高压处理对α-乳白蛋白与锦葵色素-3-葡萄糖苷相互作用的影响。
Effects of high pressure processing on the interaction of α-lactalbumin and pelargonidin-3-glucoside.
机构信息
College of Food Science and Nutritional Engineering, China Agricultural University, Beijing Advanced Innovation Center for Food Nutrition and Human Health, National Engineering Research Centre for Fruit and Vegetable Processing, Key Lab of Fruit and Vegetable Processing, Ministry of Agriculture, Beijing Key Laboratory for Food Non-thermal Processing, Beijing 100083, China.
Institute of Quality Standard & Testing Technology for Agro-Products, Chinese Academy of Agricultural Sciences, Key Laboratory of Agro-food Safety and Quality, Ministry of Agriculture, Beijing 100081, China.
出版信息
Food Chem. 2019 Jul 1;285:22-30. doi: 10.1016/j.foodchem.2019.01.129. Epub 2019 Jan 31.
The effects of high pressure processing on the binding interactions of α-lactalbumin and pelargonidin-3-glucoside were studied using the fluorescence quenching, molecular dynamic simulation and molecular docking analysis. The results of fluorescence quenching indicated that the high pressure processing significantly increased the quenching constants of α-lactalbumin at pH 7.4 and pH 8.0. The accessible fraction at pH 8.0 was significantly increased, while the fractions at pH 6.0 and pH 7.4 were increased without significant difference. Molecular dynamic simulation and docking results demonstrated that the coil structures and locations, and the residues structures in the binding site of α-lactalbumin were affected, the binding site was the typical binding site of calcium ion and not changed during the processing. The dissociation constant of histidine residues was in the range of 6.13 to 6.83, the charge on the residues increased when pH value increased, affected the binding interactions and caused the quenching constant difference.
采用荧光猝灭、分子动力学模拟和分子对接分析研究了高压处理对α-乳白蛋白与锦葵色素-3-葡萄糖苷结合相互作用的影响。荧光猝灭结果表明，高压处理在 pH 7.4 和 pH 8.0 时显著增加了α-乳白蛋白的猝灭常数。在 pH 8.0 时，可及分数显著增加，而在 pH 6.0 和 pH 7.4 时，可及分数增加，但无显著差异。分子动力学模拟和对接结果表明，α-乳白蛋白的卷曲结构和位置以及结合部位的残基结构受到影响，结合部位是典型的钙离子结合部位，在处理过程中没有改变。组氨酸残基的离解常数在 6.13 到 6.83 之间，随着 pH 值的升高，残基上的电荷增加，影响了结合相互作用并导致猝灭常数的差异。
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