New insights suggest isomaltooligosaccharides are slowly digestible carbohydrates, rather than dietary fibers, at constitutive mammalian α-glucosidase levels.

Isomaltooligosaccharides (IMOs) have been characterized as dietary fibers that resist digestion in the small intestine; however, previous studies suggested that various α-glycosidic linkages in IMOs were hydrolyzed by mammalian α-glucosidases. This study investigated the hydrolysis of IMOs by small intestinal α-glucosidases from rat and human recombinant sucrase-isomaltase complex compared to commonly used fungal amyloglucosidase (AMG) in vitro. Interestingly, mammalian α-glucosidases fully hydrolyzed various IMOs to glucose at a slow rate compared with linear maltooligosaccharides, whereas AMG could not fully hydrolyze IMOs because of its very low hydrolytic activity on α-1,6 linkages.