In vitro action of human and porcine alpha-amylases on cyclomalto-oligosaccharides
- PMID: 2279246
- DOI: 10.1016/0008-6215(90)84036-t
In vitro action of human and porcine alpha-amylases on cyclomalto-oligosaccharides
Abstract
The vitro action of human and porcine pancreatic alpha-amylases on cyclomalto-oligosaccharides (cyclodextrins) was investigated both by a high-performance liquid chromatographic analysis and a quantitative analysis of the reducing power of cyclodextrin hydrolyzates. Cyclomalto-octaose (gamma-cyclodextrin) was hydrolyzed to produce mainly maltose, but cyclomalto-hexaose and -heptaose were little affected both by human and porcine alpha-amylases. Quantitative analysis of reducing power revealed that the ring-opening rate of gamma-cyclodextrin catalyzed by human pancreatic alpha-amylase was 2.8 times slower than that catalyzed by the porcine enzyme. The number of multiple attacks on gamma-cyclodextrin and its inhibitor constants for human pancreatic alpha-amylase and porcine pancreatic alpha-amylase were almost the same.
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