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 Res Int. 2022 Jun;156:111179. doi: 10.1016/j.foodres.2022.111179. Epub 2022 Mar 23.
The structural properties, interfacial behavior, and emulsifying ability of ultrasound-treated pea protein isolate (PPI) and the legumin (11S) and vicilin (7S) globulin fractions prepared with a salt-solubilization procedure were investigated. Of the three protein groups, PPI was strongly responsive to ultrasound perturbation (20 kHz, 57-60 W·cm) showing the greatest solubility increase, particle size reduction, structure destabilization, and conformational change. Similar but less remarkable effects were observed on 11S globulins; 7S proteins, already highly soluble (>99%), were generally less sensitive to ultrasound. The ultrasound treatment significantly improved emulsifying activity, which resulted in greater emulsifying capacity and stronger interfacial adsorption for all protein samples. PPI exhibited the higher activity increase (70.8%) compared to approximately 30% for 11S and 7S. For both control and ultrasound treated proteins, the emulsifying capacity was in the order of 7S > 11S > PPI, inversely related to the trend of protein loading at the interface, indicating efficiency differences. The latter was attributed to emulsion clusters formed through protein-protein interaction in PPI and 11S emulsions which were visibly absent in 7S emulsions.
采用盐溶法制备了豌豆分离蛋白（PPI）以及球蛋白（11S 和 7S），研究了超声处理对其结构特性、界面行为和乳化能力的影响。在这三种蛋白质中，PPI 对超声扰动（20 kHz，57-60 W·cm）反应强烈，表现出最大的溶解度增加、粒径减小、结构失稳和构象变化。11S 球蛋白也表现出类似但不那么显著的效果；7S 蛋白质已经高度可溶（>99%），通常对超声不太敏感。超声处理显著提高了乳化活性，使所有蛋白质样品的乳化能力和界面吸附力都得到了增强。与 11S 和 7S 相比，PPI 的活性增加（70.8%）更高。对于对照和超声处理的蛋白质，乳化能力的顺序为 7S > 11S > PPI，与界面处蛋白质负载的趋势相反，表明效率存在差异。这归因于 PPI 和 11S 乳液中通过蛋白质-蛋白质相互作用形成的乳液簇，而在 7S 乳液中则明显不存在。
