Статья

Probing Protein−Tannin Interactions by Isothermal Titration Microcalorimetry

Richard A. FrazierSchool of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, United Kingdom, NSRU Chemistry and Biochemistry Laboratory, Department of Agriculture, The University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, United Kingdom, and Department of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United KingdomAthina PapadopoulouSchool of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, United Kingdom, NSRU Chemistry and Biochemistry Laboratory, Department of Agriculture, The University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, United Kingdom, and Department of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United KingdomI. Mueller‐HarveySchool of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, United Kingdom, NSRU Chemistry and Biochemistry Laboratory, Department of Agriculture, The University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, United Kingdom, and Department of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United KingdomDawn KissoonSchool of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, United Kingdom, NSRU Chemistry and Biochemistry Laboratory, Department of Agriculture, The University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, United Kingdom, and Department of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United KingdomRebecca J. GreenSchool of Food Biosciences, The University of Reading, P.O. Box 226, Whiteknights, Reading RG6 6AP, United Kingdom, NSRU Chemistry and Biochemistry Laboratory, Department of Agriculture, The University of Reading, P.O. Box 236, Earley Gate, Reading RG6 6AT, United Kingdom, and Department of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, United Kingdom

2003en

ABI

Аннотация

Isothermal titration microcalorimetry (ITC) has been applied to investigate protein-tannin interactions. Two hydrolyzable tannins were studied, namely myrabolan and tara tannins, for their interaction with bovine serum albumin (BSA), a model globular protein, and gelatin, a model proline-rich random coil protein. Calorimetry data indicate that protein-tannin interaction mechanisms are dependent upon the nature of the protein involved. Tannins apparently interact nonspecifically with the globular BSA, leading to binding saturation at estimated tannin/BSA molar ratios of 48:1 for tara- and 178:1 for myrabolan tannins. Tannins bind to the random coil protein gelatin by a two-stage mechanism. The energetics of the first stage show evidence for cooperative binding of tannins to the protein, while the second stage indicates gradual saturation of binding sites as observed for interaction with BSA. The structure and flexibility of the tannins themselves alters the stoichiometry of the interaction, but does not appear to have any significant affect on the overall binding mechanism observed. This study demonstrates the potential of ITC for providing an insight into the nature of protein-tannin interactions.

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Идентификаторы

DOI: 10.1021/jf021179v

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