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Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels

Bereli, Nilay; Andac, Muege; Baydemir, Goezde; Say, Ridvan; Galaev, Igor LU and Denizli, Adil (2008) In Journal of Chromatography A 1190(1-2). p.18-26
Abstract
Molecular imprinting is a method for making selective binding sites in synthetic polymers using a molecular template. The aim of this study is to prepare lysozyme-imprinted supermacroporous cryogels which can be used for the purification of lysozyme (Lyz) from egg white. N-Methacryloyl-(L)-histiclinemethylester (MAH) was chosen as the metal-coordinating monomer. In the first step, Cu2+ was complexed with MAH and the lysozyme-imprinted poly(HEMA-MAH) [Lyz-MIP] cryogel were produced by free radical polymerization initiated by N,N,N',N'-tetramethylene diamine (TEMED) in an ice bath. After that, the template (i.e., lysozyme) was removed using 0.05 M phosphate buffer containing 1 M NaCl (pH 8.0). The maximum lysozyme adsorption capacity was... (More)
Molecular imprinting is a method for making selective binding sites in synthetic polymers using a molecular template. The aim of this study is to prepare lysozyme-imprinted supermacroporous cryogels which can be used for the purification of lysozyme (Lyz) from egg white. N-Methacryloyl-(L)-histiclinemethylester (MAH) was chosen as the metal-coordinating monomer. In the first step, Cu2+ was complexed with MAH and the lysozyme-imprinted poly(HEMA-MAH) [Lyz-MIP] cryogel were produced by free radical polymerization initiated by N,N,N',N'-tetramethylene diamine (TEMED) in an ice bath. After that, the template (i.e., lysozyme) was removed using 0.05 M phosphate buffer containing 1 M NaCl (pH 8.0). The maximum lysozyme adsorption capacity was 22.9 mg/g polymer. The relative selectivity coefficients of Lyz-MIP cryogel for lysozyme/bovine serum albumin and lysozyme/cytochrome c were 4.6 and 3.2 times greater than non-imprinted poly(HEMA-MAH) (NIP) cryogel, respectively. Purification of lysozyme from egg white was also monitored by determining the lysozyme activity using Micrococcus lysodeikticus as substrate. The purity of the desorbed lysozyme was about 94% with recovery about 86%. The Lyz-MIP cryogel could be used many times without decreasing the adsorption capacity significantly. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
keywords
protein adsorption, affinity binding, purification, lysozyme, molecular recognition, cryogels, molecular imprinting
in
Journal of Chromatography A
volume
1190
issue
1-2
pages
18 - 26
publisher
Elsevier
external identifiers
  • wos:000255848600004
  • scopus:42049086545
ISSN
0021-9673
DOI
10.1016/j.chroma.2008.02.110
language
English
LU publication?
yes
id
25558efc-7723-448d-81ca-dc8a08c56948 (old id 1203672)
date added to LUP
2008-09-17 10:28:58
date last changed
2017-08-27 04:49:51
@article{25558efc-7723-448d-81ca-dc8a08c56948,
  abstract     = {Molecular imprinting is a method for making selective binding sites in synthetic polymers using a molecular template. The aim of this study is to prepare lysozyme-imprinted supermacroporous cryogels which can be used for the purification of lysozyme (Lyz) from egg white. N-Methacryloyl-(L)-histiclinemethylester (MAH) was chosen as the metal-coordinating monomer. In the first step, Cu2+ was complexed with MAH and the lysozyme-imprinted poly(HEMA-MAH) [Lyz-MIP] cryogel were produced by free radical polymerization initiated by N,N,N',N'-tetramethylene diamine (TEMED) in an ice bath. After that, the template (i.e., lysozyme) was removed using 0.05 M phosphate buffer containing 1 M NaCl (pH 8.0). The maximum lysozyme adsorption capacity was 22.9 mg/g polymer. The relative selectivity coefficients of Lyz-MIP cryogel for lysozyme/bovine serum albumin and lysozyme/cytochrome c were 4.6 and 3.2 times greater than non-imprinted poly(HEMA-MAH) (NIP) cryogel, respectively. Purification of lysozyme from egg white was also monitored by determining the lysozyme activity using Micrococcus lysodeikticus as substrate. The purity of the desorbed lysozyme was about 94% with recovery about 86%. The Lyz-MIP cryogel could be used many times without decreasing the adsorption capacity significantly.},
  author       = {Bereli, Nilay and Andac, Muege and Baydemir, Goezde and Say, Ridvan and Galaev, Igor and Denizli, Adil},
  issn         = {0021-9673},
  keyword      = {protein adsorption,affinity binding,purification,lysozyme,molecular recognition,cryogels,molecular imprinting},
  language     = {eng},
  number       = {1-2},
  pages        = {18--26},
  publisher    = {Elsevier},
  series       = {Journal of Chromatography A},
  title        = {Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels},
  url          = {http://dx.doi.org/10.1016/j.chroma.2008.02.110},
  volume       = {1190},
  year         = {2008},
}