In this work, effect of casein and whey protein interaction on the stability, antioxidant potential, and bioaccessibility of sea buckthorn polyphenols was investigated. The results revealed that casein–polyphenol and whey protein–polyphenol interaction both decreased the in vitro antioxidant capacity of polyphenols. On the other hand, the protein–polyphenol complexes increased the stability of sea buckthorn polyphenols during simulated in vitro digestion. Moreover, both the casein–polyphenol and whey protein–polyphenol complexes exhibited an increased bioaccessibility of polyphenols (60.97–64.97%) in comparison to that of free polyphenolic extract (40.01%). The main bonding force between sea buckthorn polyphenols and the proteins was found to be a hydrophobic interaction, as revealed by ATR-FTIR, UV–vis, and fluorescence spectroscopy. The particle size of casein–polyphenol and whey protein–polyphenol complexes was in the nanosize region (650–983 nm). The low span factors of polyphenol–protein complexes revealed the narrow range of particle size distribution and thus more homogeneity in the particle size. This finding highlights that the interaction between casein and whey proteins with sea buckthorn polyphenols could protect these bioactive compounds against the influence of simulated digestion.

中文翻译：

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沙棘多酚与酪蛋白和乳清蛋白的非共价相互作用：对多酚稳定性、抗氧化潜力和生物可及性的影响

在这项工作中，研究了酪蛋白和乳清蛋白相互作用对沙棘多酚的稳定性、抗氧化潜力和生物可及性的影响。结果表明，酪蛋白-多酚和乳清蛋白-多酚相互作用均降低了多酚的体外抗氧化能力。另一方面，蛋白质-多酚复合物在体外模拟过程中增加了沙棘多酚的稳定性。消化。此外，与游离多酚提取物 (40.01%) 相比，酪蛋白-多酚和乳清蛋白-多酚复合物均表现出多酚的生物可及性增加 (60.97-64.97%)。ATR-FTIR、UV-vis 和荧光光谱表明，沙棘多酚与蛋白质之间的主要结合力是疏水相互作用。酪蛋白-多酚和乳清蛋白-多酚复合物的粒径在纳米范围内（650-983 nm）。多酚-蛋白质复合物的低跨度因子表明粒径分布范围较窄，因此粒径更均匀。