N-Acetylglucosaminidase from Bifidobacterium bifidum specifically hydrolyzes [alpha]-linked N-acetylglucosamine at nonreducing terminus of O-glycan on gastric mucin

[alpha]-Linked N-acetylglucosamine is one of the major glyco-epitopes in O-glycan of gastroduodenal mucin. Here, we identified glycoside hydrolase (GH) family 89 [alpha]-N-acetylglucosaminidase, termed AgnB, from Bifidobacterium bifidum JCM 1254, which is essentially specific to GlcNAc[alpha]1-4Gal...

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Bibliographic Details
Published in:Applied microbiology and biotechnology 2015-05, Vol.99 (9), p.3941
Main Authors: Shimada, Yoshimi, Watanabe, Yuka, Wakinaka, Takura, Funeno, Yoshihisa, Kubota, Masayuki, Chaiwangsri, Thida, Kurihara, Shin, Yamamoto, Kenji, Katayama, Takane, Ashida, Hisashi
Format: Article
Language:English
Subjects:
Analysis
Antigens
Bacteria
Bifidobacteria
Biotechnology
Cloning
DNA polymerase
E coli
Enzymatic activity
Enzymes
Genomes
Microorganisms
Mucins
Physiological aspects
Probiotics
Proteins
Sodium
Studies
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Summary:[alpha]-Linked N-acetylglucosamine is one of the major glyco-epitopes in O-glycan of gastroduodenal mucin. Here, we identified glycoside hydrolase (GH) family 89 [alpha]-N-acetylglucosaminidase, termed AgnB, from Bifidobacterium bifidum JCM 1254, which is essentially specific to GlcNAc[alpha]1-4Gal structure. AgnB is a membrane-anchored extracellular enzyme consisting of a GH89 domain and four carbohydrate-binding module (CBM) 32 domains. Among four CBM32 domains, three tandem ones at C-terminus showed to bind porcine gastric mucin, suggesting that these domains enhance the enzyme activity by increasing affinity for multivalent substrates. AgnB might be important for assimilation of gastroduodenal mucin by B. bifidum and also applicable to production of prebiotic oligosaccharides from porcine gastric mucin.
ISSN:0175-7598
1432-0614
DOI:10.1007/s00253-014-6201-x