O-glycosylation of dipeptides using β-galactosidase activity ofAchatina achatinadigestive juice

✍ Scribed by Sylvie Leparoux; Marc Padrines; Yannick Fortun; Bernard Colas

• Publisher: Springer Netherlands
• Year: 1996
• Tongue: English
• Weight: 273 KB
• Volume: 18
• Category: Article
• ISSN: 0141-5492
• DOI: 10.1007/bf00128666

✦ Synopsis

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.