这项工作的主要意义是，商业酵母蛋白颗粒被成功地用于表征高内相皮克林乳液（HIPPE）。不同的超声处理时间（0,3,7,11,15分钟）用于调节作为Pickering颗粒的酵母蛋白（YP）的结构和界面特征。紧接着，研究了不同超声处理时间制备的YPs颗粒对HIPPE流变行为和聚结机理的影响。结果表明，超声处理7分钟的YPs表现出更松弛的分子结构和构象，最小的颗粒大小，最高的H0和最佳的两亲性（三相接触（θ）为88.91°）。当超声处理时间超过7分钟时，发生了从扩展到紧凑构象的转变。导致YPs颗粒的大小增加，表面疏水性（H0）的降低，和亲水性的提高。超声处理7分钟的YPs颗粒稳定的HIPPE表现出最高的吸附界面蛋白百分比和更均匀的三维（3D）蛋白网络，导致最小的液滴尺寸和最高的存储（G\'）。通过超声处理15分钟的YP颗粒稳定的HIPPE样品显示出最低的吸附蛋白百分比。这导致其界面蛋白质层厚度的减小和液滴直径的增大(D[3,2])。根据用于评估液滴的聚结概率的等式(等式(2)),其易于液滴聚结。未吸附的YPs颗粒在连续相中形成较大的聚集结构，并在3D蛋白质网络中充当“结构剂”。因此,机械上,超声处理7分钟的YPs颗粒形成的界面蛋白层对HIPPE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稳定性的贡献更大。本研究结果为商业YP在功能食品领域的应用提供了重要的新思路，作为一种有效的替代蛋白质。
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 H0 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 (H0), 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 [3,2]). 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.
PDF(Pubmed)