4.7 Article

Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein

Journal

FOOD CHEMISTRY
Volume 350, Issue -, Pages -

Publisher

ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2021.129271

Keywords

Pea protein; Ultrasonication; O/W emulsions; Dilatational rheology; Lipid oxidation

Funding

  1. USDA National Institute of Food and Agriculture, Hatch [1020736]
  2. Roquette America Inc.
  3. First-class Discipline Project of Liaoning Province, China

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High-intensity ultrasound treatment significantly improved the solubility, hydrophobicity, and particle size of pea protein isolate, leading to enhanced protein adsorption at the oil-water interface and improved emulsifying properties. The multilayer structure formed by PPIUS contributed to the physical stability of emulsions, making them less susceptible to lipid oxidation during storage compared to control protein.
In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPIUS) were investigated. HUS at 50% amplitude and 57-60 W.cm(-2) for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPIUS led to more rapid protein adsorption at the oil-water interface, improved emulsifying activity (by 18-27%) and capacity (by 11%), and enhanced emulsion physical stability. The multilayer nature, albeit less elastic, of the interfacial membrane formed by PPIUS when compared to control protein (PPIC), based on dilatational testing, contributed to the above results. Moreover, PPIUS-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structuremodifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.

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