College of Food Science, Northeast Agricultural University, Harbin, China.
School of Tea and Food Science & Technology, Anhui Agricultural University, Hefei, China.
J Sci Food Agric. 2022 Nov;102(14):6454-6463. doi: 10.1002/jsfa.12012. Epub 2022 Jun 2.
In this paper, the effects of different succinic anhydride (SA) additions on the flexibility of soy protein isolate (SPI) were investigated, and changes in protein conformation and interfacial functional properties were measured. The structure-effect relationship between conformation, flexibility, and interfacial functional properties was established.
SPI was bound to SA through disulfide bonds, and the zeta potential was reduced. The β-sheet content decreased, the disordered structure increased, and there were changes in tertiary structure and microstructure. The surface hydrophobicity, disulfide bond content, and solution turbidity were reduced to 5063, 1.0967 μmol g , and 0.0036 μmol g respectively. The best flexibility of SPI (0.3977) and interfacial functional properties were obtained when the mass ratio of SA/SPI was 15%. Correlation analysis showed a highly significant positive correlation (P < 0.01) between flexibility and emulsification and foaming properties, with correlation coefficients of 0.960 and 0.942 for flexibility with emulsifying activity and emulsion stability respectively, and 0.972 and 0.929 for flexibility with foaming capacity and foaming stability respectively.
The results suggest that succinylation-induced conformational changes of SPI improved its interfacial functional properties by changing its flexibility. These results provide theoretical guidelines for the development and application of highly emulsifiable and stable soy protein products utilizing succinylation. © 2022 Society of Chemical Industry.
本文研究了不同琥珀酸酐（SA）添加量对大豆分离蛋白（SPI）柔韧性的影响，并测量了蛋白质构象和界面功能特性的变化。建立了构象、柔韧性和界面功能特性之间的结构-效应关系。
SPI 通过二硫键与 SA 结合，ζ 电位降低。β-折叠含量降低，无序结构增加，三级结构和微观结构发生变化。表面疏水性、二硫键含量和溶液浊度分别降低至 5063、1.0967 μmol/g 和 0.0036 μmol/g。当 SA/SPI 的质量比为 15%时，SPI 的柔韧性（0.3977）和界面功能特性最佳。相关分析表明，柔韧性与乳化和起泡性能呈高度显著正相关（P<0.01），与乳化活性和乳化稳定性的相关系数分别为 0.960 和 0.942，与起泡能力和起泡稳定性的相关系数分别为 0.972 和 0.929。
琥珀酰化诱导的 SPI 构象变化通过改变其柔韧性来改善其界面功能特性。这些结果为利用琥珀酰化开发高乳化和稳定的大豆蛋白产品提供了理论指导。© 2022 化学工业协会。
