Expression and initial characterization of WbbI, a putative<scp>d</scp>-Galf:α-<scp>d</scp>-Glc β-1,6-galactofuranosyltransferase from Escherichia coli K-12

Abstract

Cloning of E. coli K-12 orf8 (wbbI) and over-expression of the corresponding enzyme as a maltose-binding fusion protein provided recombinant WbbI beta-1,6-galactofuranosyltransferase activity. Challenged with synthetic acceptor analogues in the presence of UDP-galactofuranose as a donor, WbbI showed a modest preference for pyranoside acceptor substrates of the alpha-D-gluco-configuration but it also possessed the ability to turn-over acceptor analogues.