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Characterization of protein-polyphenol interactions

Papadopoulou, A. and Frazier, R.A. (2004) Characterization of protein-polyphenol interactions. Trends in food science & technology, 15 (3-4). pp. 186-190. ISSN 0924-2244

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To link to this item DOI: 10.1016/j.tifs.2003.09.017

Abstract/Summary

Dietary polyphenols have received attention for their biologically significant functions as antioxidants, anticarcinogens or antimutagens, which have led to their recognition as potential nutraceuticals. Polyphenols also characteristically possess a significant binding affinity for proteins, which can lead to the formation of soluble and insoluble protein-polyphenol complexes. Questions remain concerning whether and to what extent the protein-polyphenol interaction influences functionality. For example, is the formation of protein-polyphenol complexes an obstacle to the nutritional bioavailability of either species? This article discusses the development of suitable methodologies to investigate the physicochemical basis of protein-polyphenol interactions and the influence of structure-activity relationships on binding affinities. (C) 2003 Elsevier Ltd. All rights reserved.

Item Type:Article
Refereed:Yes
Divisions:Faculty of Life Sciences > School of Chemistry, Food and Pharmacy > Department of Food and Nutritional Sciences
ID Code:13092
Uncontrolled Keywords:PROLINE-RICH PROTEINS, CAPILLARY-ELECTROPHORESIS, ANTIOXIDANT CAPACITY, BINDING CONSTANTS, TANNIN, PRECIPITATION, FLAVONOIDS, AFFINITY
Additional Information:Conference on New Functional Ingredients and Foods (NFIF 2003) Copenhagaen, DENMARK 9-11 Apr 2003

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