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Assessment of the reactivity of selected isoflavones against proteins in comparison to quercetin

  • Selected isoflavones (genistein, daidzein, formononetin, prunetin, biochanin A and two synthetic isoflavones) were allowed to interact with soy and whey proteins. The reaction products were analyzed in terms of covalent binding at the nucleophilic side chains of proteins. Changes in molecular properties of the proteins derivatives were documented by SDS-PAGE, IEF and SELDI-TOF-MS. The structural changes induced were studied using circular dichroism (CD). The in vitro digestibility was assessed with trypsin. The results show that the occurrence of the catechol moiety, i.e. the two adjacent (ortho) aromatic hydroxyl groups on ring B of the flavonoid structural skeleton appears to be perquisite condition for covalent binding to proteins. The catechol moiety on ring A was less reactive. Its absence lead to a slight or no significant reaction, although non-covalent interactions may still be possible even when lacking this structural element. A comparison of the data is also made with quercetin representing the flavonols.

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Author:Harshadrai M. Rawel, Holger Ranters, Sascha Rohn, Jürgen Kroll
Document Type:Article
Year of first Publication:2004
Year of Completion:2004
Release Date:2017/03/24
Source:Journal of Agricultural and Food Chemistry. - 52 (2004), 16, S. 5263 - 5271
Organizational units:Mathematisch-Naturwissenschaftliche Fakultät / Institut für Ernährungswissenschaft
Peer Review:Referiert