Specificity of amylases and cyclodextrin-glucanotransferase in reactions with 2-deoxy-maltooligosaccharides.
2-Deoxy-maltooligosaccharides of different chain length were tested as substrates for exo- and endo-amylases. Cleavage occurred with beta-amylase, yielding 2,2'-dideoxy-maltose, and with amyloglucosidase. With the alpha-amylase from Thermomonospora curvata tris-(2-deoxy)-maltotriose and the corresponding tetra- and pentasaccharides were formed. Porcine pancreatic alpha-amylase did not tolerate the deoxygenated substrate, nor 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.
Evers
B
B
Institut für Organische Chemie, Universität Hamburg, Germany.
Petríćek
M
M
Thiem
J
J
D000681:Amylases / Q000737:chemistry*; D005964:Glucosyltransferases / Q000737:chemistry*; D009844:Oligosaccharides / Q000737:chemistry*; D013379:Substrate Specificity
D009844:Oligosaccharides; C021705:maltooligosaccharides; D005964:Glucosyltransferases; C019963:cyclomaltodextrin glucanotransferase; D000681:Amylases