Physical and oxidative stability of food emulsions prepared with pea protein fractions

Effects of ultrasound on the structural and emulsifying properties and interfacial properties of oxidized soybean protein aggregates

“…Soy protein undergoes a conformational transition after being continuously attacked by oxidation, and it forms oxidative aggregates with a high degree of aggregation and reduction in emulsification activity. In the food industry, oxidized soybean protein is difficult to use [15] . To increase its emulsification and interfacial activity, it is critical to investigate methods of modulating the oxidative aggregates of soybean protein isolates.…”

Effect of ultrasonic on the structure and quality characteristics of quinoa protein oxidation aggregates

“…Due to the oxidative denaturation of quinoa protein, the groups inside the molecule recombine to form oligomers after exposure, which further form macromolecular aggregates under the action of hydrophobicity and electrostatic attraction [5] . The decrease of solubility and interfacial activity leads to the poor functional properties of quinoa proteins; hence quinoa protein is difficult to apply in food industry [6] .…”

Plant Proteins for Future Foods: A Roadmap

“…Most commercial plant protein isolates available today employ a wet extraction and fractionation technique (alkaline extraction-isoelectric precipitation) that also causes extensive protein denaturation and aggregation, severely affecting functionality because of the harsh conditions used [50]. For example, up to 75% of proteins present in pea protein isolates are insoluble and nonfunctional, and hence, unutilized [51]. In addition, endogenous phenolic compounds may form complexes with plant proteins, affecting the functional and nutritional properties of the proteins [52].…”