College of Food Science and Engineering , Ocean University of China , Qingdao 266003 , People's Republic of China.
Marine Fisheries Research Institute of Zhejiang , Zhoushan 316021 , Zhejiang , People's Republic of China.
J Agric Food Chem. 2019 Mar 13;67(10):2980-2990. doi: 10.1021/acs.jafc.8b06679. Epub 2019 Mar 5.
In this study, a novel vector for fucoxanthin (FX) was constructed using the ligand-binding property of whey protein isolate and its subsequent heteroprotein complex coacervation with lysozyme. The results showed that FX could quench the intrinsic fluorescence of the whey protein isolate by a static mechanism, indicating that they could spontaneously form a nanocomplex through non-covalent interactions. Moreover, the structural and electrostatic properties of the resulting whey protein were different from those before the binding of FX, and this could be well explained by molecular dynamics simulation. The size and ζ-potential tests showed that when the whey protein isolate was combined with FX and then coacervated with lysozyme, the heteroprotein ratio and pH, which affect the coacervation process, also changed compared to those of the free whey protein isolate. FT-IR spectroscopy results showed that FX was successfully encapsulated into complex coacervates. In addition, the heteroprotein system exhibited a higher loading efficiency and also provided a better protection for FX in heating, storage, and simulated gastrointestinal environments.
在这项研究中，利用乳清蛋白分离物的配体结合特性及其与溶菌酶的后续异源蛋白复合凝聚，构建了一种新型的岩藻黄质（FX）载体。结果表明，FX 可以通过静态机制猝灭乳清蛋白分离物的固有荧光，表明它们可以通过非共价相互作用自发形成纳米复合物。此外，所得乳清蛋白的结构和静电性质与 FX 结合前的性质不同，这可以通过分子动力学模拟得到很好的解释。大小和 ζ-电位测试表明，当乳清蛋白分离物与 FX 结合，然后与溶菌酶共凝聚时，与游离乳清蛋白分离物相比，影响共凝聚过程的异源蛋白比和 pH 值也发生了变化。傅里叶变换红外光谱结果表明，FX 已成功包封在复合凝聚体中。此外，该异源蛋白体系表现出更高的负载效率，并在加热、储存和模拟胃肠道环境中为 FX 提供了更好的保护。
