The primary significance of this work is that the commercial yeast proteins particles were successfully used to characterize the high internal phase Pickering emulsions (HIPPEs). The different sonication time (0,3,7,11,15 min) was used to modulate the structure and interface characteristics of yeast proteins (YPs) that as Pickering particles. Immediately afterward, the influence of YPs particles prepared at different sonication time on the rheological behavior and coalescence mechanism of HIPPEs was investigated. The results indicate that the YPs sonicated for 7 min exhibited a more relaxed molecular structures and conformation, the smallest particle size, the highest H and optimal amphiphilicity (the three-phase contact (θ) was 88.91°). The transition from extended to compact conformations of YPs occurred when the sonication time exceeded 7 min, resulting in an augmentation of size of YPs particles, a reduction in surface hydrophobicity (H), and an elevation in hydrophilicity. The HIPPEs stabilized by YPs particles sonicated for 7 min exhibited the highest adsorption interface protein percentage and a more homogeneous three-dimensional (3D) protein network, resulting in the smallest droplet size and the highest storage (G′). The HIPPEs sample that stabilized by YPs particles sonicated for 15 min showed the lowest adsorption protein percentage. This caused a reduction in the thickness of its interface protein layer and an enlargement in the droplet diameter (D ). It was prone to droplet coalescence according to the equation used to evaluate the coalescence probability of droplets (Eq (2)). And the non-adsorbed YPs particles form larger aggregation structures in the continuous phase and act as “structural agents” in 3D protein network. Therefore, mechanistically, the interface protein layer formed by YPs particles sonicated 7 min contributed more to HIPPEs stability. Whereas the “structural agents” contributed more to HIPPEs stability when the sonication time exceeded 7 min. The present results shed important new light on the application of commercial YPs in the functional food fields, acting as an available and effective alternative protein.

中文翻译：

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基于商业酵母蛋白的高内相Pickering乳液的稳定机理研究：通过超声处理调节Pickering颗粒的特性

这项工作的主要意义在于，商业酵母蛋白颗粒已成功用于表征高内相 Pickering 乳液 (HIPPE)。采用不同的超声处理时间（0、3、7、11、15分钟）来调节作为Pickering颗粒的酵母蛋白（YPs）的结构和界面特征。随后，研究了不同超声处理时间制备的 YPs 颗粒对 HIPPEs 流变行为和聚结机制的影响。结果表明，超声处理7 min后，YPs表现出更松弛的分子结构和构象、最小的粒径、最高的H和最佳的两亲性（三相接触角（θ）为88.91°）。当超声处理时间超过 7 分钟时，YPs 构象从伸展构象转变为紧凑构象，导致 YPs 颗粒尺寸增大、表面疏水性 (H) 降低和亲水性升高。通过 YPs 颗粒超声处理 7 分钟稳定的 HIPPE 表现出最高的吸附界面蛋白质百分比和更均匀的三维 (3D) 蛋白质网络，从而产生最小的液滴尺寸和最高的存储 (G')。通过 YPs 颗粒超声处理 15 分钟稳定的 HIPPEs 样品显示出最低的吸附蛋白百分比。这导致其界面蛋白层的厚度减小和液滴直径（D）增大。根据用于评估液滴聚结概率的方程（方程（2）），它很容易发生液滴聚结。未吸附的YPs颗粒在连续相中形成更大的聚集结构，并充当3D蛋白质网络中的“结构剂”。因此，从机理上讲，YPs 颗粒超声处理 7 分钟形成的界面蛋白层对 HIPPEs 的稳定性贡献更大。而当超声处理时间超过 7 分钟时，“结构剂”对 HIPPE 的稳定性贡献更大。目前的结果为商业 YP 作为一种可用且有效的替代蛋白质在功能性食品领域的应用提供了重要的新线索。