Yin Yaxin, Xu Jue, Shi Zihang, Pan Daodong, Wu Zhen, Zeng Xiaoqun, Tu Maolin
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, Zhejiang 315211, China; Zhejiang Key Laboratory of Food Microbiology and Nutritional Health, Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition, College of Food Science and Engineering, Ningbo University, Ningbo 315800, China.
State Key Laboratory for Managing Biotic and Chemical Threats to the Quality and Safety of Agro-products, Ningbo University, Ningbo, Zhejiang 315211, China; Zhejiang Key Laboratory of Food Microbiology and Nutritional Health, Zhejiang-Malaysia Joint Research Laboratory for Agricultural Product Processing and Nutrition, College of Food Science and Engineering, Ningbo University, Ningbo 315800, China.
Food Chem. 2025 Jun 15;477:143476. doi: 10.1016/j.foodchem.2025.143476. Epub 2025 Feb 19.
This study investigated the role of thermal drive in the formation of soy protein isolate and whey protein isolate (SPI-WPI) complexes, as well as the stability effect of SPI-WPI complexes on high internal phase Pickering emulsions (HIPPEs). The shift in the peaks in the infrared spectrum and the change in fluorescence intensity indicated the interaction between these two proteins, which implies that SPI-WPI is not two dispersed groups of particles. Maximum emulsification activity (10.65 m/g) and the absolute value of potential (37.87 mV) were achieved at an SPI to WPI mass ratio of 7:3. As the concentration and pH of the SPI-WPI complex increased, the droplets become evenly uniform and compact. It is predicted that the high concentration conditions are more favorable for the formation of a gel network structure. This research provides an effective strategy for HIPPEs stabilization using complex proteins.
本研究调查了热驱动在大豆分离蛋白和乳清分离蛋白（SPI-WPI）复合物形成中的作用，以及SPI-WPI复合物对高内相Pickering乳液（HIPPEs）的稳定性影响。红外光谱中峰的移动和荧光强度的变化表明这两种蛋白质之间存在相互作用，这意味着SPI-WPI不是两个分散的颗粒组。在SPI与WPI质量比为7:3时，实现了最大乳化活性（10.65 m/g）和电位绝对值（37.87 mV）。随着SPI-WPI复合物浓度和pH值的增加，液滴变得均匀且紧密。据预测，高浓度条件更有利于凝胶网络结构的形成。本研究为使用复合蛋白稳定HIPPEs提供了一种有效策略。
