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Hydrolytic properties of the four small intestinal mucosal α‐glucosidases on disaccharides with different linkages and compositions (LB433)

The mucosal α‐glucosidases in the small intestine, consisting of maltase, glucoamylase, sucrase, and isomaltase, are the major enzymes that digest carbohydrates to monosaccharides (e.g., glucose and fructose). In this study, disaccharides (maltose isomers, sucrose isomers) with various possible α‐linkages and compositional types (between glucose‐glucose and glucose‐fructose) were hydrolyzed by each recombinant enzyme to determine their specific α‐hydrolytic kinetic properties. The individual α‐glucosidases had various digestion activities on the disaccharides, however maltase showed the most versatile α‐hydrolytic activity on them. The results indicate that the major hydrolysis activity differs based on linkages, structural conformations of disaccharides, and their composition. This study can be applied to establish a strategy for developing new carbohydrates for extended postprandial glucose response with low glycemic response profile. These findings also suggest that all of the mammalian mucosal α‐glucosidases are necessary relevant enzymes to be used for in vitro digestibility assays when applied to testing various digestible carbohydrates and to accurately characterize their hydrolysis properties.