Abstract
Characteristic of palatinose-hydrolyzing activity was studied in the sucrase-isomaltase complex purified from adult rat intestine.
1) Palatinose-hydrolyzing activity (specific activity) was increased by purification of sucrase-iso-maltase complex in parallel with sucrase and isomaltase activity.
2) Palatinose was hydrolyzed in competition with isomaltose by sucrase-isomaltase complex.
3) Palatinose-hydrolyzing activity, like isomaltase activity, was not inhibited by α-glucosidase inhibitor, acarbose, which inhibits sucrase and maltase activity.
Therefore, we concluded that palatinose is hydrolyzed by the active site of isomaltase of sucrase-isomaltase complex.
