The first di-D-fructofuranose 1,2′:2,3′-dianhydride hydrolase (DFA-IIIase) from the genus of non-Arthrobacter (pathogen Salmonella enterica subsp. enterica serovar Mbandaka): Molecular cloning, expression, identification, and characterization

Yu, Shuhuai; Wang, Zhenlong; Li, Qiting; Zhao, Wei

doi:10.1016/j.fbio.2023.103093

Cited by 1 publication

(1 citation statement)

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“…We recently reported that DFA-IIIase has a low rate of conversion from DFA-III to inulobiose. 29,30 Probably, the low rate of conversion from DFA to inulobiose is a common characteristic of DFA hydrolase.…”

Section: Identification and Biochemicalmentioning

confidence: 99%

Metabolism of Inulin via Difructose Anhydride I Pathway in Microbacterium flavum

Li,

Wang,

Zhu

et al. 2024

J. Agric. Food Chem.

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Difructose anhydride I (DFA-I) can be produced from inulin, with DFA-I-forming inulin fructotransferase (IFTase-I). However, the metabolism of inulin through DFA-I remains unclear. To clarify this pathway, several genes of enzymes related to this pathway in the genome of Microbacterium flavum DSM 18909 were synthesized, and the corresponding enzymes were encoded, purified, and investigated in vitro. After inulin is decomposed to DFA-I by IFTase-I, DFA-I is hydrolyzed to inulobiose by DFA-I hydrolase. Inulobiose is then hydrolyzed by β-fructofuranosidase to form fructose. Finally, fructose enters glycolysis through fructokinase. A β-fructofuranosidase (MfFFase1) clears the byproducts (sucrose and fructo-oligosaccharides), which might be partially hydrolyzed by fructan β-(2,1)-fructosidase/1-exohydrolase and another fructofuranosidase (MfFFase2). Exploring the DFA-I pathway of inulin and well-studied enzymes in vitro extends our basic scientific knowledge of the energy-providing way of inulin, thereby paving the way for further investigations in vivo and offering a reference for further nutritional investigation of inulin and DFA-I in the future.

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Section: Identification and Biochemicalmentioning

confidence: 99%