Decoupling aggregation in dense protein solutions: Structural reconfiguration through disulfide reduction weakens...

High-concentration protein solutions are indispensable in food engineering for their nutritional density, yet excessive viscosity hinders processing efficiency and compromises textural quality. A green and scalable strategy is proposed for reducing the viscosity of high-concentration cod protein (CPs) solutions through structural reengineering driven by reductive disulfide bond cleavage. Na₂S₂O₅ selectively disrupts disulfide bonds, inducing conformational unfolding to expose buried hydrophobic domains. Accompanying preheating treatment (100 °C) facilitated entropy-enhanced nucleation, and rapid consumption of reactive groups driven by hydrophobic forces to reorganise into structurally dense, low-viscosity CPs particles. AFM force-curve showed that the adhesion of the modified CPs particles was reduced by 60.5 % (from 3.96 nN to 1.56 nN), which was directly correlated with the significant improvement in mobility at high concentration conditions (10 %, w/v). This work establishes a thermodynamically guided approach to protein functional tailoring through nanoscale adhesion-controlled decoupled aggregation, offering transformative potential for applications such as food processing.