Effect of sodium metabisulfite-mediated self-assembly on the quality of silver carp myofibrillar protein-EGCG composite gels.

Myofibrillar protein (MP) gels are susceptible to oxidation, which can be prevented by complexing with hydrophilic polyphenols, but may cause gel deterioration. Sodium metabisulfite (NaSO) has been used to induce self-assembly of MP and analyze the impact of self-assembly on the quality of composite gels containing high amounts of (-)-epigallocatechin gallate (EGCG). Hydrophobic forces were confirmed as the main driver of self-assembly. Self-assembly reduced the size of the MP-EGCG complex to approximately 670 nm and increased the gel's hydrophobic force by approximately 3.6-fold. The maximum hardness of the NaSO-treated MP-EGCG composite gel was 52.43 g/kg, which was approximately 49% greater than pure MP gel. After oxidative treatment, the NaSO-treated MP-EGCG composite gel had considerably lower carbonyl and dityrosine levels (2.47-μmol/g protein and 450 a.u.) than the control (8.37-μmol/g protein and 964 a.u.). Therefore, NaSO shows potential as a cost-effective additive for alleviating MP limitations in the food industry.