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首页> 外文期刊>Fluid Phase Equilibria >Adsorption isotherms and thermodynamics of α-lactalbumin on an anionic exchanger
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Adsorption isotherms and thermodynamics of α-lactalbumin on an anionic exchanger

机译：α-乳白蛋白在阴离子交换剂上的吸附等温线和热力学

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The investigation of protein adsorption phenomena on solid surfaces is important for the development of purification processes. Knowledge of this equilibrium and the induced conformational changes of proteins is essential for its understanding. Thus, the adsorption behavior of α-lactalbumin (α-la) on an anionic exchange resin, Streamline~? Q XL, at pH 7.4 and four different temperatures was studied. It was observed that the adsorptive capacity decreases with higher temperatures. Five isotherm models were fitted to the experimental data, where the Langmuir and Jovanovic models were the best. The Toth model was also reduced to the Langmuir model. The results indicated that the adsorption process is homogeneous, indicating Langmuirian behavior. Thermodynamic analysis based on the van't Hoff equation shows a spontaneous, endothermal and entropy driven process. The process became more spontaneous at higher temperatures, possibly less endothermal and unfold of the protein structure caused a negative effect on entropy associated to α-la conformational changes and small ions binding to the adsorbent, reflected by the reduction of maximum adsorptive capacity of the adsorbent.
机译：蛋白质在固体表面上的吸附现象的研究对于纯化工艺的发展很重要。了解这种平衡和诱导的蛋白质构象变化对于理解它至关重要。因此，α-乳白蛋白（α-la）在阴离子交换树脂Streamline上的吸附行为。研究了在pH 7.4和四个不同温度下的Q XL。观察到，吸附能力随着温度的升高而降低。将五个等温线模型拟合到实验数据，其中Langmuir和Jovanovic模型是最好的。 Toth模型也简化为Langmuir模型。结果表明，吸附过程是均匀的，表明了朗缪尔行为。基于van't Hoff方程的热力学分析显示了自发的，吸热的和熵驱动的过程。该过程在较高温度下变得更加自发，可能更少的内热和蛋白质结构的展开对与α-la构象变化和与吸附剂结合的离子相关的熵产生负面影响，这反映在吸附剂最大吸附能力的降低上。

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