The mechanism for the coupling reactions catalyzed by CGTase (see Fig. 2) involves first the binding of CD6 at the active site with the opening of the ring by the enzyme and the formation of a covalent, enzyme intermediate, between maltohexaose and the enzyme.16 The acceptors, glucopyranoside glycosides in the present study, then bind adjacent to the covalent, enzyme–maltohexaosyl unit, so that the C-4-OH of the glucoside makes a nucleophilic, SN2 attack onto C-1 of the maltohexanoyl unit, giving an α-(1→4) linkage and the formation of a maltoheptaose glycoside. This first product then undergoes a CGTase catalyzed disproportionation reaction between two maltoheptaose glycoside molecules to eventually give a series of large and small maltodextrin glycosides.1, 4 and 5 At low molar ratios, the large maltodextrin glycosides are substrates for the formation of the higher cyclomaltodextrins, CD7 and CD8. At higher molar ratios, the large maltodextrin glycosides decrease and hence the formation of the cyclomaltodextrins also decreases. It should be noted that for B. macerans CGTase, CD6 is the preferred donor in the coupling reactions, and CD7 and CD8 are very poor donors. 7