Complexation of bovine β-lactoglobulin with malvidin-3-O-glucoside and its effect on the stability of grape skin anthocyanin extracts

• β-Lactoglobulin bound with MG mainly via hydrophobic interaction.
• The secondary structure of β-lactoglobulin was changed by MG binding.
• Whey protein prevented the color fading and anthocyanin degradation of GSAE.
• β-Lactoglobulin–MG interaction had a positive effect on the GSAE stability.

The binding interaction between bovine β-lactoglobulin and malvidin-3-O-glucoside (MG), the major anthocyanin in grape skin anthocyanin extracts (GSAE), was studied at pH 6.3 using fluorescence, Fourier transform infrared and circular dichroism spectroscopy. The binding constant (KS), binding force and effect of the interaction on the β-lactoglobulin conformation and GSAE stability were investigated. The results indicated that β-lactoglobulin complexed with MG mainly via hydrophobic interaction with KS of 0.67 × 103 M−1 at 297 K. The secondary structure of β-lactoglobulin was changed by MG binding, with a decrease in α-helix, turn and random coil and an increase in β-sheet. Bovine whey protein effectively prevented the color fading and degradation of anthocyanin in the GSAE solution during the thermal treatment (80 °C/2 h), H2O2 oxidation (0.005% H2O2/1 h) and photo illumination (5000 lx/5 d). The whey protein-anthocyanin complexation appeared to have a positive effect on the thermal, oxidation and photo stability of GSAE.