
doi: 10.1271/bbb.61.1146
pmid: 9255978
Cyclomaltodextrin glucanotransferase from Bacillus stearothermophilus produced a series of glycosyl-trehaloses through the transglycosylation reaction with cyclomaltohexaose as the glycosyl donor and trehalose as its acceptor. After beta-amylase treatment, five species of glycosyl-trehaloses were isolated by column chromatography. After chemical and enzymatic analyses, it was concluded that these oligosaccharides were alpha-maltosyl alpha-D-glucopyranoside, alpha-maltotriosyl alpha-D-glucopyranoside, alpha-maltosyl alpha-maltoside, alpha-maltotriosyl alpha-maltoside, and alpha-maltotriosyl alpha-maltotrioside. These were not hydrolyzed by salivary amylase, artificial gastric juice, or pancreatic amylase, however they were hydrolyzed by enzymes of the small intestine.
Optics and Photonics, Glycosylation, Magnetic Resonance Spectroscopy, Hydrolysis, Molecular Sequence Data, Oligosaccharides, Trehalose, Mass Spectrometry, Geobacillus stearothermophilus, Glucose, Carbohydrate Sequence, Glucosyltransferases, Glucan 1,4-alpha-Glucosidase, Chromatography, High Pressure Liquid
Optics and Photonics, Glycosylation, Magnetic Resonance Spectroscopy, Hydrolysis, Molecular Sequence Data, Oligosaccharides, Trehalose, Mass Spectrometry, Geobacillus stearothermophilus, Glucose, Carbohydrate Sequence, Glucosyltransferases, Glucan 1,4-alpha-Glucosidase, Chromatography, High Pressure Liquid
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