The interaction between sodium alginate and myofibrillar proteins: The rheological and emulsifying properties of their mixture

The interaction between sodium alginate (SA) and turbot myofibrillar proteins (TMP) and the effects of SA concentration (0.1%–0.5%) on the rheological and emulsifying properties of the mixture at neutral pH were investigated. TMP and SA formed complexes through electrostatic repulsion and hydrophobic interaction. The FT-IR analysis indicated that hydrogen bonding was also related to the interaction. With the addition of SA, the electrostatic repulsion between molecules enhanced, which prevented protein aggregation and improved the stability of dispersions. The TMP/SA mixture showed non-Newtonian shear-thinning behavior. The viscosity gradually increased with the increasing SA concentration. TMP and SA formed an interconnected gel-like network structure with a predominant elastic behavior. The strength of network increased due to the strong repulsion between the two biopolymers. Both EAI and ESI of TMP significantly increased after SA addition. The addition of SA reduced droplet size of emulsions. The emulsions also showed pseudoplastic behavior. Addition of SA increased stability of emulsions by increasing viscosity of continuous phase. Complexation with SA effectively improved the rheological and emulsifying properties of fish myofibrillar proteins. These results contributed to the efficient utilization of marine fish proteins as functional ingredients in food products.