Complexation of bovine β-lactoglobulin with malvidin-3-O-glucoside and its effect on the stability of grape skin anthocyanin extracts
作者： Zhiyong He , Haidong Zhu , Mingzhu Xu , Maomao Zeng , Fang Qin
DOI: 10.1016/J.FOODCHEM.2016.04.048
关键词: Glucoside 、 Random coil 、 Anthocyanin 、 Whey protein 、 Binding constant 、 Chromatography 、 Hydrophobic effect 、 Malvidin 、 Circular dichroism 、 Chemistry
摘要: The binding interaction between bovine β-lactoglobulin and malvidin-3-O-glucoside (MG), the major anthocyanin in grape skin extracts (GSAE), was studied at pH 6.3 using fluorescence, Fourier transform infrared circular dichroism spectroscopy. constant (KS), force effect of on conformation GSAE stability were investigated. results indicated that complexed with MG mainly via hydrophobic KS 0.67×10(3)M(-)(1) 297K. secondary structure changed by binding, a decrease α-helix, turn random coil an increase β-sheet. Bovine whey protein effectively prevented color fading degradation solution during thermal treatment (80°C/2h), H2O2 oxidation (0.005% H2O2/1h) photo illumination (5000lx/5d). protein-anthocyanin complexation appeared to have positive thermal, GSAE.
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