A healthy Bifidobacterium dentium caramel cocktail |
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Authors: | David Teze Birte Svensson |
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Affiliation: | 1.Enzyme Engineering and Structural Biology, The Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark, Kgs. Lyngby, Denmark;2.Enzyme and Protein Chemistry, Department of Biotechnology and Biomedicine, Technical University of Denmark, Kgs. Lyngby, Denmark |
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Abstract: | β-d-fructofuranosyl glycosidases are enzymes that produce health-beneficial fructooligosaccharides from natural fructans. In a recent issue of JBC, Kashima et al. identified a novel α-d-fructofuranosyl-active enzyme, αFFase1, from the caries-associated bacterium Bifidobacterium dentium. αFFase1 reversibly forms a potential prebiotic also found in caramel, difructose dianhydride I, via intramolecular condensation of the substrate inulobiose. Kashima et al. elegantly combine NMR, X-ray crystallography, and molecular dynamics to describe an original mechanism for the reversible reactions catalyzed by αFFase1 that establishes the new glycoside hydrolase family GH172. |
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Keywords: | Glycoside hydrolase GH172 caramel prebiotic difructo anhydride enzyme mechanism protein crystallography molecular dynamics CAZy channel |
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