直接超高温 (dUHT) 牛奶被认为是下一代液态奶产品，因为它保留了比 UHT 牛奶更多的营养成分和更好的风味。然而，沉降和老化胶凝是开发 dUHT 牛奶的紧迫问题。乳清蛋白相互作用在 dUHT 牛奶不稳定中的作用很少见报道。在这项研究中，在 75 °C（预热）、145 °C（dUHT）和 37 °C 下，通过热力学、光谱学和计算机方法研究了 α-乳清蛋白 (α-La) 和 β-乳球蛋白 (β-Lg) 之间的相互作用C（存储）。结果表明，α-La 可以通过疏水性和放热反应与 β-Lg 相互作用。在 dUHT 和储存期间，α-La/β-Lg 复合物的平均分子量 (MW) 分布从 20.3 kDa 增加到 274.4 kDa。粒径从 135.53 ± 5.26 nm 增加到 153.50 ± 3.83 nm，zeta 电位从 −27.80 ± 5.90 mV 减少到 −7.73 ± 2.65 mV。纤维簇状蛋白桥促进 α-La/β-Lg 聚集体的形成。通过分子对接和动力学模拟探索了α-La和β-Lg之间的相互作用机制。结果发现，热处理降低了α-La和β-Lg的结合自由能，促进了α-La/β-Lg复合物的形成。静电和范德华力是结合的主要能量贡献者。UHT 处理增加了氢键的数量并削弱了疏水相互作用。这些发现表明，α-La 和 β-Lg 之间的相互作用在热处理和储存过程中形成聚集体，这有助于优化 dUHT 牛奶的加工和储存。静电和范德华力是结合的主要能量贡献者。UHT 处理增加了氢键的数量并削弱了疏水相互作用。这些发现表明，α-La 和 β-Lg 之间的相互作用在热处理和储存过程中形成聚集体，这有助于优化 dUHT 牛奶的加工和储存。静电和范德华力是结合的主要能量贡献者。UHT 处理增加了氢键的数量并削弱了疏水相互作用。这些发现表明，α-La 和 β-Lg 之间的相互作用在热处理和储存过程中形成聚集体，这有助于优化 dUHT 牛奶的加工和储存。

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Direct ultra-high temperature (dUHT) milk is considered as the next generation of liquid milk product because it keeps more nutritional ingredients and better flavor than UHT milk. However, sedimentation and age gelation are urgent problems to develop dUHT milk. The role of whey protein interaction in the destabilization of dUHT milk is rarely reported. In this study, the interaction between α-lactalbumin (α-La) and β-lactoglobulin (β-Lg) was investigated by thermodynamics, spectroscopy and silico approach at 75 °C (preheat), 145 °C (dUHT) and 37 °C (storage). The results showed that α-La could interact with β-Lg via hydrophobicity along with exothermic reaction. During dUHT and storage, the average molecular weight (MW) distribution of α-La/β-Lg complexes increased from 20.3 kDa to 274.4 kDa. The particle size increased from 135.53 ± 5.26 nm to 153.50 ± 3.83 nm and the zeta potential decreased from −27.80 ± 5.90 mV to −7.73 ± 2.65 mV. Fibrous cluster-like protein bridges promoted the formation of α-La/β-Lg aggregates. The interaction mechanism between α-La and β-Lg was explored by molecular docking and dynamics simulations. It was found that heat treatment reduced the binding free energy of α-La and β-Lg and promoted the formation of α-La/β-Lg complexes. Electrostatic and van der Waals were the main energy contributors to the binding. UHT treatment increased the number of hydrogen bonds and weakened the hydrophobic interaction. These findings indicate that the interaction between α-La and β-Lg forms aggregates during heat treatment and storage, which help to optimize process and storage of dUHT milk.