Chromatographic adsorption of serum albumin and antibody proteins in cryogels with benzyl-quaternary amine ligands.

Junxian Yun, Xiuhong Cheng, Jialei Ye, Shaochuan Shen, Gensheng Yang, Kejian Yao, Harald Kirsebom, Dong-Qiang Lin, Yi-Xin Guan, Shan-Jing Yao

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The preparation and characterization of mixed-mode adsorbents for a typical separation purpose are of great importance in bioseparation areas. In this work, we prepared a new monolithic cryogel with a combination of ion-exchange and hydrophobic functions by employing benzyl-quaternary amine groups. The fundamental cryogel properties, protein equilibrium adsorption isotherm and chromatographic adsorption in the cryogel were measured experimentally. The results showed that, by using bovine serum album as the model protein, the dual functional cryogel has protein binding capability even in salt solution and the buffer with pH close or below the protein isoelectric point due to both the electrostatic and hydrophobic interactions. A capillary-based adsorption model was developed, which provided satisfied insights of the microstructure, axial dispersion, mass transfer as well as protein adsorption characteristics within the cryogel bed. The chromatographic isolation of bioactive proteins from rabbit blood serum was carried out by the cryogel. Immunoglobulin G antibody with a purity of 98.2% and albumin with a purity of 96.8% were obtained, indicating that the cryogel could be an interesting and promising adsorbent in bioseparation areas.
    Original languageEnglish
    Pages (from-to)173-183
    JournalJournal of Chromatography A
    Volume1381
    DOIs
    Publication statusPublished - 2015

    Subject classification (UKÄ)

    • Industrial Biotechnology

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