为提高核桃分离蛋白(WalPI)的功能特性,选择亲水性乳清蛋白分离物(WPI)通过pH循环技术配制WalPI-WPI纳米颗粒(nano-WalPI-WPI)。这些纳米WalPI-WPI颗粒随后用于稳定高内相Pickering乳液(HIPEs)。通过将WalPI与WPI的质量比从9:1调整到1:1,所得纳米WalPI-WPI的尺寸范围为70.98至124.57nm,多分散指数小于0.326。当WalPI与WPI的质量比为7:3时,各种功能性质均有显著提高:变性峰值温度,乳化活性指数,乳化稳定性指数提高了6.09倍,0.54°C,318.94m2/g,552.95分钟,分别,表面疏水性下降59.23%,与WalPI纳米粒子(nano-WalPI)相比,具有最佳的整体性能。纳米WalPI-WPI通过疏水相互作用保持在一起,氢键,和静电力,保留了完整的一级结构,并在中和过程中提高了对结构变化的抵抗力。纳米WalPI-WPI稳定的HIPEs表现出小于30μm的平均液滴尺寸,液滴均匀分散并保持完整的球形结构,表现出优异的储存稳定性。所有HIPE均表现出假塑性行为,具有良好的触变性能。本研究为增强疏水性蛋白的功能特性提供了理论基础,并为构建复合蛋白作为乳化剂稳定的乳液体系提供了新的方法。
To enhance the functional properties of walnut protein isolate (WalPI), hydrophilic whey protein isolate (WPI) was selected to formulate WalPI-WPI nanoparticles (nano-WalPI-WPI) via a pH cycling technique. These nano-WalPI-WPI particles were subsequently employed to stabilize high internal phase Pickering emulsions (HIPEs). By adjusting the mass ratio of WalPI to WPI from 9:1 to 1:1, the resultant nano-WalPI-WPI exhibited sizes ranging from 70.98 to 124.57 nm, with a polydispersity index of less than 0.326. When the mass ratio of WalPI to WPI was 7:3, there were significant enhancements in various functional properties: the solubility, denaturation peak temperature, emulsifying activity index, and emulsifying stability index increased by 6.09 times, 0.54 °C, 318.94 m2/g, and 552.95 min, respectively, and the surface hydrophobicity decreased by 59.23%, compared with that of WalPI nanoparticles (nano-WalPI), with the best overall performance. The nano-WalPI-WPI were held together by hydrophobic interactions, hydrogen bonding, and electrostatic forces, which preserved the intact primary structure and improved resistance to structural changes during the neutralization process. The HIPEs stabilized by nano-WalPI-WPI exhibited an average droplet size of less than 30 μm, with droplets uniformly dispersed and maintaining an intact spherical structure, demonstrating superior storage stability. All HIPEs exhibited pseudoplastic behavior with good thixotropic properties. This study provides a theoretical foundation for enhancing the functional properties of hydrophobic proteins and introduces a novel approach for constructing emulsion systems stabilized by composite proteins as emulsifiers.