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

被引:22
|
作者
Shimada, Yoshimi [1 ]
Watanabe, Yuka [2 ]
Wakinaka, Takura [2 ]
Funeno, Yoshihisa [1 ]
Kubota, Masayuki [1 ]
Chaiwangsri, Thida [3 ]
Kurihara, Shin [4 ]
Yamamoto, Kenji [5 ]
Katayama, Takane [4 ]
Ashida, Hisashi [1 ]
机构
[1] Kinki Univ, Fac Biol Oriented Sci & Technol, Wakayama 6496493, Japan
[2] Kyoto Univ, Grad Sch Biostudies, Sakyo Ku, Kyoto 6068502, Japan
[3] Univ Phayao, Sch Med Sci, Phayao 56000, Thailand
[4] Ishikawa Prefectural Univ, Host Microbe Interact Res Lab, Nonoichi, Ishikawa 9218836, Japan
[5] Ishikawa Prefectural Univ, Res Inst Bioresources & Biotechnol, Nonoichi, Ishikawa 9218836, Japan
关键词
alpha-N-Acetylglucosaminidase; Bifidobacterium bifidum; CBM32; GH89; Mucin; Probiotics; HUMAN-MILK OLIGOSACCHARIDES; GLYCOSIDE HYDROLASE FAMILY; CARBOHYDRATE-BINDING MODULE; ENDO-BETA-GALACTOSIDASE; MOLECULAR-CLONING; BIOSE-I; LONGUM; DISACCHARIDE; DEGRADATION; ACETYLGALACTOSAMINIDASE;
D O I
10.1007/s00253-014-6201-x
中图分类号
Q81 [生物工程学(生物技术)]; Q93 [微生物学];
学科分类号
071005 ; 0836 ; 090102 ; 100705 ;
摘要
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.
引用
收藏
页码:3941 / 3948
页数:8
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