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A healthy Bifidobacterium dentium caramel cocktail

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 reve...

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Detalles Bibliográficos
Autores principales: Teze, David, Svensson, Birte
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Society for Biochemistry and Molecular Biology 2021
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8718956/
https://www.ncbi.nlm.nih.gov/pubmed/34838821
http://dx.doi.org/10.1016/j.jbc.2021.101452
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author Teze, David
Svensson, Birte
author_facet Teze, David
Svensson, Birte
author_sort Teze, David
collection PubMed
description 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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spelling pubmed-87189562022-01-07 A healthy Bifidobacterium dentium caramel cocktail Teze, David Svensson, Birte J Biol Chem Editors' Pick Highlight 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. American Society for Biochemistry and Molecular Biology 2021-11-25 /pmc/articles/PMC8718956/ /pubmed/34838821 http://dx.doi.org/10.1016/j.jbc.2021.101452 Text en © 2021 The Authors https://creativecommons.org/licenses/by/4.0/This is an open access article under the CC BY license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Editors' Pick Highlight
Teze, David
Svensson, Birte
A healthy Bifidobacterium dentium caramel cocktail
title A healthy Bifidobacterium dentium caramel cocktail
title_full A healthy Bifidobacterium dentium caramel cocktail
title_fullStr A healthy Bifidobacterium dentium caramel cocktail
title_full_unstemmed A healthy Bifidobacterium dentium caramel cocktail
title_short A healthy Bifidobacterium dentium caramel cocktail
title_sort healthy bifidobacterium dentium caramel cocktail
topic Editors' Pick Highlight
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8718956/
https://www.ncbi.nlm.nih.gov/pubmed/34838821
http://dx.doi.org/10.1016/j.jbc.2021.101452
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