Abstract：
The elucidation of the interaction mechanism between phospholipids and milk proteins within emulsions is pivotal for comprehending the properties of infant formula fat globules. In this study, multispectral methods and molecular docking were employed to explore the relationship between phosphatidylcholine (PC) and whey protein isolate (WPI). Observations indicate that the binding constant, alongside thermodynamic parameters, diminishes as temperature ascends, hinting at a predominantly static quenching mechanism. Predominantly, van der Waals forces and hydrogen bonds constitute the core interactions between WPI and PC. This assertion is further substantiated by Fourier transform infrared spectroscopy, which verifies PC\'s influence on WPI\'s secondary structure. A detailed assessment of thermodynamic parameters coupled with molecular docking reveals that PC predominantly adheres to specific sites within α-lactalbumin, β-lactoglobulin, and bovine serum albumin, propelled by a synergy of hydrophobic interactions, hydrogen bonding, and van der Waals forces, with binding energies noted at -5.59, -6.71, and -7.85 kcal/mol, respectively. An increment in PC concentration is observed to amplify the emulsification properties of WPI whilst concurrently diminishing the zeta potential. This study establishes a theoretical foundation for applying the PC-WPI interaction mechanism in food.
摘要：
阐明乳液中磷脂和乳蛋白之间的相互作用机制对于理解婴儿配方脂肪球的特性至关重要。在这项研究中,采用多光谱方法和分子对接技术探讨磷脂酰胆碱（PC）与乳清分离蛋白（WPI）的关系。观察表明，结合常数，除了热力学参数，随着温度的升高，暗示主要是静态淬火机制。主要是,范德华力和氢键构成了WPI和PC之间的核心相互作用。傅里叶变换红外光谱进一步证实了这一论断，用于验证PC对WPI二级结构的影响。对分子对接的热力学参数的详细评估表明，PC主要粘附于α-乳清蛋白内的特定位点，β-乳球蛋白，和牛血清白蛋白,由疏水相互作用的协同作用推动，氢键,和范德华部队,结合能分别为-5.59、-6.71和-7.85kcal/mol，分别。观察到PC浓度的增加放大了WPI的乳化性质,同时降低了ζ电位。本研究为PC-WPI相互作用机制在食品中的应用奠定了理论基础。
