Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1203672
- author
- Bereli, Nilay ; Andac, Muege ; Baydemir, Goezde ; Say, Ridvan ; Galaev, Igor LU and Denizli, Adil
- organization
- publishing date
- 2008
- 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
- pmid:18395214
- 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
- 2016-04-01 14:11:33
- date last changed
- 2022-04-14 08:25:49
@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}},
keywords = {{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}},
doi = {{10.1016/j.chroma.2008.02.110}},
volume = {{1190}},
year = {{2008}},
}