Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste.
(2016) In Journal of Chromatography. B 1021. p.204-212- Abstract
- Monolithic macroporous cryogel imprinted with protein G was prepared using a functional co-monomer of N-methacryloyl-l-phenylalanine and 2-hydroxyethyl methacrylate. The chemical structure of the cryogel prepared was studied by FTIR-spectroscopy and its porosity was analysed using scanning electron microscopy. The cryogel was used to purify protein G from recombinant Escherichia coli cell lysate and the effect of pH, temperature, ionic strength, flow rate, etc on the adsorption of protein G to the monolithic column have been investigated. The selectivity of the imprinted cryogel was studied using protein A and myoglobin. It was possible to capture about 9mg of Protein G per g of the cryogel.
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/8576677
- author
- Asliyuce Coban, Sevgi LU ; Mattiasson, Bo LU and Mamo, Gashaw LU
- organization
- publishing date
- 2016-01-04
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chromatography. B
- volume
- 1021
- pages
- 204 - 212
- publisher
- Elsevier
- external identifiers
-
- pmid:26794291
- scopus:84961327651
- pmid:26794291
- wos:000376545600024
- ISSN
- 1873-376X
- DOI
- 10.1016/j.jchromb.2015.12.060
- language
- English
- LU publication?
- yes
- id
- feeaeb3c-e780-42ab-9885-f809427c4429 (old id 8576677)
- date added to LUP
- 2016-04-01 10:35:00
- date last changed
- 2022-04-04 19:31:49
@article{feeaeb3c-e780-42ab-9885-f809427c4429, abstract = {{Monolithic macroporous cryogel imprinted with protein G was prepared using a functional co-monomer of N-methacryloyl-l-phenylalanine and 2-hydroxyethyl methacrylate. The chemical structure of the cryogel prepared was studied by FTIR-spectroscopy and its porosity was analysed using scanning electron microscopy. The cryogel was used to purify protein G from recombinant Escherichia coli cell lysate and the effect of pH, temperature, ionic strength, flow rate, etc on the adsorption of protein G to the monolithic column have been investigated. The selectivity of the imprinted cryogel was studied using protein A and myoglobin. It was possible to capture about 9mg of Protein G per g of the cryogel.}}, author = {{Asliyuce Coban, Sevgi and Mattiasson, Bo and Mamo, Gashaw}}, issn = {{1873-376X}}, language = {{eng}}, month = {{01}}, pages = {{204--212}}, publisher = {{Elsevier}}, series = {{Journal of Chromatography. B}}, title = {{Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste.}}, url = {{http://dx.doi.org/10.1016/j.jchromb.2015.12.060}}, doi = {{10.1016/j.jchromb.2015.12.060}}, volume = {{1021}}, year = {{2016}}, }