maltooctaose has been researched along with maltohexaose* in 3 studies
3 other study(ies) available for maltooctaose and maltohexaose
| Article | Year |
|---|---|
Donor substrate specificity of 4-alpha-glucanotransferase of porcine liver glycogen debranching enzyme and complementary action to glycogen phosphorylase on debranching.
Glycogen debranching enzyme (GDE) has both 4-alpha-glucanotransferase and amylo-alpha-1,6-glucosidase activities. Here, we examined 4-alpha-glucanotransferase action of porcine liver GDE on four 6(4)-O-alpha-maltooligosyl-pyridylamino(PA)-maltooctaoses, in the presence or absence of an acceptor, maltohexaose. HPLC analysis of digested fluorogenic branched dextrins revealed that in the presence or absence of acceptor, 6(4)-O-alpha-glucosyl-PA-maltooctaose (B4/81) was liberated from 6(4)-O-alpha-maltopentaosyl-PA-maltooctaose (B4/85), 6(4)-O-alpha-maltotetraosyl-PA-maltooctaose (B4/84) and 6(4)-O-alpha-maltotriosyl-PA-maltooctaose (B4/83), whereas 6(4)-O-alpha-maltosyl-PA-maltooctaose (B4/82) was resistant to the enzyme. The fluorogenic product was further hydrolyzed by amylo-alpha-1,6-glucosidase to PA-maltooctaose (G8PA) and glucose. The ratio of the rates of 4-alpha-glucanotransferase actions on B4/85, B4/84 and B4/83 in the absence of the acceptor was 0.15, 0.42 and 1.00, respectively. The rates increased with increasing amounts of acceptor, changing the ratio of the rates to 0.09, 1.00 and 0.60 (with 0.5 mM maltohexaose) and 0.10, 1.00 and 0.58 (with 1.0 mM maltohexaose), respectively. Donor substrate specificity of GDE 4-alpha-glucanotransferase suggests complementary action of GDE and glycogen phosphorylase on glycogen degradation in the porcine liver. Glycogen phosphorylase degrades the maltooligosaccharide branches of glycogen by phosphorolysis to form maltotetraosyl branches, and phosphorolysis does not proceed further. GDE 4-alpha-glucanotransferase removes a maltotriosyl residue from the maltotetraosyl branch such that the alpha-1,6-linked glucosyl residue is retained. Topics: Animals; Binding Sites; Chromatography, High Pressure Liquid; Dextrins; Glycogen Debranching Enzyme System; Glycogen Phosphorylase; Glycoside Hydrolases; Kinetics; Liver; Oligosaccharides; Substrate Specificity; Swine | 2008 |
Enzymatic preparation of maltohexaose, maltoheptaose, and maltooctaose by the preferential cyclomaltooligosaccharide (cyclodextrin) ring-opening reaction of Pyrococcus furiosus thermostable amylase.
Specific-length maltooligosaccharides, particularly maltohexaose, maltoheptaose, and maltooctaose, were prepared from cyclomaltooligosaccharides (cyclodextrins, CDs) by the preferential cyclodextrin ring-opening reaction of an amylolytic enzyme from Pyrococcus furiosus. The enzyme primarily produces maltohexaose, maltoheptaose, and maltooctaose by hydrolyzing alpha-, beta-, and gamma-CD, respectively. This study aims to develop a high-efficiency synthesis of specific maltooligosaccharides at high-purity. [formula: see text] Topics: Amylases; Chromatography, Thin Layer; Cyclodextrins; Enzyme Stability; Glucans; Hot Temperature; Kinetics; Oligosaccharides; Pyrococcus furiosus | 2006 |
Transfer reactions catalyzed by cyclodextrin glucosyltransferase using 4-thiomaltosyl and C-maltosyl fluorides as artificial donors.
Cyclodextrin glycosyltransferase enzyme from Bacillus circulans catalyzed the effective conversion of 4-thio-alpha-maltosyl fluoride into cyclo-alpha-(1-->4(2))-thiomalto -tetraoside, -pentaoside, -hexaoside and linear hemithiomaltooligosaccharides. However, under the same conditions, C-maltosyl fluoride afforded only linear modified maltotetraose, maltohexaose and maltooctaose in moderate yield. Topics: Bacillus; Carbohydrate Sequence; Fluorine Compounds; Glucosyltransferases; Kinetics; Maltose; Molecular Sequence Data; Oligosaccharides | 1997 |