Incorporating water-release and lateral protein interactions in modeling equilibrium adsorption for ion-exchange chromatography

Microcalorimetric study of the adsorption of PEGylated lysozyme on a strong cation exchange resin

“…Similar results were found in other studies on the adsorption energetics of proteins on chromatographic resins especially at high salt concentrations, adsorber loadings and near the isoelectric point of the proteins [10,11]. It has been shown that there also can be strongly endothermal effects in ion exchange chromatography similar to the behaviour found in hydrophobic interaction chromatography [12][13][14] and that entropic effects must play a major role in the adsorption of proteins on ion exchange resins [15].…”

Methods for characterization of biochromatography media

“…A microcolumn with ∼100–200 μL of resin can be integrated in a flow calorimeter. This system has been used for direct measurement of the heat of adsorption enabling thermodynamic analysis of protein adsorption on various resins .…”

Adsorptive behavior of α-lactalbumin on cation-exchange supermacroporous monolithic column

“…Composition, structure, chemical surface, magnitude and signal of charges and protein hydration degree are important [8]. Calorimetric studies have shown that protein adsorption process on ion exchange sorbents is often endothermic, suggesting that other processes are taking place besides the expected ion-exchange interaction [36,[42][43][44]. So, it is important to obtain more in-depth knowledge on energy variations (enthalpy and entropy) involved in this process.…”