Beijing Advanced Innovation Center for Food Nutrition and Human Health (BTBU), School of Food & Chemical Engineering, Beijing Engineering and Technology Research Center of Food Additives, Beijing Higher Institution Engineering Research Center of Food Additives and Ingredients, Beijing Key Laboratory of Flavor Chemistry, Beijing Laboratory for Food Quality and Safety, Beijing Technology & Business University, Beijing, China.
Food Funct. 2018 Jul 17;9(7):3956-3964. doi: 10.1039/c8fo00371h.
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.
据报道,带相反电荷的乳铁蛋白(LF)-叶黄素液滴和乳清蛋白分离物(WPI)-二十二碳六烯酸(DHA)液滴的受控杂凝聚增强了乳液的物理化学性质。未吸附蛋白质对乳液杂凝聚的物理化学性质的影响尚不清楚。因此,研究了未吸附蛋白质对 LF-叶黄素液滴和 WPI-DHA 液滴杂凝聚物理化学稳定性的影响。通过共聚焦激光扫描显微镜(CLSM)和冷冻扫描电子显微镜(cryo-SEM)观察粒径、Zeta 电位、传输物理稳定性、微观结构,测量未清洗和清洗杂凝聚的化学稳定性(叶黄素降解和 DHA 氧化)。结果表明,与未清洗乳液相比,WPI-DHA 乳液、杂凝聚 LF-叶黄素/WPI-DHA 乳液和 LF-叶黄素乳液的粒径和不稳定性指数在清洗后发生了变化。清洗后的 1 号杂凝聚 LF-叶黄素/WPI-DHA 乳液的不稳定性指数比未清洗样品高 10.5 倍。微观结构图像表明,清洗后的单一和杂凝聚乳液导致了乳析。未吸附的蛋白质对乳液的物理稳定性有很大的保护作用,特别是对杂凝聚的 LF-叶黄素/WPI-DHA 乳液。清洗后的单一和杂凝聚乳液中叶黄素、脂质氢过氧化物和硫代巴比妥酸反应物(TBARS)值的 DHA 降解率均高于未清洗样品。这证明了未吸附的蛋白质主导了杂凝聚的物理化学稳定性。这为功能性成分杂凝聚体的传递系统的研究奠定了基础。