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The use of enzyme-assisted aqueous extraction to extract soybean oil will produce soy protein hydrolysates (SPH) that have good antioxidant properties but are bitter and hygroscopic. To microencapsulate these hydrolysates, soy protein isolate/maltodextrin mixtures were used as the carrier. The effects of spray-drying and freeze-drying on the bitterness, hygroscopicity, and antioxidant properties were compared. The properties of different dried samples were compared using solubility, hygroscopicity, moisture content, water activity, flowability, and glass transition temperature (Tg). The results showed that the spray-drying was more effective than freeze-drying. Hygroscopicity was reduced to 18.2 g/100 g, and the Tg value was raised to 80.8°C. The morphology was analyzed using scanning electron microscopy, and the antioxidant properties of the samples were measured using the ABTS˙+ radical scavenging activity. The results showed that spray-dried SPH had more carrier masking, which weakened bitterness, reduced moisture absorption, and had no significant negative impact on its oxidation resistance, solubility, and flowability, and spray-drying after carrier encapsulation of SPH improved the recovery rate.

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Background: Protein-polysaccharide complexes have been widely used to stabilize high-internal-phase emulsion (HIPEs). However, it is still unknown whether soy protein isolate-dextran (SPI-Dex) complexes can stabilize HIPEs or what is the effect of Dex concentration on the HIPEs. Furthermore, the non-covalent interaction mechanism between SPI and Dex is also unclear. Therefore, we fabricated SPI-Dex complexes and used them to stabilize HIPEs-loaded quercetin and explore the interaction mechanism between SPI and Dex, as well as the effect of Dex concentration on the particle size, ζ-potential, microstructure, rheology, quercetin encapsulation efficiency, and gastrointestinal fate of the HIPEs.Results: Spectral analysis (fourier transform infrared spectroscopy, ultraviolet spectroscopy, and fluorescence spectroscopy) results identified the formation of SPI-Dex complexes, and indicated that the addition of Dex changed the spatial structure of SPI, whereas thermodynamic analysis (ΔH > 0, ΔS > 0) showed that hydrophobic interactions were the main driving forces in the formation of SPI-Dex complexes. Compared with HIPEs stabilized by SPI, the SPI-Dex complex-stabilized HIPEs had smaller particles (3000.33 ± 201.22 nm), as well as higher ζ-potential (−21.73 ± 1.10 mV), apparent viscosities, modulus, and quercetin encapsulation efficiency (98.19 ± 0.14%). In addition, in vitro digestion revealed that SPI-Dex complex-stabilized HIPEs significantly reduced the release of free fatty acid and improved quercetin bioaccessibility. Conclusion: HIPEs stabilized by SPI-Dex complexes delayed the release of free fat acid and improved the bioaccessibility of quercetin, and may be help in designing delivery systems for bioactive substances with specific properties.

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