Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
7589698 | Food Chemistry | 2016 | 9 Pages |
Abstract
The interactions of α- and β-casein with malvidin-3-O-glucoside (MG), the major anthocyanin in grape skin anthocyanin extracts (GSAE), were examined at pH 6.3 by fluorescence, fourier transform infrared (FTIR) and circular dichroism (CD) spectroscopy. The binding constant (KS), binding force and effects of the interactions on the caseins conformation and GSAE stability were investigated. The results showed that α- and β-casein bound with MG via hydrophilic (van der Waals forces or hydrogen bonding) and hydrophobic interactions, respectively. α-Casein had a slightly stronger binding affinity toward MG than β-casein, with respective KS values of 0.51 Ã 103 Mâ1 and 0.46 Ã 103 Mâ1 at 297 K. The secondary structures of α- and β-casein were changed by MG binding, with a decrease in α-helix and an increase in turn for α-casein and no change in α-helix and a decrease in turn for β-casein. The casein-anthocyanin interaction appeared to have a positive effect on the thermal, oxidation and photo stability of GSAE.
Keywords
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Zhiyong He, Mingzhu Xu, Maomao Zeng, Fang Qin, Jie Chen,