Conformation changes and emulsifying properties of myofibrillar proteins in water: Effects of electrostatic interaction with chitosan

Great interests have been attracted toward muscle protein in a water-soluble state with improved functionality for further designing meat protein fortified low-salt functional foods. In the present study, electrostatic interaction of chitosan (CH) with myofibrillar proteins (MP) in water aqueous solution was investigated, and the linked structure changes and emulsion stabilization of MP were studied. Results showed that the electrostatic interaction inhibited MP aggregation, and smaller particle size complexes were formed at pH 6.0, leading to the loss of β-sheet contents and recovery of α-helix contents with decreasing MP/CH mixing ratio (5:1 and 1:1). The tertiary structure confirmed the conformation changes of MP in which more hydrophobic groups and active sulfhydryl groups were exposed (P < 0.05), and the fluorescence was also quenched. With decreasing mixing ratio, the droplet size of emulsion decreased (P < 0.05), while the absorbed protein content increased (P < 0.05). After 7 d of storage, complex at a ratio of 1:1 displayed desirable emulsion stability, which could be due to the improved emulsifying capacity, enhanced electrostatic repulsion and steric effects. These findings provide a better understanding of conformation changes of MP in water aqueous solution induced by electrostatic interactions at mild acidic pH and help to fabricate stable protein/polysaccharide emulsification systems for further developing meat protein-based functional food to deliver health.