Acceptor Specificity of the Transglycosylation Catalyzed by Cyclodextrin Glycosyltransferase

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Abstract
The structural features of the sugars required as an acceptor of cyclodextrin glycosyl-transferases from Bacillus megaterium and B. macerans were investigated using 22 kinds of monosaccharides and their derivatives. It is concluded on the basis of the experimental results that the requirement for an acceptor of the intermolecular transfer reaction catalyzed by this enzyme is the pyranose structure having the same configurations of the free C2-, C3- and C4- hydroxy 1 groups as D-glucopyranose. The reaction products of the B. megaterium enzyme from starch and 2-deoxy-D-glucose, a poor acceptor, were analyzed by paper chromatography. The main product was isolated and identified by the chemical and enzymatic methods as 4-O-α-D-glucopyranosyl-2-deoxy-D-glucose. The products contained a series of ordinary maltooligo- saccharides besides a series of maltooligosaccharides each terminated by a single 4-O-α-D-glucosyl-2-deoxy-D-glucose residue at the reducing end.