College of Food Science and Engineering, Gansu Agricultural University, Lanzhou, 730070, China; College of Science, Gansu Agricultural University, Lanzhou, 730070, China.
College of Food Science and Engineering, Gansu Agricultural University, Lanzhou, 730070, China.
Food Chem. 2022 Aug 1;384:132508. doi: 10.1016/j.foodchem.2022.132508. Epub 2022 Feb 19.
The effects of change in pH, heat and ultrasound pre-treatments on the binding mechanism of quercetin (Q) with whey protein concentrate (WPC) were investigated, as well as the antioxidant capacity and stability of Q in the complexes. The main interaction between WPC and Q was hydrophobic and was not affected by pre-treatments. The binding affinity for Q with WPC at pH 7.4 after heating at 80 °C for 30 min, was the strongest, resulting in a WPC-Q complex with a more compact structure, the smallest particle size (184.43 ± 10.47 nm) and the largest ζ-potential (-20.58 ± 0.60 mV). This complex also provided the greatest stabilization of Q, when exposed to 37 °C and light. Complexation of WPC with Q reduced the ABTS radical scavenging capacity of Q, but enhanced its DPPH radical scavenging capacity and reducing power. These findings provide valuable information for optimizing the formation conditions of WPC-Q.
研究了 pH 值、热和超声预处理变化对乳清蛋白浓缩物（WPC）与槲皮素（Q）结合机制的影响，以及 Q 在复合物中的抗氧化能力和稳定性。WPC 和 Q 之间的主要相互作用是疏水性的，不受预处理的影响。在 80°C 加热 30 分钟后，在 pH 7.4 下，Q 与 WPC 的结合亲和力最强，形成了具有更紧凑结构的 WPC-Q 复合物，其粒径最小（184.43±10.47nm），ζ 电位最大（-20.58±0.60mV）。当暴露于 37°C 和光时，这种复合物还为 Q 提供了最大的稳定性。WPC 与 Q 的络合降低了 Q 的 ABTS 自由基清除能力，但增强了其 DPPH 自由基清除能力和还原能力。这些发现为优化 WPC-Q 的形成条件提供了有价值的信息。
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