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Synthesis and use of protein G imprinted cryogel as affinity matrix to purify protein G from cell lyaste.

Asliyuce Coban, Sevgi LU ; Mattiasson, Bo LU and Mamo, Gashaw LU (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.
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author
; and
organization
publishing date
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}},
}