INVITRO ACTION OF HUMAN AND PORCINE ALPHA-AMYLASES ON CYCLOMALTOOLIGOSACCHARIDES

The vitro action of human and porcine pancreatic α-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 (γ-cyclodextrin) was hydrolyzed to produce mainly maltose, but cyclomalto-hexaose and -heptaose were little affected both by human and porcine α-amylases. Quantitative analysis of reducing power revealed that the ring-opening rate of γ-cyclodextrin catalyzed by human pancreatic α-amylase was 2.8 times slower than that catalyzed by the porcine enzyme. The number of multiple attacks on γ-cyclodextrin and its inhibitor constants for human pancreatic α-amylase and porcine pancreatic α-amylase were almost the same. © 1990.