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Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent
Chen, Wei-Dong; Hu, Han-Hua; Wang, Yan-Dong; Chen, WD, China Univ Petr Beijing, Fac Chem Sci & Engn, Dept Biochem Engn, Beijing 102249, Peoples R China
2006-11-01
Source PublicationCHEMICAL ENGINEERING SCIENCE
ISSN0009-2509
Volume61Issue:21Pages:7068-7076
AbstractThe ion-exchange equilibrium of bovine serum albumin (BSA) to an anion exchanger, DEAE Spherodex M, has been studied by batch adsorption experiments at pH values ranging from 5.26 to 7.6 and ionic strengths from 10 to 117.1 mmol/l. Using the unadjustable adsorption equilibrium parameters obtained from batch experiments, the applicability of the steric mass-action (SMA) model was analyzed for describing protein ion-exchange equilibrium in different buffer systems. The parametric sensitivity analysis was performed by perturbing each of the model parameters, while holding the rest constant. The simulation results showed that, at high salt concentrations or low pHs close to the isoelectric point of the protein, the precision of the model prediction decreased. Parametric sensitivity analysis showed that the characteristic charge and protein steric factor had the largest effects on ion-exchange equilibrium, while the effect of equilibrium constant was about 70%-95% smaller than those of characteristic charge and steric factor under all conditions investigated. The SMA model with the relationship between the adjusted characteristic charge and the salt concentration can well predict the protein adsorption isotherms in a wide pH range from 5.84 to 7.6. It is considered that the SMA model could be further improved by taking into account the effect of salt concentration on the intermolecular interactions of proteins. (c) 2006 Elsevier Ltd. All rights reserved.; The ion-exchange equilibrium of bovine serum albumin (BSA) to an anion exchanger, DEAE Spherodex M, has been studied by batch adsorption experiments at pH values ranging from 5.26 to 7.6 and ionic strengths from 10 to 117.1 mmol/l. Using the unadjustable adsorption equilibrium parameters obtained from batch experiments, the applicability of the steric mass-action (SMA) model was analyzed for describing protein ion-exchange equilibrium in different buffer systems. The parametric sensitivity analysis was performed by perturbing each of the model parameters, while holding the rest constant. The simulation results showed that, at high salt concentrations or low pHs close to the isoelectric point of the protein, the precision of the model prediction decreased. Parametric sensitivity analysis showed that the characteristic charge and protein steric factor had the largest effects on ion-exchange equilibrium, while the effect of equilibrium constant was about 70%-95% smaller than those of characteristic charge and steric factor under all conditions investigated. The SMA model with the relationship between the adjusted characteristic charge and the salt concentration can well predict the protein adsorption isotherms in a wide pH range from 5.84 to 7.6. It is considered that the SMA model could be further improved by taking into account the effect of salt concentration on the intermolecular interactions of proteins. (c) 2006 Elsevier Ltd. All rights reserved.
SubtypeArticle
KeywordIon Exchange Adsorption Isothermal Protein Simulation Separations
DepartmentChina Univ Petr Beijing, Fac Chem Sci & Engn, Dept Biochem Engn, Beijing 102249, Peoples R China; Tianjin Univ, Sch Chem Engn & Technol, Dept Biochem Engn, Tianjin 300072, Peoples R China; Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Peoples R China
Subject AreaEngineering ; Chemical
DOI10.1016/j.ces.2006.07.036
WOS HeadingsScience & Technology ; Technology
Indexed BySCI
Language英语
WOS Research AreaEngineering
WOS SubjectEngineering, Chemical
WOS IDWOS:000241446700017
WOS KeywordBOVINE SERUM-ALBUMIN ; ION-EXCHANGE ; AQUEOUS-SOLUTIONS ; CHROMATOGRAPHY ; RETENTION ; DIFFUSION ; KINETICS ; OPTIMIZATION ; SEPARATIONS ; SIMULATION
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Cited Times:12[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/152342/8814
Collection期刊论文
Corresponding AuthorChen, WD, China Univ Petr Beijing, Fac Chem Sci & Engn, Dept Biochem Engn, Beijing 102249, Peoples R China
Affiliation1.China Univ Petr Beijing, Fac Chem Sci & Engn, Dept Biochem Engn, Beijing 102249, Peoples R China
2.Tianjin Univ, Sch Chem Engn & Technol, Dept Biochem Engn, Tianjin 300072, Peoples R China
3.Chinese Acad Sci, Inst Hydrobiol, Wuhan 430072, Peoples R China
Recommended Citation
GB/T 7714
Chen, Wei-Dong,Hu, Han-Hua,Wang, Yan-Dong,et al. Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent[J]. CHEMICAL ENGINEERING SCIENCE,2006,61(21):7068-7076.
APA Chen, Wei-Dong,Hu, Han-Hua,Wang, Yan-Dong,&Chen, WD, China Univ Petr Beijing, Fac Chem Sci & Engn, Dept Biochem Engn, Beijing 102249, Peoples R China.(2006).Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent.CHEMICAL ENGINEERING SCIENCE,61(21),7068-7076.
MLA Chen, Wei-Dong,et al."Analysis of steric mass-action model for protein adsorption equilibrium onto porous anion-exchange adsorbent".CHEMICAL ENGINEERING SCIENCE 61.21(2006):7068-7076.
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