Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds - Archive ouverte HAL Accéder directement au contenu
Article Dans Une Revue Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology Année : 1997

Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds

Résumé

Alpha-amylase inhibitor (alpha-AI) from kidney bean (Phaseolus vulgaris L. cv Tendergreen) seeds has been purified to homogeneity by heat treatment in acidic medium, ammonium sulphate fractionation, chromatofocusing and gel filtration. Two isoforms, alpha-AI1 and alpha-AI1', of 43 kDa have been isolated which differ from each other by their isoelectric points and neutral sugar contents. The major isoform alpha-AI1 inhibited human and porcine pancreatic alpha-amylases (PPA) but was devoid of activity on alpha-amylases of bacterial or fungal origins. As shown on the Lineweaver-Burk plots, the nature of the inhibition is explained by a mixed non-competitive inhibition mechanism. Alpha-AI1 formed a 1:2 stoichiometric complex with PPA which showed an optimum pH of 4.5 at 30 degrees C. Owing to the low optimum pH found for alpha-AI activity, inhibitor-containing diets such as beans or transgenic plants expressing alpha-AI should be devoid of any harmful effect on human health.
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Dates et versions

hal-01849235 , version 1 (05-06-2019)

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Véronique Le Berre, Coralie Bompard-Gilles, Françoise Payan, Pierre Rougé. Characterization and functional properties of the α-amylase inhibitor (α-AI) from kidney bean (Phaseolus vulgaris) seeds. Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1997, 1343 (1), pp.31 - 40. ⟨10.1016/S0167-4838(97)00100-3⟩. ⟨hal-01849235⟩
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