Abstract The incorporation of bioactive molecules is important to improve food functionality. Despite the low solubility of some bioactive molecules, e.g., flavonoids, their binding with proteins contribute to their incorporation. There are some studies regarding globular proteins as flavonoid nanocarriers, but binding between flavonoids and βCN monomers, which are flexible proteins, is less reported. Here, the thermodynamics and kinetics of naringin–β-casein (NR–βCN) binding were determined by fluorescence spectroscopy (FS) and surface plasmon resonance (SPR). FS indicated that NR binds with βCN close to Trp143 with K b 24 ° C = 2.71 × 104 m −1 and a key role of desolvation. SPR revealed that NR also binds far from Trp143 ( K b 24 ° C = 7.01 × 103 m −1) with small enthalpic and entropic temperature dependencies. We also present the kinetic parameters related to an intermediate complex formation, which was formed with minimal conformation and desolvation changes. Our results demonstrate βCN monomers as potential nanocarriers for NR.

中文翻译：

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β-酪蛋白单体作为潜在的类黄酮纳米载体：β-酪蛋白-柚皮苷结合的热力学和动力学通过荧光光谱和表面等离子体共振

摘要 生物活性分子的掺入对于改善食品功能很重要。尽管一些生物活性分子（例如类黄酮）的溶解度低，但它们与蛋白质的结合有助于它们的掺入。有一些关于球状蛋白质作为类黄酮纳米载体的研究，但黄酮类化合物与βCN单体之间的结合是柔性蛋白质，报道较少。在这里，柚皮素-β-酪蛋白（NR-βCN）结合的热力学和动力学通过荧光光谱（FS）和表面等离子体共振（SPR）确定。FS 表明NR 与βCN 结合接近Trp143，K b 24 °C = 2.71 × 104 m -1 和去溶剂化的关键作用。SPR 显示 NR 还结合远离 Trp143 (K b 24 °C = 7.01 × 103 m -1) 的小焓和熵温度依赖性。我们还介绍了与中间复合物形成相关的动力学参数，该复合物形成时具有最小的构象和去溶剂化变化。我们的结果表明 βCN 单体可作为 NR 的潜在纳米载体。