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Noncovalent Cross-Linking of Casein by Epigallocatechin Gallate Characterized by Single Molecule Force Microscopy

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Department of Molecular Biology and Biotechnology, University of Sheffield, Western Bank, Sheffield S10 2TN, United Kingdom, Department of Chemistry, University of Sheffield, Brook Hill, Sheffield S3 7HF, United Kingdom, and Department of Physics, University of Sheffield, Hounsfield Road, Sheffield S3 7RH, United Kingdom
Cite this: J. Agric. Food Chem. 2006, 54, 12, 4077–4081
Publication Date (Web):May 12, 2006
https://doi.org/10.1021/jf053259f
Copyright © 2006 American Chemical Society

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    Abstract

    Interaction of the tea polyphenol epigallocatechin gallate (EGCG) with β-casein in milk affects the taste of tea and also affects the stability of the tea and the antioxidant ability of the EGCG. In addition, interaction of polyphenols with the chemically similar salivary proline-rich proteins is largely responsible for the astringency of tea and red wine. With the use of single molecule force microscopy, we demonstrate that the interaction of EGCG with a single casein molecule is multivalent and leads to reduction in the persistence length of casein as calculated using the wormlike chain model and a reduction in its radius of gyration. The extra force required to stretch casein in the presence of EGCG is largely entropic, suggesting that multivalent hydrophobic interactions cause a compaction of the casein micelle.

    Keywords: Epigallocatechin gallate; polyphenol; casein; single molecule force microscopy; astringency; compaction

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     Current address:  Fresenius Kabi, Hafnerstrasse 36, A-8055 Graz, Austria.

     Department of Molecular Biology and Biotechnology.

     Department of Chemistry.

    §

     Department of Physics.

    *

     Corresponding author. Phone:  +44 114 222 4224. Fax:  +44 114 222 2800. E-mail:  [email protected].

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