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 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
URI	https://reading-clone.eprints-hosting.org/id/eprint/8524
Item Type	Article
Refereed	Yes
Divisions	Life Sciences > School of Agriculture, Policy and Development
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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