School of Medicine, Shenzhen University, Shenzhen, Guangdong Province 518060, PR China.
School of Medicine, Shenzhen University, Shenzhen, Guangdong Province 518060, PR China.
Food Chem. 2019 Nov 15;298:125024. doi: 10.1016/j.foodchem.2019.125024. Epub 2019 Jun 15.
We investigated the allergenicity, digestibility and functional properties of whey protein isolate (WPI) after covalent conjugation with chlorogenic acid (CHA). The covalent conjugation of CHA may cause an unfolded protein structure. The WPI-CHA conjugate showed lower IgE binding capacity but higher intestinal digestibility than unmodified WPI. Furthermore, after digestion, the IgE binding capacity of β-lactoglobulin and α-lactoalbumin was lower in the digested WPI-CHA conjugate than digested WPI. Moreover, the solubility, emulsifying activity, foaming properties and antioxidant capacity of WPI were enhanced by covalent conjugation of CHA. Covalent conjugation with CHA might reduce the allergenicity in vitro of WPI by improving the functional properties of the protein.
我们研究了乳清蛋白分离物(WPI)与绿原酸(CHA)共价结合后的变应原性、消化率和功能特性。CHA 的共价结合可能导致蛋白质结构展开。与未修饰的 WPI 相比,WPI-CHA 缀合物的 IgE 结合能力较低,但肠道消化率较高。此外,在消化后,消化的 WPI-CHA 缀合物中β-乳球蛋白和α-乳白蛋白的 IgE 结合能力低于消化的 WPI。此外,WPI 的溶解度、乳化活性、泡沫性能和抗氧化能力通过与 CHA 的共价结合得到增强。通过改善蛋白质的功能特性,CHA 的共价结合可能降低 WPI 的体外变应原性。