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Implications from γ-globulin adsorption onto cation exchangers fabricated by sequential alginate grafting and sulfonation

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Chinese Journal of Chemical Engineering 2021年第1期34卷 121-125页

作者： Xianxiu Li Yan Sun Xiaoyan Dong Department of Biochemical Engineering School of Chemical Engineering and TechnologyTianjin UniversityTianjin 300354China Key Laboratory of Systems Bioengineering and Frontiers Science Center for Synthetic Biology(Ministry of Education) Tianjin UniversityTianjin 300072China

Our previous work proved that high adsorption capacity and uptake rate of lysozyme were achieved on alginate(Alg)-grafted re sin with an ionic capacity(IC) of 240 mmol·L^(-1)(Alg-FF-240).Moreover,the salt-tolerant feature of Alg-FF-230 was improved by using sequential alginate grafting and sulfonation strategy.Inspired by the enhanced adsorption performance of lysozyme,we have herein proposed to investigate the static and dynamic adsorption behaviors of γ-globulin on a series of Alg-grafted resins with different grafting densities and sulfonation degrees.The adsorption ca pacity of γ-globulin decreased with increa sing alginate-grafting density(IC) from 160 to 230 mmol·L^(-1) at 0 mmol·L^(-1) NaCl because of the steric hindrance caused by the alginate-grafting layer.Effects of ionic strength(IS) indicated that the adsorption capacities of the resins with the IC value of 230-370 mmol·L^(-1) were much higher than CM Sepharose FF at 50-100 mmol·L^(-1) NaCl,and the uptake rate of Alg-FF-230 was about twice as much as that of CM Sepharose FF.This work demonstrated the important effects of alginate-grafting layer and IS in γ-globulin adsorption behavior,which would be helpful in the design of Alggrafted resins and the selection of proper IS condition for protein purification.

关键词： Alginate Sulfonation γ-globulin Adsorption capacity Uptake rate

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Fabrication of high-capacity cation-exchangers for protein adsorption: Comparison of grafting-from and grafting-to approaches

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Frontiers of Chemical Science and Engineering 2019年第1期13卷 120-132页

作者： Ming Zhao Run Liu Jian Luo Yan Sun Qinghong Shi Department of Biochemical Engineering School of Chemical Engineering and Technology Tianjin University Tianjin 300350 China Key Laboratory of Systems Bioengineering (Ministry of Education) Tianjin University Tianjin 300072 China State Key Laboratory of Biochemical Engineering Institute of Process Engineering Chinese Academy of Sciences Beijing 100190 China

In this work, we have synthesized two polymer-grafted cation exchangers: one via the grafting-from approach, in which sulfopropyl methacrylate (SPM) is grafted through atom transfer radical polymerization onto Sepharose FF (the thus resulting exchanger is referred as Sep-g-SPM), and another via the grafting-to approach, in which the polymer of SPM is directly coupled onto Sepharose FF (the thus resulting exchanger is called as Sep-pSPM). Protein adsorption on these two cation exchangers have been also investigated. At the same ligand density, Sep-g-SPM has a larger accessible pore radius and a smaller depth of polymer layer than Sep-pSPM, due to the controllable introduction of polymer chains with the regular distribution of the ligand. Therefore, high-capacity adsorption of lysozyme and γ-globulin could be achieved simultaneously in Sep-g-SPM with an ionic capacity (IC) of 308 mmol·L^-1. However, Sep-pSPM has an irregular chain distribution and different architecture of polymer layer, which lead to more serious repulsive interaction to proteins, and thus Sep-pSPM has a lower adsorption capacity for γ-globulin than Sep-g-SPM with the similar IC. Moreover, the results from protein uptake experiments indicate that the facilitated transport of adsorbed γ-globulin occurs only in Sep-pSPM and depends on the architecture of polymer layers. Our research provides a clear clue for the development of high-performance protein chromatography.

关键词： polymer-grafted ionic exchanger grafting technique protein adsorption atom transfer radical polymerization γ-globulin

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