The transglycosylation activity of P-galactosidase from Achatina uchutina digestive juice was tested for glycosylating protected hydroxy amino acids. Attractive yields of ~-galactosyl-(ZSer-OMe) (35%) and P-galactosyl-(Z-Hyp-OMe) (28%) could be obtained using lactose as glycosyl donor and the corresponding amino acid methyl esters N-protected by a benzyloxycarbonyl group (Z) as glycosyl acceptors.
Enzymatic O-glycosylation of dipeptide derivatives containing a serine residue in the N or C terminal position and alanine or glycine as the second amino acid was achieved using the transgalactosylation activity of [3-galactosidase from the Achatina achatina digestive juice. Reactions were performed with lactose as glycosyl donor and the dipeptide ethyl (or methyl) esters N-protected by a benzyloxycarbonyl group (Z) as glyeosyl acceptors. Yields of galactosyl-dipeptide derivatives were much higher than those obtained with the E.coli 13-galactosidase as catalyst.
scite is a Brooklyn-based organization that helps researchers better discover and understand research articles through Smart Citations–citations that display the context of the citation and describe whether the article provides supporting or contrasting evidence. scite is used by students and researchers from around the world and is funded in part by the National Science Foundation and the National Institute on Drug Abuse of the National Institutes of Health.