Abstract
Emulsifying properties are one of the important functional properties of myofibrillar protein (MP), and improving the stability of the MP emulsions under a wide range of pH conditions can help resist the effects of unfavourable acid–base factors during processing. Previously, the continuous cyclic wet heating glycation was carried out to successfully prepare the MP–glucose conjugates, and the present study explored mechanism of the conjugates to stabilize emulsions under different pH conditions. The results showed that MP aggregated by intermolecular hydrophobic interactions under acidic conditions, while electrostatic repulsion induced the stretching of molecular conformation, and the emulsifying performance was significantly (P < 0.05) improved under neutral and alkaline conditions. Compared with the control MP, the more flexible structures and higher solubility of glycated molecules promoted the adsorption at the oil–water interface with increasing pH, resulting in a more uniform distribution of smaller oil droplets, which enhanced the internal structures and improved the rheological properties of the emulsions; meanwhile, due to the stronger intermolecular electrostatic repulsion and the steric hindrance, the emulsions prepared by glycated MP exhibited better dynamic stability and storage stability, especially at pH 11.
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