Bovine bone protein-quercetin conjugates for improved physical and oxidative stability of oil-in-water emulsions

To enhance the functional properties of bovine bone proteins (BBP) for food-related applications, their quercetin conjugates (BBP-QC), with antioxidant and emulsifying properties, were prepared by alkaline induction. The structural changes of BBP-QC conjugates were investigated, and their different concentrations were examined for the physical and oxidative stability of oil-in-water (O/W) emulsions. Structural characterization using Fourier transform infrared spectroscopy (FT-IR) and fluorescence spectroscopy confirmed the covalent binding of QC with BBP resulting in a conformational change in BBP. Particle size and ζ-potential measurements showed that 0.6% BBP-QC effectively improved the physical stability, increased the net charge of the O/W emulsion. Fluorescence microscopy observation of emulsion microstructure showed that the distribution of oil droplets in the BBP-QC stabilized emulsion was smaller and more uniform than that without the conjugates and effectively alleviated the phase separation in the emulsion. The 0.6% BBP-QC emulsion had a peroxide value (PV) and thiobarbituric acid reactive substances (TBARS) value of only 1.45 mmol/kg and 3.32 μmol/kg after 12 days. Additionally, BBP-QC stabilized emulsions exhibited excellent antioxidant capacity in vitro antioxidant experiments. This study highlights the excellent properties of BBP-QC conjugates as novel emulsifiers with high antioxidant activity and potential applications in the food industry. [Display omitted] •Preparation of a novel antioxidant emulsifier based on bovine bone protein-quercetin conjugates.•The effect of BBP-QC conjugates on the physical and oxidative stability of emulsion was determined.•Further revealed the possible intrinsic mechanism of BBP-QC covalent stabilized emulsion.•Improved thermodynamic instability of oil-in-water emulsions.