Particle‐size distribution effects in batch adsorption

Carta, Giorgio; Ubiera, Antonio

doi:10.1002/aic.690491208

Cited by 42 publications

(15 citation statements)

References 23 publications

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“…Staby et al [35] determined the particle size distributions of commercially available Toyopearl SP-650 C and SP-550 C and found them to be much wider, with a mean particle size of 80 μm for both adsorbents using Coulter counting and of 93 and 78 μm for SP-650 C and SP-550 C respectively using SEM. Transport modeling can account for the particle size distribution of the adsorbent [36][37][38], but the adsorbents studied here lie within sufficiently narrow distributions to allow monodispersity to be assumed.…”

Section: Resultsmentioning

confidence: 47%

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates

Langford

Yan

et al. 2007

Journal of Chromatography A

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Intraparticle transport of proteins usually represents the principal resistance controlling their uptake in preparative separations. In ion-exchange chromatography two limiting models are commonly used to describe such uptake: pore diffusion, in which only free protein in the pore lumen contributes to transport, and homogeneous diffusion, in which the transport flux is determined by the gradient in the total protein concentration, free or adsorbed. Several studies have noted a transition from pore to homogeneous diffusion with increasing ionic strength in some systems, and here we investigate the mechanistic basis for this transition. The studies were performed on a set of custom-synthesized methacrylate-based strong cation exchangers differing in ligand density into which uptake of two proteins was examined using confocal microscopy and frontal loading experiments. We find that the transition in uptake mechanism occurs in all cases studied, and generally coincides with an optimum in the dynamic binding capacity at moderately high flow rates. The transition appears to occur when protein-surface attraction is weakened sufficiently, and this is correlated with the isocratic retention factor k' for the system of interest: the transition occurs in the vicinity of k' ~ 3000. This result, which may indicate that adsorption is sufficiently weak to allow the protein to diffuse along or near the surface, provides a predictive basis for optimizing preparative separations using only isocratic retention data.

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Section: Resultsmentioning

confidence: 47%

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates

Langford

Yan

et al. 2007

Journal of Chromatography A

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“…A good fit including the long tailing portion of the breakthrough curve could again be obtained accounting for the PSD with a value D e = e p D p = 2.3 10 ±7 cm 2 /s. The relevant equations accounting for the PSD are discussed in [36].…”

Section: Reviewmentioning

confidence: 47%

“…With the best fit D e -value uptake rates are underpredicted for short times and overpredicted for long times, when all but the largest particles are completely saturated. However, accounting for the actual particle size distribution (PSD) (see [36] for the relevant equations) provides an excellent fit with D e = e p D p = 2.9 10 ±7 cm 2 /s, in good agreement with the values determined from isocratic and LGE experiments. Interestingly, the effect of the PSD is much less important when the isotherm is linear [36].…”

mentioning

confidence: 48%

“…However, accounting for the actual particle size distribution (PSD) (see [36] for the relevant equations) provides an excellent fit with D e = e p D p = 2.9 10 ±7 cm 2 /s, in good agreement with the values determined from isocratic and LGE experiments. Interestingly, the effect of the PSD is much less important when the isotherm is linear [36]. In this case, using the average particle size proves satisfactory except when the PSD is highly skewed or bimodal [34±35].…”

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confidence: 48%

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Protein Mass Transfer Kinetics in Ion Exchange Media: Measurements and Interpretations

2005

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The paper gives a summary of successful methods for measuring protein mass transfer kinetics in ion exchange matrices along with models needed to interpret experimental results. Both macroscopic methods (isocratic elution, gradient elution, batch adsorption, frontal analysis) and microscopic methods are considered. In all cases the main focus is the determination of the effective intraparticle diffusivity in order to permit a comparison of different stationary phases and provide a basis for predicting chromatographic process performance. Experimental results for representative systems are evaluated alongside the experimental and modeling aspects. Practical criteria for the selection of experimental conditions and the application of different models are discussed along with the advantages and disadvantages of the various approaches.

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“…However, all the simulated breakthrough curves contained a tailing, which the models could not predict. This phenomenon may result from the extra-column effects as well as the particle size distributions [25]. Displacement of impurities or protein dimmers may also play a role when adsorption is close to equilibrium.…”

Section: Simulation Of Breakthrough Curvescontrasting

confidence: 44%

Breakthrough Model of Recombinant Human-Like Collagen in Immobilized Metal Affinity Chromatography

Wang

Fan

Luo

2008

Appl Biochem Biotechnol

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The adsorption of recombinant human-like collagen by metal chelate media was investigated in a batch reactor and in a fixed-bed column. The adsorption equilibrium and kinetics had been studied by batch adsorption experiments. Equilibrium parameters and protein diffusivities were estimated by matching the models with the experimental data. Using the parameters of equilibrium and kinetics, various models, such as axial diffusion model, linear driving force model, and constant pattern model, were used to simulate the breakthrough curves on the columns. As a result, the most suitable isotherm was the Langmuir-Freundlich model, and the ionic strength had no effect on the adsorption capacity of chelate media. In addition, the pore diffusion model fitted very well to the kinetic data. The pore diffusivities decreased with increasing the initial protein concentration, however had little change with the ionic strength. The results also indicated that the models predict breakthrough curves reasonably well to the experimental data, especially at low initial protein concentration (0.3 mg ml(-1)) and low flow rate (34 cm h(-1)). By the results, we optimized the experimental conditions of a chromatographic process using immobilized metal affinity chromatography to purify recombinant human-like collagen.

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Particle‐size distribution effects in batch adsorption

Abstract: Mathematical models for pore-diffusion-controlled batch adsorption that take an ar

Cited by 42 publications

References 23 publications

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates

Chromatography of proteins on charge-variant ion exchangers and implications for optimizing protein uptake rates

Protein Mass Transfer Kinetics in Ion Exchange Media: Measurements and Interpretations

Breakthrough Model of Recombinant Human-Like Collagen in Immobilized Metal Affinity Chromatography

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