SPECIFICITY OF AMYLASES AND CYCLODEXTRIN-GLUCANOTRANSFERASE IN REACTIONS WITH 2-DEOXY-MALTOOLIGOSACCHARIDES

2-Deoxy-maltooligosaccharides of different chain length were tested as substrates for exoand endo-amylases. Cleavage occurred with beta-amyl ase, yielding 2,2'-dideoxy-maltose, and with amyloglucosidase. With th e alpha-amylase from Thermomonospora curvata tris-(2-deoxy)-maltotrios e and the corresponding tetra- and pentasaccharides were formed. Porci ne pancreatic a-amylase did not tolerate the deoxygenated substrate, n or were cyclization experiments with cyclodextrin-glucanotransferase ( CGT) successful. In a coupling reaction with CGT, however, a series of transfer products to the acceptor 2-deoxyglucose were obtained. (C) 1 997 Elsevier Science Ltd.