超声
豌豆蛋白
萝卜
蛋白质二级结构
化学
十二烷基硫酸钠
生物化学
色谱法
生物
植物
作者
Libo Liu,Miao Yu,Chengwen Hu,Lu Gao,Weijia He,Hong Wei Chu,Tong Zhang,Chun Li,Wenkui Guo
摘要
Abstract BACKGROUND Pea protein, as a by‐product of peas ( Pisum sativum L .), is rich in a variety of essential amino acids that can meet the body's protein needs and is a valuable source of protein. Since the function of pea protein is closely related to its structure, pea protein has been subjected to different modifications in recent years to improve its application in food and to develop new products. RESULTS The effects of sonication frequency (primary and secondary time) on pea protein isolate's (PPI's) structural and functional properties were investigated. Sodium dodecyl sulfate polyacrylamide gel electrophoresis demonstrated that different sonication frequencies at the same power (600 W) treatment had no effect on PPI's molecular weight. Fourier‐transform infrared spectroscopy revealed that treatment at different sonication frequencies caused secondary structural changes in PPI. The particle size distribution, foaming, stability, surface hydrophobicity, emulsification, and oxidation resistance of PPI were improved after primary and secondary sonication, but secondary sonication was not more effective than primary sonication for an extended period of time. CONCLUSION Overall, ultrasound is able to improve the structural and functional properties of pea proteins within a suitable range. It provides a theoretical basis for elucidating the modification of the structure and function of plant proteins by ultrasound and lays the foundation for the development of plant proteins in food applications as well as development. © 2023 Society of Chemical Industry.
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