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A Pickering emulsion was prepared using β-cyclodextrin (β-CD) and a cinnamaldehyde (CA)/β-CD composite as emulsifiers and corn oil, camellia oil, lard oil, and fish oil as oil phases. It was confirmed that Pickering emulsions prepared with β-CD and CA/β-CD had good storage stability. The rheological experiments showed that all emulsions had G′ values higher than G″, thus confirming their gel properties. The results of temperature scanning rheology experiments revealed that the Pickering emulsion prepared with β-CD and CA/β-CD composites had high stability, in the range of 20–65 °C. The chewing properties of Pickering emulsions prepared by β-CD and corn oil, camellia oil, lard, and herring oil were 8.02 ± 0.24 N, 7.94 ± 0.16 N, 36.41 ± 1.25 N, and 5.17 ± 0.13 N, respectively. The chewing properties of Pickering emulsions made with the CA/β-CD composite and corn oil, camellia oil, lard, and herring oil were 2.51 ± 0.05 N, 2.56 ± 0.05 N, 22.67 ± 1.70 N, 3.83 ± 0.29 N, respectively. The texture properties confirmed that the CA/β-CD-composite-stabilized-emulsion had superior palatability. After 28 days at 50 °C, malondialdehyde (MDA) was detected in the emulsion. Compared with the β-CD and CA + β-CD emulsion, the CA/β-CD composite emulsion had the lowest content of MDA (182.23 ± 8.93 nmol/kg). The in vitro digestion results showed that the free fatty acid (FFA) release rates of the CA/β-CD composite emulsion (87.49 ± 3.40%) were higher than those of the β-CD emulsion (74.32 ± 2.11%). This strategy provides ideas for expanding the application range of emulsifier particles and developing food-grade Pickering emulsions with antioxidant capacity.

Native soy protein isolate (N-SPI) has a low denaturation point and low solubility, limiting its industrial application. The influence of different industrial modification methods (heat (H), alkaline (A), glycosylation (G), and oxidation (O)) on the structure of SPI, the properties of the gel, and the gel properties of soy protein isolate (SPI) in myofibril protein (MP) was evaluated. The study found that four industrial modifications did not influence the subunit composition of SPI. However, the four industrial modifications altered SPI’s secondary structure and disulfide bond conformation content. A-SPI exhibits the highest surface hydrophobicity and I850/830 ratio but the lowest thermal stability. G-SPI exhibits the highest disulfide bond content and the best gel properties. Compared with MP gel, the addition of H-SPI, A-SPI, G-SPI, and O-SPI components significantly improved the properties of the gel. Additionally, MP-ASPI gel exhibits the best properties and microstructure. Overall, the four industrial modification effects may impact SPI’s structure and gel properties in different ways. A-SPI could be a potential functionality-enhanced soy protein ingredient in comminuted meat products. The present study results will provide a theoretical basis for the industrialized production of SPI.