Novel Affinity Disks for Bovine Serum Albumin Purification

The adsorption characteristics of bovine serum albumin (BSA) onto the supermacroporous poly(hydroxyethylmethacrylate)-Reactive Green 19 [p(HEMA)-RG] cryogel disks have been investigated in this paper. p(HEMA) cryogel disks were prepared by radical polymerization initiated by N,N,N′,N′-tetramethylene...

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Vydané v:Applied biochemistry and biotechnology Ročník 175; číslo 1; s. 454 - 468
Hlavní autori: Tuzmen, Nalan, Kalburcu, Tülden, Uygun, Deniz Aktaş, Akgol, Sinan, Denizli, Adil
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: Boston Springer-Verlag 01.01.2015
Springer US
Springer Nature B.V
Predmet:
Adsorption
Ammonium
Animals
Biochemistry
Biotechnology
Blood
bovine serum albumin
Cattle
Chemistry
Chemistry and Materials Science
Cryogels - chemistry
Electrophoresis, Polyacrylamide Gel
enthalpy
Hydrogels
ice
ionic strength
polyacrylamide gel electrophoresis
Polymerization
Proteins
purification methods
Serum Albumin, Bovine - chemistry
Serum Albumin, Bovine - isolation & purification
Sodium chloride
sodium dodecyl sulfate
sorption isotherms
temperature
Bovine serum albumin
Affinity adsorption
Cryogels
Dye ligand
Blood
ISSN:0273-2289, 1559-0291, 1559-0291
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Shrnutí:The adsorption characteristics of bovine serum albumin (BSA) onto the supermacroporous poly(hydroxyethylmethacrylate)-Reactive Green 19 [p(HEMA)-RG] cryogel disks have been investigated in this paper. p(HEMA) cryogel disks were prepared by radical polymerization initiated by N,N,N′,N′-tetramethylene diamine (TEMED) and ammonium persulfate (APS) pair in an ice bath. Reactive Green (RG) 19 was covalently attached to the p(HEMA) cryogel disks. These disks were used in BSA adsorption studies to interrogate the effects of pH, initial protein concentration, ionic strength, and temperature. BSA adsorption capacity of the p(HEMA)-RG cryogel disk was significantly improved after the incorporation of RG. Adsorption capacity reached a plateau value at about 0.8 mg/mL at pH 4.0. The amount of adsorbed BSA decreased from 37.7 to 13.9 mg/g with increasing NaCl concentration. The enthalpy of BSA adsorption onto the p(HEMA)-RG cryogel disk was calculated as −58.4 kJ/mol. The adsorption equilibrium isotherm was fitted well by the Freundlich model. BSA was desorbed from cryogel disks (over 90 %) using 0.5 M NaSCN, and the purity of desorbed BSA was confirmed by sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). The experimental results showed that the p(HEMA)-RG cryogel disks have potential for the quick protein separation and purification process.
Bibliografia:http://dx.doi.org/10.1007/s12010-014-1273-8
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ISSN:0273-2289
1559-0291
1559-0291
DOI:10.1007/s12010-014-1273-8