Skip to Main content Skip to Navigation
Journal articles

Investigating the Product Profiles and Structural Relationships of New Levansucrases with Conventional and Non-Conventional Substrates

Abstract : The synthesis of complex oligosaccharides is desired for their potential as prebiotics, and their role in the pharmaceutical and food industry. Levansucrase (LS, EC 2.4.1.10), a fructosyl-transferase, can catalyze the synthesis of these compounds. LS acquires a fructosyl residue from a donor molecule and performs a non-Lenoir transfer to an acceptor molecule, via β-(2→6)-glycosidic linkages. Genome mining was used to uncover new LS enzymes with increased transfructosylating activity and wider acceptor promiscuity, with an initial screening revealing five LS enzymes. The product profiles and activities of these enzymes were examined after their incubation with sucrose. Alternate acceptor molecules were also incubated with the enzymes to study their consumption. LSs from Gluconobacter oxydans and Novosphingobium aromaticivorans synthesized fructooligosaccharides (FOSs) with up to 13 units in length. Alignment of their amino acid sequences and substrate docking with homology models identified structural elements causing differences in their product spectra. Raffinose, over sucrose, was the preferred donor molecule for the LS from Vibrio natriegens, N. aromaticivorans, and Paraburkolderia graminis. The LSs examined were found to have wide acceptor promiscuity, utilizing monosaccharides, disaccharides, and two alcohols to a high degree.
Complete list of metadatas

Cited literature [55 references]  Display  Hide  Download

https://www.hal.inserm.fr/inserm-02913693
Contributor : Alexandre G. de Brevern <>
Submitted on : Monday, August 10, 2020 - 11:31:34 AM
Last modification on : Tuesday, November 3, 2020 - 11:18:02 AM

Identifiers

Collections

Citation

Andrea Hill, Salwa Karboune, Tarun Narwani, Alexandre de Brevern. Investigating the Product Profiles and Structural Relationships of New Levansucrases with Conventional and Non-Conventional Substrates. International Journal of Molecular Sciences, MDPI, 2020, 21 (15), pp.5402. ⟨10.3390/ijms21155402⟩. ⟨inserm-02913693⟩

Share

Metrics

Record views

26

Files downloads

48