Acceptor specificity of cyclodextrin glycosyltransferase from Bacillus stearothermophilus and synthesis of alpha-D-glucosyl O-beta-D-galactosyl-(1----4)-beta-D-glucoside.

Bacillus stearothermophilus CGTase had a wider acceptor specificity than Bacillus macerans CGTase did and produced large amounts of transfer products of various acceptors such as D-galactose, D-mannose, D-fructose, D- and L-arabinose, D- and L-fucose, L-rhamnose, D-glucosamine, and lactose, which were inefficient acceptors for B. macerans CGTase. The main component of the smallest transfer products of lactose was assumed to be alpha-D-glucosyl O-beta-D-galactosyl-(1----4)-beta-D-glucoside.