Foaming and emulsifying properties of extensively and mildly extracted Bambara groundnut proteins: A comparison of legumin, vicilin and albumin protein

Particle-stabilized emulsions, also referred to as Pickering emulsions, have garnered exponentially increasing interest in recent years. This has also led to the first food applications, although the number of related publications is still rather low. The involved stabilization mechanisms are fundamentally different as compared to conventional emulsifiers, which can be an asset in terms of emulsion stability. Even though most of the research on Pickering emulsions has been conducted on model systems, with inorganic solid particles, recent progress has been made on the utilization of food-grade or food-compatible organic particles for this purpose. This review reports the latest advances in that respect, including technical challenges, and discusses the potential benefits and drawbacks of using Pickering emulsions for food applications, as an alternative to conventional emulsifier-based systems.

Structural unfolding of soy protein isolate (SPI) as induced by holding (0, 0.5, 1, 2, and 4 h) in acidic (pH 1.5-3.5) and alkaline (pH 10.0-12.0) pH solutions, followed by refolding (1 h) at pH 7.0, was analyzed. Changes in emulsifying properties of treated SPI were then examined. The pH-shifting treatments resulted in a substantial increase in protein surface hydrophobicity, intrinsic tryptophan fluorescence intensity, and disulfide-mediated aggregation, along with the exposure of tyrosine. After the pH-shifting processes, soy protein adopted a molten globule-like conformation that largely maintained the original secondary structure and overall compactness but lost some tertiary structure. These structural modifications, consequently, led to markedly improved emulsifying activity of SPI as well as the emulsion stability.