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The effect of unadsorbed proteins on the physiochemical properties of the heteroaggregates of oppositely charged lactoferrin coated lutein droplets and whey protein isolate coated DHA droplets

机译:吸附蛋白对相反电荷的乳铁蛋白涂层叶黄素液滴和乳清蛋白分离涂层DHA液滴的杂碳杂种物质化学性质的影响

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It was reported that the controlled heteroaggregation of oppositely charged lactoferrin (LF)-lutein droplets and whey protein isolate (WPI)-DHA droplets enhanced the physicochemical properties of emulsions. The effect of the unadsorbed proteins on the physicochemical properties of the heteroaggregates of emulsions has not been clear. Therefore, the effects of unadsorbed proteins on the physicochemical stability of heteroaggregates of LF-lutein droplets and WPI-DHA droplets were investigated. The particle size, zeta-potential, transmission-physical stability, microstructure were observed by confocal laser scanning microscopy (CLSM) and cryo-scanning electron microscopy (cryo-SEM) and the chemical stability (lutein degradation and DHA oxidation) of the unwashed and washed heteroaggregates were measured. The results showed that compared with unwashed emulsions, the particle sizes and instability indexes of WPI-DHA emulsions, heteroaggregated LF-lutein/WPI-DHA emulsions and LF-lutein emulsions changed after washing. The instability index of washed-1 heteroaggregated LF-lutein/WPI-DHA emulsion was 10.5 times greater compared with the unwashed samples. The microstructure images showed that the washed single and heteroaggregated emulsions resulted in creaming. The unadsorbed proteins had a great protective effect on the physical stability of the emulsions, especially for the heteroaggregated LF-lutein/WPI-DHA emulsion. The degradation rate of lutein, lipid hydroperoxides and thiobarbituric acid reactive substance (TBARS) values of DHA in washed single and heteroaggregated emulsions were higher than those of the unwashed samples. This proved that the unadsorbed proteins dominated the physicochemical stabilities of heteroaggregates. This laid the foundation for the study of a delivery system of functional component heteroaggregates.
机译:据报道,对相反电荷的乳蛋白(LF) - 乳蛋白液滴和乳清蛋白分离物(WPI)-DHA液滴的受控杂种聚集增强了乳液的物理化学性质。未吸附蛋白对乳液的杂碳凝结物的物理化学性质的影响尚未清楚。因此,研究了未吸附蛋白对LF-叶黄素液滴和WPI-DHA液滴的杂凝集物物理化学稳定性的影响。通过共聚焦激光扫描显微镜(CLSM)和低温扫描电子显微镜(Cryo-SEM)和未知的化学稳定性(Cryo-SEM)和化学稳定性(Lutein降解和DHA氧化)观察到粒径,Zeta电位,透射性物理稳定性,微观结构测量洗涤的杂芳聚格。结果表明,与未洗过的乳液,WPI-DHA乳液的颗粒尺寸和不稳定性指标相比,杂种中的LF-叶黄素/ WPI-DHA乳液和LF-叶黄素乳液在洗涤后改变。与未洗过的样品相比,洗涤-1杂种的LF-叶黄素/ WPI-DHA乳液的不稳定性指数较大了10.5倍。微观结构图像显示洗涤的单碳和杂种中的乳液导致乳霜。未吸入的蛋白质对乳液的物理稳定性具有很大的保护作用,特别是对于杂种的LF-叶黄素/ WPI-DHA乳液。洗涤的单碳酸盐中DHA的叶黄素,脂质氢过氧化钠和硫酸硫脲酸反应物质(TBARS)值的降解率高于未洗过的样品。这证明了未吸附的蛋白质主要占杂碳凝集物的物理化学稳定性。这为研究功能组分杂种聚糖的输送系统奠定了基础。

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    《Food & Function》 |2018年第7期|共9页
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  • 中图分类 食品工业;
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