Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent

Chen, Weidong; Hu, Hanhua; Wang, Yandong

doi:10.1016/j.ces.2006.07.036

Cited by 18 publications

(8 citation statements)

References 38 publications

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“…Several works have been conducted with the purpose of recovering and purifying whey proteins by different methods [8][9][10][11][12][13]. Ion-exchange chromatography (IEC) has been extensively employed in protein recovery and purification [14][15][16][17][18][19]. IEC is advantageous because separation typically occurs in the presence of aqueous buffers and hydrophilic surfaces as opposed to the harsher solvents and hydrophobic stationary phases used in reversed-phase chromatography.…”

Section: Introductionmentioning

confidence: 99%

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

Machado

Minim

Fontan

et al. 2015

Fluid Phase Equilibria

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Section: Introductionmentioning

confidence: 99%

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

Machado

Minim

Fontan

et al. 2015

Fluid Phase Equilibria

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“…The SMA model has been widely reported for predicting and describing nonlinear ion-exchange adsorption of proteins; − it has been applied to ion-exchange displacement systems − and metal-affinity systems. , The model parameters and accuracy of the SMA model in describing ion-exchange adsorption are influenced by pH and ionic strength, − as well as by the ligand density of the ion-exchange media . To obtain the SMA parameters, a simple experimental protocol was presented by Seidel-Morgenstern: a set of linear elution experiments and nonlinear frontal experiments for both proteins and displacer were carried out.…”

Section: Introductionmentioning

confidence: 99%

Adsorption of Proteins onto Ion-Exchange Chromatographic Media: A Molecular Dynamics Study

Liang

Fieg

Keil

et al. 2012

Ind. Eng. Chem. Res.

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Molecular dynamics (MD) simulations with coarse-grained models are used to investigate the adsorption process of proteins onto an ion-exchange chromatographic medium. The adsorption of human serum albumin (HSA) and bovine hemoglobin (bHb) on the anion exchanger Q Sepharose FF is studied. These two proteins have similar molecule sizes with different isoelectric points. To obtain a reliable set of data, simulations with different initial conditions are carried out for each protein. Convincingly, the results of the MD simulations are qualitatively consistent with those of previous experiments. HSA reaches a stable adsorption in all simulations, while the binding sites can differ. In contrast, bHb reaches a stable adsorption only in one simulation. Due to the stronger protein–ligand interaction of HSA, it adsorbs faster, stronger, and with more binding sites onto Q Sepharose FF than bHb. The spatial movements during the adsorption process and the adsorbed states are investigated in detail. Moreover, we studied the underlying physical relevance of two parameters (characteristic charge and steric factor) of the steric mass action (SMA) model for HSA and for bHb with MD simulations and compared them with the results of experiments. The results reveal that MD simulations are useful to interpret the physical consistence of the SMA parameters.

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“…Under this condition, BSA is closer to its p I , which reduces the adsorption, probably due to a lower net charge of the protein. This phenomenon has been reported before . However, to get a better handling of the SFF for ECP, the SFF has to be dried.…”

Section: Resultsmentioning

confidence: 62%

“…In the static approach, a solute and the adsorbent are mixed until the adsorption equilibrium is reached , . After quantitative analysis of the solute concentration in the bulk phase, the mass balance is closed to calculate the loading of adsorbent:

true q = \frac{(c_{0} - c_{e})}{m_{normalad}} V_{normalL}

…”

Section: Theorymentioning

confidence: 99%

Extended Elution by Characteristic Point Method for Characterization of Protein Ion‐Exchange Adsorption

et al. 2017

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An adequate characterization of adsorption isotherms is mandatory for chromatographic process development. Here, the elution by characteristic point (ECP) is a suitable method with low consumption of material and time. However, the ECP method requires a highly ideal behavior of the measured system. An innovative extended ECP approach is presented to characterize a non‐ideal system by the example of protein ion‐exchange adsorption. A marker, here bovine hemoglobin, is used to quantify all non‐idealities, e.g., convection, dispersion, or low number of theoretical plates. The system signal of the marker is used to compensate the system signal of the interesting solute, here bovine serum albumin. The resulting isotherm agrees well with the control results of a validated static approach.

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Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent

Cited by 18 publications

References 38 publications

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

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

Adsorption of Proteins onto Ion-Exchange Chromatographic Media: A Molecular Dynamics Study

Extended Elution by Characteristic Point Method for Characterization of Protein Ion‐Exchange Adsorption

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