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

Area of Science:

• Food Science
• Biochemistry
• Materials Science

Background:

• High-concentration protein solutions are vital in food engineering.
• Excessive viscosity in these solutions impedes processing and affects texture.
• A need exists for efficient methods to reduce protein solution viscosity.

Purpose of the Study:

• To develop a green and scalable method for reducing the viscosity of high-concentration cod protein (CPs) solutions.
• To achieve this through structural reengineering by cleaving disulfide bonds.
• To improve the processing and textural properties of protein solutions.

Main Methods:

• Utilized sodium metabisulfite (Na2S2O5) to selectively cleave disulfide bonds in cod proteins.
• Applied a preheating treatment at 100°C to facilitate protein structural reorganization.
• Employed Atomic Force Microscopy (AFM) force-curve analysis to measure particle adhesion.

Main Results:

• Disulfide bond cleavage and unfolding exposed hydrophobic domains in CPs.
• Preheating and hydrophobic interactions led to the formation of dense, low-viscosity CPs particles.
• AFM showed a 60.5% reduction in CPs particle adhesion (from 3.96 nN to 1.56 nN).
• Improved particle mobility was observed at high concentrations (10%, w/v).

Conclusions:

• A thermodynamically guided approach for protein functional tailoring was established.
• Nanoscale adhesion control through decoupled aggregation offers a method to reduce viscosity.
• This strategy has transformative potential for food processing applications.