维西林
豆科植物
豌豆蛋白
化学
球蛋白
乳状液
萝卜
色谱法
贮藏蛋白
溶解度
分离蛋白
食品科学
生物化学
植物
生物
有机化学
免疫学
基因
作者
Lei Sha,Youling L. Xiong
标识
DOI:10.1016/j.foodres.2022.111179
摘要
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-2) 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.
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