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The inhibitory activity against porcine alpha-glucosidase was dependent on the chemical structure of the side chain at the C-6 position. GA was 4-6 times more active than maltose. The replacement of the carboxyl group at the C-2 position of GA with a hydroxyl group (2-OH) did not affect the inhibitory activity. However, the C-2 hydroxy group of glycyrrhizin (GL), a major component of Glycyrrhiza glabra, inhibited the glucosidase activity 2-4 times more potently than GA. The inhibition by GL was not affected by co-incubation with GA. The inhibition of the glucosidase activity by GL was not additive to that by GA. The inhibitory activities of GL and GA were not influenced by changes in their pKa values and ionization. The inhibitory activity of GL decreased when it was esterified, but the inhibitory activity of GA increased. 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