Title of article :
Protein recognition via ion-coordinated molecularly imprinted supermacroporous cryogels
Author/Authors :
Bereli، نويسنده , , Nilay and Andaç، نويسنده , , Müge and Baydemir، نويسنده , , Gِzde and Say، نويسنده , , Ridvan and Galaev، نويسنده , , Igor Yu and Denizli، نويسنده , , Adil، نويسنده ,
Issue Information :
روزنامه با شماره پیاپی سال 2008
Pages :
9
From page :
18
To page :
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)-histidinemethylester (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.
Keywords :
Cryogels , molecular imprinting , Molecular recognition , Lysozyme purification , protein adsorption , Affinity binding
Journal title :
Journal of Chromatography A
Serial Year :
2008
Journal title :
Journal of Chromatography A
Record number :
1510753
Link To Document :
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