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Open Access Issue
Preparation in Vitro Digestibility of Perilla Oil Multilayer Emulsion
Food Science 2022, 43(12): 58-65
Published: 25 June 2022
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In view of the fact that perilla oil tends to be oxidized during storage, with soy protein isolate (SPI) or its blends with chitosan (CS) and sodium alginate (SA) as the emulsifier, electrostatic layer-by-layer self-assembly was used to encapsulate perilla oil to maintain its physical stability and for its sustained release. The microscopic morphology and stability of the perilla oil single-layer emulsion, double-layer emulsion and three-layer emulsion were investigated, and an in vitro simulated digestion model was established to determine changes in the fatty acid composition of the three emulsions before and after digestion by gas chromatography. The results showed that the three emulsions, prepared using a wall material composed of 1.0% SPI solution, 2.0% CS solution, and 1.5% SA solution, had small particle size, high potential, and good physical and chemical stability. Under acidic conditions, the multi-layer emulsions could better protect polyunsaturated fatty acids. As the number of layers increased, the oxidation rate of perilla oil became slower. The in vitro simulated digestion results showed that the three-layer emulsion had a better sustained-release effect than the single-layer and double-layer emulsions, and the multi-layer emulsion could ensure the effective release of fatty acids from the oil. These findings can guide the development of slow-release systems for oils.

Open Access Issue
Effect of Charge Density Modification of Soy Protein Isolate by Succinylation on Its Conformation and Emulsifying Properties
Food Science 2022, 43(4): 39-45
Published: 25 February 2022
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In this paper, we explored the relationship between the conformational changes of soybean protein isolate (SPI) caused by charge density modification through succinylation and the improvement in emulsifying properties. Succinic anhydride was used to modify SPI. The conformational changes of SPI with different degrees of succinylation were analyzed by fluorescence spectroscopy, ultraviolet spectroscopy and Fourier transform infrared (FTIR) spectroscopy. The effect of succinylation on the physiochemical properties of SPI was characterized by scanning electron microscopy, zeta potential, surface hydrophobicity, molecular flexibility and emulsification. The results showed through succinylation reaction, succinyl groups were successfully grafted onto SPI, so that the isoelectric point of SPI decreased and the electronegativity increased. Additionally, the microstructure was changed with small holes on the surface of the smooth and irregular sheet structure, and the the molecular mass was increased. The increase in charge density led to unfolding of the tertiary structure of SPI, exposure of tryptophan residues burying and tyrosine residues, and a red shift in the fluorescence and ultraviolet absorption spectra, which proved that succinylated SPI is located in a more hydrophilic environment. The reaction between free amino groups in SPI and succinyl groups transformed the N–H bond into C–N bond, resulting in changes in the amide Ⅲ band. The surface hydrophobicity of succinylated SPI was decreased, the molecular flexibility was increased, and the emulsification activity and emulsifon stability were improved compared to SPI. This study confirmed that the increase in the charge density of succinylated SPI can affect the spatial conformation of SPI and consequently improve the emulsifying properties significantly.

Open Access Basic Research Issue
Effect of Pasteurization on Oxidative Stability of Oil Body Emulsions from Various Crops
Food Science 2022, 43(7): 23-30
Published: 15 April 2022
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The present work was executed in order to investigate the influence of pasteurization on the oxidative stability of oil body emulsions from soybean, sunflower, peanut, sesame and walnut. The basic composition and fatty acid composition of the five oil bodies and the composition of their associated proteins were evaluated, and the influence of pasteurization at 85 ℃ for 10 min on the physical and oxidative stability of the oil body emulsions was investigated by dynamic laser scattering and confocal laser scanning microscopy. The results showed that the oil bodies revealed significant differences in their basic composition and fatty acid composition as well as the composition of their associated proteins. The oil body-associated proteins consisted of intrinsic and extrinsic membrane proteins. Unsaturated fatty acids were the major ones in oil bodies. Oleic acid, linoleic acid and α-linolenic acid were the predominant unsaturated acids. Of these five oil bodies, soybean oil bodies had the highest contents of protein and moisture, and the lowest oil content. Peanut oil bodies had the highest relative content of saturated fatty acids (21.27%), while walnut oil bodies had the highest relative content of unsaturated fatty acids (90.10%). Pasteurization is proven to improve the oxidative stability of oil body emulsions from soybean and peanut significantly. However, it can promote the oxidation of oil body emulsions from sunflower, sesame and walnut. These results provide evidence supporting the industrial application of oil bodies in salad, vegetable milk and other similar products.

Open Access Issue
Binding Mechanism and Conformation and Functional Changes of Soybean Protein-Baicalein Complexes
Food Science 2023, 44(4): 91-98
Published: 25 February 2023
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This study aimed to explore the binding mechanism of soybean β-conglycinin (7S)/glycinin (11S) with baicalein, and to investigate the changes in the conformational and functional properties of the complexes. Fourier transform infrared (FT-IR) spectroscopy indicated that baicalein could induce the transformation of β-sheets into α-helices and random coils. Intrinsic fluorescence spectra confirmed that the addition of baicalein made the structure of 7S and 11S more compact. The reaction of baicalein with the proteins took place spontaneously and quenched the protein fluorescence in a static manner. The 7S and 11S proteins bound to baicalein by hydrogen bonds and hydrophobic interactions, respectively. Molecular docking results showed that the affinity of baicalein to 11S was higher than that to 7S. Scanning electron microscopy (SEM) showed microstructure differences between 7S and 11S and their complexes. In addition, the surface hydrophobicity of 7S and 11S was decreased and the functional properties such as thermal stability were improved after combining with baicalein.

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