The interactions of gallic acid and tannic acid with purified brush border sucrase (EC 3.2.1.48) from mouse intestine have been studied. These findings indicate that both gallic acid and tannic acid inhibit sucrase activity, which is pH dependent. Kinetic analysis revealed that enzyme inhibition by gallic acid is a pure V effect at pH 5.0, which changes to mixed type at pH 7.2, and pure K effect at pH 8.5. In contrast, sucrase inhibition by tannic acid was a pure K effect at acidic pH and uncompetitive type in the alkaline pH range. Far-CD spectroscopic analysis revealed an increase in the helicity of the enzyme at acidic pH in the presence of tannic acid but no change at alkaline pH. Fluorescence spectra revealed a red shift in λmax of the enzyme, suggesting that tryptophan residues come to a more hydrophilic environment in the presence of polyphenols. These findings suggest that inhibition of mice sucrase by polyphenols is pH dependent, and is associated with conformational modifications of the enzyme.

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