Comparison of the specific mechanical energy, specific thermal energy, and functional properties of cold and hot extruded pea protein isolate.

Pea protein is a popular source of plant-based protein, though its application in meat and dairy analog products is still lacking. This is particularly true in the development of products with fatty and creamy textures. Cold denaturation may be a way to induce these types of textures in food since this is a universal phenomenon in protein that occurs due to a weakening of hydrophobic interactions at cold temperatures. This work utilizes a single screw extruder to systematically study the impacts of moisture content (50-65 %) and pH (2,4.5,8) on the outlet temperatures, specific mechanical energy, specific thermal energy, and texture of cold-extruded pea protein. It was found that at pH 2 and moistures of 60 % and greater, the temperature of the product exiting the extruder is <5.5 °C, and also produced 13.7 %-36.5 % more specific thermal energy, indicating the occurrence of cold denaturation in these products. Based on these findings, a comparison of hot and cold extrusion was conducted as a function of pH and oil content. It was found that cold extrusion imparts 43.0 %-56.2 % more mechanical energy into the protein than hot extrusion, and the cold extruded protein had higher values of Young's modulus and breaking stress. The protein extruded at low temperatures was also able to bind 32.93 % more oil than hot extruded proteins when extruded with 10 % added oil, which may aid in the formation of protein-based fat memetics for the food industry.

Physicochemical characterization of changes in pea protein as the result of cold extrusion.

Pea protein is a popular plant-based protein for mimicking textures in meat and dairy analogues which are more sustainable than their animal-based counterparts. However, precise mechanisms for generating specific textures through different processing methods are still being evaluated. This work utilizes a novel low-temperature extrusion process to selectively alter the chemical structure of pea protein. Changes in secondary structure, surface hydrophobicity, electrostatic interactions, and disulfide bonding are characterized through FTIR, ANS- probes, zeta potential, and SDS-PAGE. Extrudates are further characterized using texture parameter analysis. It was found that a linear combination of physicochemical data, generated with multiple linear regression modelling, led to reasonable estimates of the specific mechanical energy and textural properties. This work offers a new method of reactive extrusion to selectively modify interactions in pea protein using low temperature extrusion, and applications may include fatty textures, since the extrudates are found to be largely stabilized through hydrophobic interactions evaluated with surface hydrophobicity measurements.