Structural analysis of (2 → 1)-β-d-fructofuranosides linked to a terminal difructose dianhydride III produced by Bacteroides endo-type inulin fructotransferase DOI Creative Commons
Akihiro Ishiwata,

Yurina Shite,

Kanefumi Kitahara

и другие.

International Journal of Biological Macromolecules, Год журнала: 2025, Номер unknown, С. 143064 - 143064

Опубликована: Апрель 1, 2025

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 accumulated inulin-degradation product in a culture supernatant is revealed linear oligo-(2 → 1)-β-d-fructofuranosides linked to difructose dianhydride III (DFA III) at reducing end. Additionally, we developed method quantify endo-IFTase activity by measuring DFA released after sequential treatment with GH32 β-d-fructofuranosidase. Using this approach, investigated effect varying concentrations subunits 1 2 found that an equimolar mixture two exhibited highest enzymatic activity, indicating active complex forms 1:1 ratio. accepts fructooligosaccharide DP7 (GF6) shortest substrate, suggesting recognizes region between subsites +3 - 3. This study provides insights into understanding species elucidates molecular mechanisms underlying prebiotic effects

Язык: Английский

Structural analysis of (2 → 1)-β-d-fructofuranosides linked to a terminal difructose dianhydride III produced by Bacteroides endo-type inulin fructotransferase DOI Creative Commons
Akihiro Ishiwata,

Yurina Shite,

Kanefumi Kitahara

и другие.

International Journal of Biological Macromolecules, Год журнала: 2025, Номер unknown, С. 143064 - 143064

Опубликована: Апрель 1, 2025

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 accumulated inulin-degradation product in a culture supernatant is revealed linear oligo-(2 → 1)-β-d-fructofuranosides linked to difructose dianhydride III (DFA III) at reducing end. Additionally, we developed method quantify endo-IFTase activity by measuring DFA released after sequential treatment with GH32 β-d-fructofuranosidase. Using this approach, investigated effect varying concentrations subunits 1 2 found that an equimolar mixture two exhibited highest enzymatic activity, indicating active complex forms 1:1 ratio. accepts fructooligosaccharide DP7 (GF6) shortest substrate, suggesting recognizes region between subsites +3 - 3. This study provides insights into understanding species elucidates molecular mechanisms underlying prebiotic effects

Язык: Английский

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