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The synthesis of complex oligosaccharides is desired for their potential asprebiotics, and their role in the pharmaceutical and food industry.Levansucrase (LS, EC 2.4.1.10), a fructosyl-transferase, can catalyze thesynthesis of these compounds. LS acquires a fructosyl residue from a donormolecule and performs a non-Lenoir transfer to an acceptor molecule, via$\beta$-(2$\to$6)-glycosidic linkages. Genome mining was used to uncover new LSenzymes with increased transfructosylating activity and wider acceptorpromiscuity, with an initial screening revealing five LS enzymes. The productprofiles and activities of these enzymes were examined after their incubationwith sucrose. Alternate acceptor molecules were also incubated with the enzymesto study their consumption. LSs from Gluconobacter oxydans and Novosphingobiumaromaticivorans synthesized fructooligosaccharides (FOSs) with up to 13 unitsin length. Alignment of their amino acid sequences and substrate docking withhomology models identified structural elements causing differences in theirproduct spectra. Raffinose, over sucrose, was the preferred donor molecule forthe LS from Vibrio natriegens, N. aromaticivorans, and Paraburkolderiagraminis. The LSs examined were found to have wide acceptor promiscuity,utilizing monosaccharides, disaccharides, and two alcohols to a high degree.

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