A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

Bian, Liujiao; Yang, Xinlin; Liu, Li

doi:10.1002/cjoc.200790044

Cited by 3 publications

(3 citation statements)

References 23 publications

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“…The applicability of this method was confirmed with some small solute molecules and protein molecules in some chromatographic systems at different solvent concentrations and experimental temperatures. 17,18 Then the effect of experimental temperatures on their thermodynamic equilibrium constants K SL can be discussed.…”

Section: Resultsmentioning

confidence: 99%

“…It has experimentally proven that for different solute molecules on different chromatographic media, their frontal analysis data can be described well by this equation, 17 and the thermodenaturation behavior of Bacillus subtilis α-amylase on five kinds of chromatographic media was studied with this frontal analysis equation. 18 Therefore, in this paper, this equation is also used to determine the thermodynamic equilibrium constant K SL of some aromatic hydrocarbons and Bacillus subtilis α-amylases on different chromatographic media.…”

Section: Frontal Analysis Systemsmentioning

confidence: 99%

“…All the volumes occupied by the bulk solu- In a previous paper, 17 a simple frontal analysis equation for solute molecule adsorption on a chromatographic medium was presented, which gives the relationship between the average breakthrough time t 0 in a break-through curve and the feed solute concentration c f in a feed solution:…”

Section: Frontal Analysis Systemsmentioning

confidence: 99%

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Thermodynamics and Extra‐thermodynamics of Bacillus subtilis α‐Amylase in Some Chromatographic Systems

et al. 2009

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The thermodynamics and extra-thermodynamics of Bacillus subtilis α-amylase in five kinds of chromatographic systems were studied by determining their adsorption equilibrium constant K SL , enthalpy change, entropy change, free energy change and compensation temperature under different temperature areas. The results showed that on an RP-C 18 reversed-phase medium, a Zn-chelated Sepharose fast-flow affinity medium and a WCX-1 cation-exchange medium, their ln K SL separately linearly changed with the reciprocal of absolute temperatures under two different temperature ranges of 13-30 and 30-50 ℃; and on PEG-400 and modified PEG-400 hydrophobic media, their ln K SL separately linearly decreased with the reciprocal of absolute temperatures under the temperature areas of 13-40 and 13-30 ℃, while when the temperatures were separately over 40 and 30 ℃, they violently decreased with the reciprocal of absolute temperatures. Through studying the relations among the enthalpy change, entropy change, free energy change and the conformational change of α-amylase under the different temperature areas, it was found that on the RP-C 18 reversed-phase medium and Zn-chelated Sepharose fast-flow affinity medium under the temperature range of 30-50 ℃ and on the WCX-1 cation-exchange medium under the temperature range of 13-30 ℃, their adsorption procedures were driven by both the enthalpy change and the entropy change; while on the Zn-chelated Sepharose fast-flow affinity medium under the temperature range of 13-30 ℃, on the WCX-1 cation-exchange medium under the temperature range of 30-50 ℃ and on the PEG-400 and modified PEG-400 hydrophobic media under the temperature range of 13-65 ℃, their adsorption procedures were driven only by the entropy change. Finally, by comparing the compensation temperatures of α-amylase in these chromatographic systems each other, it was further found that their enthalpy changes could be compensated only with their entropy changes rising from their conformational change.

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Section: Resultsmentioning

confidence: 99%

Section: Frontal Analysis Systemsmentioning

confidence: 99%

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Thermodynamics and Extra‐thermodynamics of Bacillus subtilis α‐Amylase in Some Chromatographic Systems

et al. 2009

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Studies on the Thermodenaturation Behavior of Bacillus subtilisα‐Amylase on Chromatographic Media

Bian¹,

Wang

Yang

et al. 2008

Chin. J. Chem.

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The thermodenaturation behavior of Bacillus subtilis α-amylase on some chromatographic media was studied by determining their adsorption parameters with frontal analysis. The experimental results show that on a RP-C 18 reversed-phase medium, a Chelating Sepharose Fast-Flow chelated by Zn 2＋ affinity medium and a WCX-1 cation-exchange medium, a stable conformation of α-amylase molecule separately exists below or over 30 ; while ℃ on a PEG-400 hydrophobic medium and a modified PEG-400 medium, a stable conformation of α-amylase molecule separately exists below 40 and 30 , and w ℃ hen the experimental temperatures are separately over 40 and 30 , ℃ a drastically conformational change of α-amylase molecules can continuously take place. And by combining the intrinsic fluorescence emission spectrum and thermal inactivation profile of α-amylase in free solution and on the PEG-400 and modified PEG-400 hydrophobic media, it can be concluded that in liquid chromatographic procedure, chromatographic media can induce the conformational change of α-amylase molecules and promote their thermodenaturation; and in hydrophobic interaction chromatography, the higher the hydrophobicity of chromatographic medium, the lower the conformational change temperature of α-amylase molecules on the chromatographic medium.

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Derivation of adsorption capacity and adsorption isotherm by a single adsorbate concentration in liquid–solid system

et al. 2021

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A Simple Frontal Analysis Equation to Determine the Adsorption Parameters of Solute Molecules on Different Adsorbents

Cited by 3 publications

References 23 publications

Thermodynamics and Extra‐thermodynamics of Bacillus subtilis α‐Amylase in Some Chromatographic Systems

Thermodynamics and Extra‐thermodynamics of Bacillus subtilis α‐Amylase in Some Chromatographic Systems

Studies on the Thermodenaturation Behavior of Bacillus subtilisα‐Amylase on Chromatographic Media

Derivation of adsorption capacity and adsorption isotherm by a single adsorbate concentration in liquid–solid system

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