Galactosylation and glucosylation by use of β-galactosidase

Article abstract of DOI:10.1016/0040-4039(92)88050-F

The transglucosylation activity of β-galactosidase derived from Aspergillus oryzae and Escherichia coli, respectively, was examined in reaction systems containing up to 50% acetonitrile. Starting with ortho-nitrophenyl β-galactoside (1), which functions both as donor and as acceptor, β-Gal(1-6)β-Gal-PhNO₂-o (2) and β-Gal(1-3)β-Gal-PhNO₂-o (3) were obtained. Under similar conditions the enzyme from A. oryzae converts para-nitrophenyl β-glucoside (5) to β-Glc(1-2)β-Glc-PhNO₂-p (6) and α-Glc(1-4)β-Glc-PhNO₂-p (7). Incubation of 1 and L-serine in the presence of the A. oryzae β-galactosidase leads to β-Gal-L-Ser (4).