Enzymatic synthesis of some O-beta-D-digalactosyl glycopeptides, using beta-D-galactosidase.
Disaccharide-peptide conjugates were obtained in yields of 30-50% from o-nitrophenyl beta-D-galactopyranoside by employing beta-D-galactosidase from E. coli as catalyst. Two series of beta-D-galactosyldipeptides were examined as galactosyl acceptors. They both contain an L-serine residue beta-linked to the anomeric carbon of galactose. In the first series, serine is in the N-terminal position of the dipeptide; in the second series, serine is in the C-terminal position. The second amino acid is L-alanine or glycine. Some of our substrates gave a high yield of beta-(1-->3)-digalactosyldipeptide derivatives and all gave very little of the beta-(1-->6) regioisomer. The conditions and the limitations of the transgalactosylation reaction are discussed.[1]References
- Enzymatic synthesis of some O-beta-D-digalactosyl glycopeptides, using beta-D-galactosidase. Bay, S., Namane, A., Cantacuzene, D. Carbohydr. Res. (1993) [Pubmed]
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