1997 Volume 61 Issue 7 Pages 1146-1149
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 β-amylase treatment, five species of glycosyl-trehaloses were isolated by column chromatography. After chemical and enzymatic analyses, it was concluded that these oligosaccharides were α-maltosyl α-D-glucopyranoside, α-maltotriosyl α-D-glucopyranoside, α-maltosyl α-maltoside, α-maltotriosyl α-maltoside, and α-maltotriosyl α-maltotrioside. These were not hydrolyzed by salivary amylase, artificial gastric juice, or pancreatic amylase, however they were hydrolyzed by enzymes of the small intestine.
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