Glycosylhydrolases of various origins were used to produce fucose-containing disaccharides with prebiotic potential using different donor substrates and L-fucose as the acceptor substrate. Eight different disaccharides were synthesized as follows: three β-D-galactosyl-L-fucosides with glycosidase CloneZyme Gly-001-02 using D-lactose as a donor substrate, two with a structure similar to prebiotics; one β-D-galactosyl-L-fucose with β-D-galactosidase from Aspergillus oryzae using D-lactose as a substrate donor; and four α-D-glucosyl-L-fucosides with α-D-glucosidase from Saccharomyces cerevisiae using D-maltose as a donor substrate. All disaccharides were purified and hydrolyzed. In all cases, an L-fucose moiety was present, and it was confirmed for β-D-galactosyl-L-fucose by mass spectrometry. High concentrations of L-fucose as the acceptor substrate enhanced the synthesis of the oligosaccharides in all cases. The three enzymes were able to synthesize fucose-containing disaccharides when L-fucose was used as the acceptor substrate, and the highest yield was 20% using β-D-galactosidase from Aspergillus oryzae.
Keywords: Disaccharides synthesis; Fucose-containing disaccharides; Glycosylhydrolases; Transglycosylation.