Ion-exchange equilibria of lysozyme myoglobin and bovine serum albumin

Whitley, Roger D.; Wachter, Ralph F.; Liu, F.; Wang, N.-H.L.

doi:10.1016/s0021-9673(01)92653-6

Cited by 101 publications

(50 citation statements)

References 11 publications

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“…However, in the case of protein ion exchange, some of the above assumptions are not completely realistic turning the Langmuir model as an empirical mathematical model more than a rigorous theoretical one. Moreover, it was reported by many authors [18], [13], [19] that Langmuir model can be used to describe adsorption isotherms at constant pH and ionic strength.…”

Section: Theorymentioning

confidence: 99%

Equilibrium and Kinetics of High Molecular Weight Protein Uptake in Ion Exchange Chromatography

Wakkel¹,

Alfenore²,

Mathé³

et al. 2015

IJCEA

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Abstract-Equilibrium and kinetic experiments have been carried out in order to study the effect of protein size in the purification of high molecular weight (HMW) proteins by IEC. The current work focused on two proteins uptake by Q HyperZ chromatographic media. Bovine Serum Albumin (BSA) and ferritin have been selected due to their close isoelectric point (4.9 and 4.4 respectively) and their different molecular weight (66.5 and 450 kDa respectively). As usually reported in the literature, equilibrium uptake for BSA has been higher than for ferritin at the same buffer conditions (pH, ionic strength), suggesting complex phenomena for ferritin uptake. Moreover, contrary to the general rule in ion-exchange processes, ferritin uptake has not been really affected by the increase of NaCl concentration. In fact, no significant change in the ferritin uptake has been quantified with the increasing of salt concentration from 0 to 100 mM. However, the kinetics of ferritin ion exchange has showed a classical behaviour, according to the homogenous diffusion model. The determination of the effective diffusion coefficient for ferritin has been possible from transient uptake at different protein initial concentrations. Thus, in spite of its large size, ferritin seems to diffuse inside the macro-porous anion-exchange particles.

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Section: Theorymentioning

confidence: 99%

Equilibrium and Kinetics of High Molecular Weight Protein Uptake in Ion Exchange Chromatography

Wakkel¹,

Alfenore²,

Mathé³

et al. 2015

IJCEA

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show abstract

“…Then, the fast association and total dissociation may alternatively dominate the adsorption process with no equilibrium achieved and the observed equilibrium concentration would be accordingly zero. This phenomenon would happen only when the feed protein concentration is very dilute, such as the criterion in eqn (9).…”

Section: Adsorption Isothermsmentioning

confidence: 99%

“…Accordingly, a concave-down Scatchard plot may be more accurately modeled by a two-step adsorption process described above. Instead of using the complicated two-step adsorption model, however, a two-parameter adsorption equation, eqn (9), is adopted in this study. In addition to the advantages in simplicity and the capability of converting into kinetic form, this simple model also shows a good applicability for the affinity adsorption of pepsin and chymosin.…”

Section: Adsorption Isothermsmentioning

confidence: 99%

An isotherm model describing concave-down scatchard curve for heterogeneous affinity adsorption

Suen

1997

J. Chem. Technol. Biotechnol.

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: A new isotherm model, derived for a concave-down Scatchard curve, is presented to Ðt the experimental results for pepsin and chymosin adsorption to pepstatin A affinity membranes. The new model is converted into a kinetic expression and used for the Ðtting of association curves. The results from the new kinetic model show a better agreement with the experimental data than the Langmuir kinetic model. The new kinetic model is also used together with the affinity membrane model to predict the single-solute breakthrough curves, which performs well in matching the experimental curves.

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“…In those studies, the most frequently used ones are the Langmuir model and its various modified forms (Fritz and Schlunder, 1974;Hu et al, 1992). The Langmuir model can be used to describe adsorption isotherms at constant pH and ionic strength (Whitley et al, 1989;Skidmore et al, 1990, Bosma andWesselingh, 1998). To describe the influence of salt concentration on the equilibrium, the double-layer model (Ståhlberg et al, 1992;Roth and Lenhoff, 1993;Ståhlberg, 1999), the competitive Langmuir-Freundlich isotherm (James and Do, 1991) and the Langmuir model with an empirical relation between the equilibrium constant and the salt concentration (Hu et al, 1992) were developed.…”

Section: Introductionmentioning

confidence: 99%

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

Chen

Wang

2006

Chemical Engineering Science

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Ion-exchange equilibria of lysozyme myoglobin and bovine serum albumin

Cited by 101 publications

References 11 publications

Equilibrium and Kinetics of High Molecular Weight Protein Uptake in Ion Exchange Chromatography

Equilibrium and Kinetics of High Molecular Weight Protein Uptake in Ion Exchange Chromatography

An isotherm model describing concave-down scatchard curve for heterogeneous affinity adsorption

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

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