論文 - 詳細
| RRC ID | 88806 |
|---|---|
| 著者 | Ishiwata A, Shite Y, Kitahara K, Tanaka K, Ito Y, Fujita K. |
| タイトル | Structural analysis of (2 → 1)-β-d-fructofuranosides linked to a terminal difructose dianhydride III produced by Bacteroides endo-type inulin fructotransferase. |
| ジャーナル | Int J Biol Macromol |
| Abstract |
The glycoside hydrolase (GH) family 91 inulin fructotransferase (IFTase) complexes from Bacteroides ovatus and B. caccae act as endo-type IFTases targeting inulin. However, their degradation mechanism remains unclear. Herein, the exact structure of the accumulated inulin-degradation product in a culture supernatant is revealed as linear oligo-(2 → 1)-β-d-fructofuranosides linked to difructose dianhydride III (DFA III) at the reducing end. Additionally, we developed a method to quantify endo-IFTase activity by measuring DFA III released from inulin after sequential treatment with endo-IFTase and GH32 β-d-fructofuranosidase. Using this approach, we investigated the effect of varying concentrations of endo-IFTase subunits 1 and 2 and found that an equimolar mixture of the two subunits exhibited the highest enzymatic activity, indicating that the active complex forms in a 1:1 ratio. The endo-IFTase accepts fructooligosaccharide DP7 (GF6) as the shortest substrate, suggesting that the complex recognizes the region between subsites +3 and - 3. This study provides insights into the understanding of inulin degradation by Bacteroides species and elucidates the molecular mechanisms underlying prebiotic effects of inulin. |
| 巻・号 | 310(Pt 1) |
| ページ | 143064 |
| 公開日 | 2025-5-1 |
| DOI | 10.1016/j.ijbiomac.2025.143064 |
| PII | S0141-8130(25)03616-5 |
| PMID | 40220837 |
| MeSH | Bacterial Proteins Bacteroides* / enzymology Disaccharides* / chemistry Disaccharides* / metabolism Hexosyltransferases* / chemistry Hexosyltransferases* / metabolism Inulin / chemistry Inulin / metabolism Substrate Specificity |
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| 最多言及媒体 | X(Twitter) |
| 各媒体での言及数の合計 | 1 |
| 過去6か月間でのオルトメトリクス指標の変動値 | 0.0 |
| リソース情報 | |
| 一般微生物 | JCM5824 JCM9498 |