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Journal article

A healthy Bifidobacterium dentium caramel cocktail

From

Enzyme Engineering and Structural Biology, Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark1

Novo Nordisk Foundation Center for Biosustainability, Technical University of Denmark2

Enzyme and Protein Chemistry, Section for Protein Chemistry and Enzyme Technology, Department of Biotechnology and Biomedicine, Technical University of Denmark3

Department of Biotechnology and Biomedicine, Technical University of Denmark4

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, α FFase1, from the caries-associated bacterium Bifidobacterium dentium. α FFase1 reversibly forms a potential prebiotic also found in caramel, difructose dianhydride I (DFA 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 α FFase1 that establishes the new glycoside hydrolase family GH172.

Language: English
Year: 2022
Pages: 101452
ISSN: 1083351x , 00219258 and 10678816
Types: Journal article
DOI: 10.1016/j.jbc.2021.101452
ORCIDs: Teze, David and Svensson, Birte

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