数字农科院2.0

Analysis of oil-water interface behavior of soy protein isolate-β-Lactoglobulin blend system and rheological properties in high internal phase emulsion

文献类型： 外文期刊

作者： Runkang Qiu;Peihua Ma;Zhaoshi Chen;Huanxiang Luo;Linggao Liu;Bei Fan;Litao Tong;Lili Wang;Liya Liu;Fengzhong Wang

作者机构：

关键词： Dynamic large oscillation rheology;High internal phase emulsions;Interfacial rheology;Soy protein isolate (SPI)

期刊名称： Food Hydrocolloids

ISSN： 0268-005X

年卷期： 2025 年 170 卷

页码：

收录情况： SCIE（2025版） ; ; EI（2025版）

摘要： Blends of soy protein isolate (SPI) and β-lactoglobulin (β-LG) might enhance the interfacial properties and rheology of high internal phase emulsions (HIPEs). However, the stabilization mechanism and correlation remain unclear. This work compared the behavior of the SPI-β-LG blend at the oil-water (O/W) interface with SPI and β-LG. The oscillatory rheology of HIPEs based on these protein blends was further investigate. In SPI-β-LG blends, a higher β-LG ratio increased β-turn structures and modified hydrophobic regions, resulting in better solubility, larger particle sizes, and improved flexibility. Compared with SPI, SPI-β-LG blends showed better diffusion, permeation, and arrangement at the O/W interface, significantly reducing the interfacial tension. After absorption, SPI-β-LG blends formed a viscoelastic interfacial film, whose response at large amplitude oscillatory dilatation (LAOD) depended on the β-LG ratio. Below 50 %, the film was thin, showing linear elasticity at LAOD (≥25 %). Above 50 %, the film possessed higher viscoelasticity, exhibiting strain softening during extension and compression at LAOD. HIPEs formed by SPI-β-LG blends with a higher β-LG ratio were observed in smaller oil droplets by optical microscopy and confocal laser scanning microscopy. Compared to SPI, rheology showed that the HIPEs stabilized by SPI-β-LG blends exhibited superior viscosity, gel strength, and viscoelasticity, showing greater elasticity and enhanced resistance to deformation under large amplitude oscillatory shear (LAOS). Thus, the correlation analysis suggested that the interfacial absorption behavior of SPI-β-LG blends showed strong relevance with the gel strength of HIPEs. This work helps to explore protein blends to enhance the quality of food-grade HIPEs.

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