| Abstract
| - Enzymatic approaches for the preparation of oligosaccharides are interesting alternatives totraditional chemical synthesis, the main advantage being the regio- and stereoselectivity offeredwithout the need for protecting groups. The use of solid-phase techniques offers easy workupprocedures and the prospect of automatability. Here, we report the first application of glycosynthasesto solid-phase oligosaccharide synthesis by use of the 51 kDa serine and glycine mutants ofAgrobacterium sp. β-glucosidase, Abg E358S and E358G. Acceptors were linked to PEGA resinthrough a backbone amide linker (BAL), and using these mutated enzymes, a galactose moietywas transferred from a donor sugar, α-d-galactosyl fluoride, with high efficiency (>90%) togetherwith excellent recovery of material. Furthermore, it was demonstrated that a resin-bound modelglycopeptide was also an acceptor for the glycosynthase.
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