Journal of Bioscience and Bioengineering, Vol.91, No.1, 85-87, 2001
Production and characterization of active soluble human beta 1, 4-galactosyltransferase in Escherichia coli as a useful catalyst in synthesis of the Gal beta 1 -> 4 GlcNAc linkage
An active and soluble human beta1,4-galactosyltransferase (beta -GT) was produced in Escherichia coli using a maltose-binding protein fusion system. The purified recombinant beta -GT has a K-m value of 0.035 mM for UDP-galactose and a V-max of 643 x 10(3) nmol/mg/h. The enzyme catalyzes the transfer of galactose from UDP-galactose to N-linked oligosaccharides. The properties of the purified enzyme were identical to those of bovine milk beta -GT.