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Probing protein-tannin interactions by isothermal titration microcalorimetry

Frazier, R.A., Papadopoulou, A., Mueller-Harvey, I., Kissoon, D. and Green, R.J. (2003) Probing protein-tannin interactions by isothermal titration microcalorimetry. Journal of Agricultural and Food Chemistry, 51 (18). pp. 5189-5195. ISSN 0021-8561

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To link to this article DOI: 10.1021/jf021179v

Abstract/Summary

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.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Chemistry
Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13409
Uncontrolled Keywords:tannin, polyphenol, protein, albumin, gelatin, titration, microcalorimetry, BOVINE SERUM-ALBUMIN, MOLECULAR RECOGNITION, SALIVARY PROTEINS, PLANT, POLYPHENOLS, VEGETABLE TANNINS, MASS-SPECTROMETRY, CONDENSED TANNINS, BINDING, PRECIPITATION, PROCYANIDIN

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