Efficient chemoenzymatic synthesis of globotriose and its derivatives with a recombinant α-(1→4)-galactosyltransferase Original Research Article

A truncated α-(1→4)-galactosyltransferase (LgtC) gene from Neisseria meningitidis was cloned. The recombinant glycosyltransferase was expressed in Escherichia coli BL21 (DE3) strain with high specific activity (5 units/mg protein). Its acceptor specificity was carefully characterized. Then the purified enzyme was utilized in highly efficient syntheses of globotriose and a variety of α-(1→4)-galactosylated derivatives as potential antibacterial agents.