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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.

The protein conformation of soymilk is the key to affecting the instant solubility of soymilk flour. This study aimed to evaluate the effect of cavitation jet treatment time (0, 2, 4, 6, and 8 min) on the instant solubility of soymilk flour based on the conformational changes of protein in soymilk. The results showed that the cavitation jet treatment for 0–4 min significantly unfolded the protein structure of soymilk and increased the content of soluble protein, which reduced the particle size and increased the electrostatic repulsion and the viscosity of soymilk. This was beneficial for soymilk droplets fully atomized and repolymerized in the spray drying tower, forming soymilk flour particles with large size, smooth surface, and uniform distribution. When the cavitation jet treatment time was 4 min, the wettability (from 127.3 ± 2.5 s to 84.7 ± 2.1 s), dispersibility (from 70.0 ± 2.0 s to 55.7 ± 2.1 s), and solubility (from 56.54% to 78.10%) of soymilk flour were significantly improved. However, when the time of the cavitation jet treatment was extended to 8 min, the protein of soymilk aggregated and the stability of soymilk decreased, which reduced the particle size and hurt the surface characteristics of soymilk flour after spray drying. It resulted in a decrease in the instant solubility of soymilk flour. Therefore, the cavitation jet treatment with proper time increases the instant solubility of soymilk flour by improving the protein conformation of soymilk.

The combination of protein and flavonoids can ameliorate the problems of poor solubility and stability of flavonoids in utilization. In this study, soybean protein isolate pretreated by ultrasonication was selected as the embedding wall material, which was combined with luteolin to form a soybean protein isolate-luteolin nanodelivery system. The complexation effect and structural changes of soybean protein isolate (SPI) and ultrasonic pretreatment (100 W, 200 W, 300 W, 400 W and 500 W) of soybean protein isolate with luteolin (LUT) were compared, as well as the changes in digestion characteristics and antioxidant activity in vitro. The results showed that proper ultrasonic pretreatment increased the encapsulation efficacy, loading amount and solubility to 89.72%, 2.51 μg/mg and 90.56%. Appropriate ultrasonic pretreatment could make the particle size and the absolute value of ζ-potential of SPI-LUT nanodelivery system decrease and increase respectively. The FTIR and fluorescence results show that appropriate ultrasonic pretreatment could reduce α-helix, β-sheet and random coil, increase β-turn, and enhance fluorescence quenching. The thermodynamic evaluation results indicate that the ΔG 0 and ΔS > 0, so the interaction of LUT with the protein was spontaneous and mostly governed by hydrophobic interactions. The XRD results show that the LUT was amorphous and completely wrapped by SPI. The DSC results showed that ultrasonic pretreatment could improve the thermal stability of SPI-LUT nanodelivery system to 112.66 ± 1.69 °C. Digestion and antioxidant analysis showed that appropriate ultrasonic pretreatment increased the LUT release rate and DPPH clearance rate of SPI-LUT nanodelivery system to 89.40 % and 55.63 % respectively. This study is a preliminary source for the construction of an SPI nanodelivery system with ultrasound pretreatment and the deep processing and utilization of fat-soluble active substances.