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Capillary electrochromatographic separation of proteins on a column coated with titanium dioxide nanoparticles
Author(s) -
Hsieh YiLing,
Chen TseHsien,
Liu ChuenYing
Publication year - 2006
Publication title -
electrophoresis
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.666
H-Index - 158
eISSN - 1522-2683
pISSN - 0173-0835
DOI - 10.1002/elps.200500897
Subject(s) - ovalbumin , chromatography , chemistry , analyte , egg white , adsorption , buffer (optical fiber) , nanoparticle , phosphate , silicon dioxide , capillary action , ligand (biochemistry) , phosphate buffered saline , chemical engineering , materials science , antigen , biochemistry , nanotechnology , organic chemistry , telecommunications , genetics , receptor , computer science , engineering , composite material , biology
A TiO 2 nanoparticle (TiO 2 NP)‐coated open‐tubular column for the capillary electrochromatographic separation of proteins is described. The surface chemistry of the TiO 2 NPs on the inner wall of the fused silica was significantly affected by the running buffer. By varying of the phosphate buffer pH, only cathodic EOF was indicated. The results showed that TiO 2 NPs are existed as a complexed form with the buffer ligand. Good separation of conalbumin (ConA), apo‐transferrin (apoTf), ovalbumin (OVA), and BSA could be achieved with phosphate buffer (40 mM, pH 8.0) and an applied voltage of 15 kV. Five peaks of glycoisoforms of OVA were observed under these conditions. In comparison with the retention behavior of the analytes on the bare fused‐silica column, the new column's high resolving power seems to be predominantly derived from the ligand exchange of the analytes with the phosphate adsorbed onto the TiO 2 NPs. The method was also used to separate egg‐white proteins. Both acidic and basic proteins in egg white were separated in a single run. The microheterogeneities of OVA could also be found in it. The separation efficiency for the main peak of OVA in egg white was around 10 000 plates/m.