Yu Xiaoshuai, Wang Zhenguo, Duan Yumin, Wang Kexin, Huo Jinjie, Wang Lishuang, Ma Xiaoqi, Wang Peng, Xiao Zhigang
College of Food Science and Technology, Bohai University, Jinzhou, China.
College of Grain Science and Technology, Shenyang Normal University, Shenyang, China.
J Sci Food Agric. 2025 May;105(7):3643-3653. doi: 10.1002/jsfa.14116. Epub 2025 Jan 10.
Soy protein isolate (SPI) has poor emulsifying ability because of its low molecular flexibility and compact structure, limiting its application in extruded protein-based foods. Extrusion technology has emerged as a promising way to alter the structural properties of proteins. Therefore, the impacts of grape seed proanthocyanidin (GSP) on structural and emulsifying characteristics of SPI in extrusion field were explored in this study.
After extrusion treatment, the molecular chains of SPI were unfolded. In comparison with extruded SPI, the interaction with GSP led to a rightward shift in particle size distribution and an enhancement in zeta potential values of the protein. As GSP concentration increased from 20 to 80 g kg, the free sulfhydryl content of SPI was reduced by 4.17%, 25%, 29.24% and 35.85% compared with that of extruded SPI. The addition of GSP altered the secondary structure of SPI and enhanced the microenvironment polarity. Meanwhile, SDS-PAGE results indicated that the protein presented lower molecular weight with the introduction of GSP. Compared with extruded SPI, the supplementation with GSP increased the molecular flexibility while it decreased the surface hydrophobicity of SPI. Correlation analyses demonstrated that these structural changes induced an improvement in emulsifying activity and emulsion stability of SPI. GSP mainly binds to SPI through hydrogen bonds and hydrophobic interactions under the extrusion environment.
This study demonstrated that GSP is a potential modifier, which can be applied to improve the emulsifying capacity of extruded SPI-based foods. © 2025 Society of Chemical Industry.
大豆分离蛋白(SPI)因其分子柔性低和结构紧凑而具有较差的乳化能力,限制了其在挤压蛋白基食品中的应用。挤压技术已成为改变蛋白质结构特性的一种有前景的方法。因此,本研究探讨了葡萄籽原花青素(GSP)对挤压过程中SPI结构和乳化特性的影响。
挤压处理后,SPI的分子链展开。与挤压后的SPI相比,与GSP的相互作用导致粒径分布向右移动,蛋白质的ζ电位值增加。随着GSP浓度从20 g/kg增加到80 g/kg,与挤压后的SPI相比,SPI的游离巯基含量分别降低了4.17%、25%、29.24%和35.85%。GSP的添加改变了SPI的二级结构,增强了微环境极性。同时,SDS-PAGE结果表明,随着GSP的引入,蛋白质的分子量降低。与挤压后的SPI相比,添加GSP增加了SPI的分子柔性,同时降低了其表面疏水性。相关性分析表明,这些结构变化导致SPI的乳化活性和乳液稳定性提高。在挤压环境下,GSP主要通过氢键和疏水相互作用与SPI结合。
本研究表明,GSP是一种潜在的改性剂,可用于提高基于挤压SPI的食品的乳化能力。©2025化学工业协会。