Parallel transport of BSA by surface and pore diffusion in strongly basic chitosan

Yoshida, Hiroyuki; Yoshikawa, Motonobu; Kataoka, Takeshi

doi:10.1002/aic.690401213

Cited by 164 publications

(101 citation statements)

References 26 publications

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“…[27][28][29] A few other sets of experimental data on the surface and lateral diffusion of various solutes in RPLC and of macromolecules on other stationary phases are available and listed in Table 2. Results previously published [27][28][29][30][31][32][33][34][35] suggest that Ds is a few orders of magnitude 725 ANALYTICAL SCIENCES JULY 2000, VOL. 16 Fig.…”

Section: Derivation Of An Estimate Of Dsmentioning

confidence: 95%

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

Miyabe

Guiochon

2000

ANAL. SCI.

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Molecular imprinting is a most attractive method of preparation of dedicated stationary phases for chromatography. Its use for enantioseparations is attracting considerable interest. 1,2 Imprinted materials can provide a very high selectivity for the objective compound, i.e., the imprinted molecule. [1][2][3][4][5] Although analytical applications are rapidly developing, the situation on the preparative front is less rosy. 1 Columns packed with imprinted stationary phases exhibit a poor efficiency and elution peaks are often unsymmetrical, especially for the more retained enantiomer. Sellergren et al. 1,2 suggested that the nonlinear behavior of the adsorption isotherm was the main cause of the broad and unsymmetrical bands observed for L-phenylalanine anilide (PA) on an L-PA imprinted chiral stationary phase. Although the possibility of a slow mass transfer kinetics was also pointed out, no detailed study supported this assumption. Yet, information on the mass transfer characteristics of imprinted stationary phases is necessary to clarify strategies for the improvement of these materials.Most kinetic studies in chromatography assume that four mass transfer processes are involved in a column, (1) axial dispersion, (2) fluid-to-particle mass transfer, (3) intraparticle diffusion, and (4) adsorption/desorption. 6 The contributions of these four processes to peak spreading are evaluated separately. Axial dispersion and the fluid-to-particle mass transfer resistance are inherent to flow processes through packed beds. They are well understood, relatively easy to control, and their contributions are often small. By contrast, intraparticle diffusion and adsorption/desorption give often larger contributions to the mass transfer resistance in the column. Their properties are intrinsic to each packing material and they are still often poorly understood. In order to evaluate the actual performance of packing materials, the characteristics of the mass transfer kinetics inside stationary phase particles must be clarified.Sajonz et al. 7 measured the adsorption equilibrium isotherm and the mass transfer kinetics of L-and D-PA on a polymeric stationary phase imprinted with L-PA, using a staircase frontal analysis method. The isotherm was well represented by either the Bi-Langmuir or the Freundlich models, but not by the simple Langmuir isotherm. The equilibrium data suggested that the distribution of the adsorption energy on the surface of the imprinted stationary phase is heterogeneous and showed that this phase has a high selectivity for the imprinted L-enantiomer. The lumped mass transfer rate coefficient (km,L) was calculated from each single breakthrough curve by applying the transport model of chromatography. 6 The values of km,L increased with increasing concentration of the enantiomers. The extent of the positive concentration dependence of km,L was larger for L-PA than for D-PA. It is expected that a more detailed analysis of the overall mass transfer rate parameter, km,L, could provide new, useful information and all...

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Section: Derivation Of An Estimate Of Dsmentioning

confidence: 95%

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

Miyabe

Guiochon

2000

ANAL. SCI.

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“…[1][2][3][4] The mass transfer in the porous material/solution system has been often analyzed in terms of diffusion in pores of the material. [5][6][7][8][9][10] However, analysis of the mass transfer mechanism is generally difficult.…”

Section: Introductionmentioning

confidence: 99%

External and Intraparticle Diffusion of Coumarin 102 with Surfactant in the ODS-silica Gel/water System by Single Microparticle Injection and Confocal Fluorescence Microspectroscopy

Nakatani

Matsuta

2015

ANAL. SCI.

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“…For bioprocess applications where large diameter adsorbent beads and high mobile phase velocities are typically utilized, chromatographic efficiency is nearly completely determined by mass transfer kinetics [25]. Accordingly, numerous studies have been devoted to protein mass transfer in chromatography media (e.g., [26][27][28][29][30][31]). However, to our knowledge, the effects of urea on protein-binding capacity, chromatography retention, and intraparticle mass transfer in ion-exchange columns have not been investigated in a systemic fashion.…”

Section: Introductionmentioning

confidence: 99%

Impact of denaturation with urea on recombinant apolipoprotein A‐I_Milano ion‐exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics

Hunter

Suda²,

Das

et al. 2007

Biotechnology Journal

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We have studied the equilibrium uptake behavior and mass transfer rate of recombinant apolipoprotein A-I Milano (apo A-I M ) on Q Sepharose HP under non-denaturing, partially denaturing, and fully denaturing conditions. The protein of interest in this study is composed of amphipathic α helices that serve to solubilize and transport lipids. The dual nature of this molecule leads to the formation of micellar-like structures and self association in solution. Under non-denaturing conditions equilibrium uptake is 134 mg/mL media and the isotherm is essentially rectangular. When fully denatured with 6 M urea, the equilibrium binding capacity decreases to 25 mg/mL media and the isotherm becomes less favorable. The decrease in both binding affinity and media capacity when the protein is completely denatured with 6 M urea can be explained by the loss of all alpha helical structure. The rate of apo A-I M mass transfer on Q Sepharose HP was characterized using a macropore diffusion model. Results of modeling studies indicate that effective pore diffusivity increases from 4.5 × 10 -9 cm 2 /s in the absence of urea to 6.0 × 10 -8 cm 2 /s when apo A-I M is fully denatured with 6 M urea. Based on light-scattering data reported for apo A-I, protein self association appears to be the dominant cause of slow protein mass transfer observed under non-denaturing conditions.

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Parallel transport of BSA by surface and pore diffusion in strongly basic chitosan

Cited by 164 publications

References 26 publications

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

External and Intraparticle Diffusion of Coumarin 102 with Surfactant in the ODS-silica Gel/water System by Single Microparticle Injection and Confocal Fluorescence Microspectroscopy

Impact of denaturation with urea on recombinant apolipoprotein A‐I_Milano ion‐exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics

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Parallel transport of BSA by surface and pore diffusion in strongly basic chitosan

Cited by 164 publications

References 26 publications

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

Kinetic Study of the Concentration Dependence of the Mass Transfer Rate Coefficient in Enantiomeric Separation on a Polymeric Imprinted Stationary Phase

External and Intraparticle Diffusion of Coumarin 102 with Surfactant in the ODS-silica Gel/water System by Single Microparticle Injection and Confocal Fluorescence Microspectroscopy

Impact of denaturation with urea on recombinant apolipoprotein A‐IMilano ion‐exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics

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Product

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Impact of denaturation with urea on recombinant apolipoprotein A‐I_Milano ion‐exchange adsorption: Equilibrium uptake behavior and protein mass transfer kinetics