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Evaluation of the interactions between rosmarinic acid and bovine milk casein

机译：迷迭香酸和牛酪蛋白相互作用的评价

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Polyphenols can interact with proteins, which gives rise to a significant loss of their biological properties. The objective of this research was the study of interactions in model systems composed of the polyphenol rosmarinic acid (RA) and bovine milk alpha-s1-casein, beta-casein and kappa-casein. Radical cation quenching assay (ABTS, 2,2'-azinobis-3-ethyl-benzothiazoline-6-sulfonic-acid), optical density, liquid chromatography (RP-HPLC, reverse phase-high performance liquid chromatography, and SEC, size exclusion chromatography), dynamic light scattering (DLS) and zeta-potential, Fourier transform infrared spectroscopy (FTIR) and differential scanning calorimetry (DSC) were used for the screening of the interactions at 0, 3 and 24 h of storage time and at the refrigeration temperature 4 degrees C. Interactions were assessed at the pH of the complexes in water, 6.8, and at acidic pH 3 and 4.5. Results showed the occurrence of non-covalent interactions such as hydrophobic, hydrogen bonding and dipole-dipole. Radical cation quenching activity of RA significantly decreased in the presence of caseins, meaning that the amount of free RA diminished. Higher and the same degree of interaction were observed for alpha-s1-casein and beta-casein. Complex dimensions were different depending on pH, time and on the primary and secondary structure of caseins. Interactions were shown to be favoured at the lowest pH, where complexes are biggest, and reversible at all pH conditions tested. The results of this study must be complemented with the analysis of more complex systems to take into account the effect of other milk components - lipids, sugars and minerals - on the interaction of RA.
机译：多酚可以与蛋白质相互作用，从而导致其生物学特性的重大损失。这项研究的目的是研究由多酚迷迭香酸（RA）和牛乳α-s1-酪蛋白，β-酪蛋白和kappa-酪蛋白组成的模型系统中的相互作用。自由基阳离子猝灭测定（ABTS，2,2'-叠氮基双-3-乙基-苯并噻唑啉-6-磺酸），光密度，液相色谱（RP-HPLC，反相高效液相色谱和SEC，尺寸排阻色谱），动态光散射（DLS）和ζ电势，傅里叶变换红外光谱（FTIR）和差示扫描量热法（DSC）用于筛选在储存时间0、3和24小时以及在冷藏时的相互作用温度为4℃。在水中复合物的pH为6.8，在酸性pH为3和4.5下评估相互作用。结果表明发生了非共价相互作用，例如疏水，氢键和偶极-偶极相互作用。在酪蛋白存在下，RA的自由基阳离子猝灭活性显着降低，这意味着游离RA的数量减少了。对于α-s1-酪蛋白和β-酪蛋白，观察到更高和相同程度的相互作用。复杂的尺寸取决于pH，时间以及酪蛋白的一级和二级结构。研究表明，在最低pH值（复合物最大）下，相互作用是有利的，并且在所有测试的pH条件下都可逆。该研究的结果必须与更复杂系统的分析相辅相成，以考虑其他乳成分（脂质，糖和矿物质）对RA相互作用的影响。

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