solutions and services for research, biotechnology development and production, and pharmaceutical drug therapy development and production.

© 2021 Merck KGaA, Darmstadt, Germany and/or its affiliates. All Rights Reserved.

Reproduction of any materials from the site is strictly forbidden without permission.