Chromatographic adsorption of serum albumin and antibody proteins in cryogels with benzyl-quaternary amine ligands.
(2015) In Journal of Chromatography A 1381. p.173-183- 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... (More)
- 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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/5039778
- author
- Yun, Junxian ; Cheng, Xiuhong ; Ye, Jialei ; Shen, Shaochuan ; Yang, Gensheng ; Yao, Kejian ; Kirsebom, Harald LU ; Lin, Dong-Qiang ; Guan, Yi-Xin and Yao, Shan-Jing
- organization
- publishing date
- 2015
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chromatography A
- volume
- 1381
- pages
- 173 - 183
- publisher
- Elsevier
- external identifiers
-
- pmid:25618356
- wos:000349590600019
- scopus:84922791871
- pmid:25618356
- ISSN
- 0021-9673
- DOI
- 10.1016/j.chroma.2014.11.081
- language
- English
- LU publication?
- yes
- id
- c757a03a-39fd-4bb9-9aa2-055abb968e77 (old id 5039778)
- date added to LUP
- 2016-04-01 10:22:52
- date last changed
- 2022-04-27 21:29:33
@article{c757a03a-39fd-4bb9-9aa2-055abb968e77,
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.}},
author = {{Yun, Junxian and Cheng, Xiuhong and Ye, Jialei and Shen, Shaochuan and Yang, Gensheng and Yao, Kejian and Kirsebom, Harald and Lin, Dong-Qiang and Guan, Yi-Xin and Yao, Shan-Jing}},
issn = {{0021-9673}},
language = {{eng}},
pages = {{173--183}},
publisher = {{Elsevier}},
series = {{Journal of Chromatography A}},
title = {{Chromatographic adsorption of serum albumin and antibody proteins in cryogels with benzyl-quaternary amine ligands.}},
url = {{http://dx.doi.org/10.1016/j.chroma.2014.11.081}},
doi = {{10.1016/j.chroma.2014.11.081}},
volume = {{1381}},
year = {{2015}},
}