Sha Lei, Koosis Aeneas O, Wang Qingling, True Alma D, Xiong Youling L
College of Food Science and Engineering, Bohai University, Jinzhou, Liaoning 121013, China; Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States.
Department of Animal and Food Sciences, University of Kentucky, Lexington, KY 40546, United States.
Food Chem. 2021 Jul 15;350:129271. doi: 10.1016/j.foodchem.2021.129271. Epub 2021 Feb 9.
In this study, the structural, interfacial, and emulsifying properties of high-intensity ultrasound (HUS)-treated pea protein isolate (PPI) were investigated. HUS at 50% amplitude and 57-60 W·cm for 5 min markedly improved protein solubility (by 132%), surface hydrophobicity (by 173%), and reduced particle size (by 52%). These physicochemical changes in PPI 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 PPI when compared to control protein (PPI), based on dilatational testing, contributed to the above results. Moreover, PPI-stabilized emulsions exhibited a tendency of being less susceptible to lipid oxidation during storage. Thus, structure-modifying HUS may be a valuable processing technology for the manufacture of pea protein-based emulsion foods.
在本研究中，对高强度超声（HUS）处理的豌豆分离蛋白（PPI）的结构、界面和乳化特性进行了研究。50%振幅、57 - 60 W·cm的HUS处理5分钟显著提高了蛋白质溶解度（提高了132%）、表面疏水性（提高了173%）并减小了粒径（减小了52%）。PPI的这些物理化学变化导致蛋白质在油水界面的吸附更快，提高了乳化活性（提高了18 - 27%）和乳化能力（提高了11%），并增强了乳液的物理稳定性。基于拉伸试验，与对照蛋白（PPI）相比，PPI形成的界面膜具有多层性质，尽管弹性较小，但促成了上述结果。此外，PPI稳定的乳液在储存期间表现出对脂质氧化不太敏感的趋势。因此，结构改性的HUS可能是制造豌豆蛋白基乳液食品的一种有价值的加工技术。
