| RRC ID |
7012
|
| 著者 |
Miwa M, Horimoto T, Kiyohara M, Katayama T, Kitaoka M, Ashida H, Yamamoto K.
|
| タイトル |
Cooperation of β-galactosidase and β-N-acetylhexosaminidase from bifidobacteria in assimilation of human milk oligosaccharides with type 2 structure.
|
| ジャーナル |
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.
|
| 巻・号 |
20(11)
|
| ページ |
1402-9
|
| 公開日 |
2010-11-1
|
| 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 |
4.06
|
| 引用数 |
68
|
|
WOS 分野
|
BIOCHEMISTRY & MOLECULAR BIOLOGY
|
| リソース情報 |
| 一般微生物 |
JCM 1254
JCM 7054
JCM 12489
JCM 1192
JCM 1205
JCM 1217
JCM 1222
JCM 7004
JCM 1255
JCM 1275
JCM 10602
JCM 8224
JCM 1194
JCM 7096
JCM 1200
JCM 5824
JCM 6421
JCM 10261
JCM 10541
JCM 10539
JCM 6567
JCM 8732
JCM 8733 |
