Constructing a strongly interacting Pea-Cod binary protein system by introducing metal cations toward enhanced...

Area of Science:

• Food Science and Technology
• Protein Chemistry
• Materials Science

Background:

• Developing plant-animal protein systems is crucial for the food industry.
• Understanding salt's effect on binary protein aggregation is limited.
• Existing knowledge is primarily based on single protein models.

Purpose of the Study:

• To investigate the impact of ionic strength on pea-cod protein aggregation.
• To understand how salt addition influences the gel network formation in binary protein systems.
• To optimize nutritional and rheological properties of plant-animal protein systems.

Main Methods:

• Utilized Transmission Electron Microscopy (TEM) and Dynamic Light Scattering (DLS) to analyze protein aggregates.
• Varied ionic strength using CaCl2 and NaCl during thermal processing.
• Measured disulfide bond formation, storage modulus, gelling temperature, and network protein proportion.

Main Results:

• Increased ionic strength led to larger heat-induced protein aggregates.
• Disulfide bonds significantly increased with CaCl2 and NaCl addition.
• Salt improved gelling properties, evidenced by higher storage modulus and increased network protein proportion.
• Gelling temperature decreased below 50°C at elevated ionic strength.

Conclusions:

• Ionic strength modulation is effective in mitigating repulsive forces and strengthening protein gel networks.
• Specific ion binding (Ca2+) enhances protein aggregation, similar to moderate salt concentrations.
• Findings support the design of improved, cost-effective, and healthier plant-animal binary protein systems.