Effects of High Pressure Processing and Thermal Treatment on the Interaction between alpha-Lactalbumin and Pelargonium-3-Glucoside
文献类型： 外文期刊
作者： Tian, Xuezhi 1 ; Zou, Hui 1 ; Yang, Peiqing 1 ; Ma, Yan 1 ; Li, Yuwan 1 ; Zhao, Liang 1 ; Wang, Yongtao 1 ; Liao, Xiaojun 1 ;
作者机构： 1.China Agr Univ, Coll Food Sci & Nutr Engn, Beijing 100083, Peoples R China
2.Natl Engn Res Ctr Fruit & Vegetable Proc, Beijing 100083, Peoples R China
3.Minist Agr, Key Lab Fruit & Vegetable Proc, Beijing 100083, Peoples R China
4.Beijing Key Lab Food Nonthermal Proc, Beijing 100083, Peoples R China
5.Shandong Agr Univ, Food Sci & Engn Coll, Tai An 271000, Shandong, Peoples R China
6.Xinjiang Acad Agr Sci, Inst Agroprod Storage & Proc, Urumqi 830091, Peoples R China
关键词： high pressure processing; thermal treatment; alpha-Lactalbumin; pelargonidin-3-glucoside; binding behavior; interaction
期刊名称：MOLECULES （ 影响因子：4.927； 五年影响因子：5.11 ）
ISSN：
年卷期： 2022 年 27 卷 15 期
页码：
收录情况： SCI
摘要： In this study, high pressure processing (HPP) and thermal treatment were comparatively evaluated by examining their impacts on the binding behavior and interaction between alpha-lactalbumin (alpha-La) and pelargonium-3-glucoside (P3G) under pH values of 6.0, 7.4, and 8.0. The methods of circular dichroism spectroscopy, fluorescence quenching, dynamic light scattering, and molecular simulation were used to characterize the effects of processing-induced changes in protein structure, size distribution, binding site conformation, and residue charges on their binding characteristics between them. The results indicated that the thermal treatments significantly increased the quenching constants of the complex at pH 7.4/8.0 and 60/80 degrees C, as well as the accessible fraction of protein at pH 8.0/80 degrees C. Both HPP and thermal treatments increased the random coil content and showed limited effects on the alpha-helix and beta-sheet contents of alpha-La and caused the aggregation of the complex to varying degrees. Molecular dynamic simulation and docking analyses revealed that the binding site of the complex did not change under different processing conditions, but the solvent-accessible surface area varied under different conditions.
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