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High‐capacity purification of hen egg‐white proteins by ion‐exchange electrochromatography with an oscillatory transverse electric field
Author(s) -
Yuan Wei,
Zhao GuoFeng,
Dong XiaoYan,
Sun Yan
Publication year - 2006
Publication title -
journal of separation science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.72
H-Index - 102
eISSN - 1615-9314
pISSN - 1615-9306
DOI - 10.1002/jssc.200600149
Subject(s) - chromatography , electric field , chemistry , dbc , electrochromatography , analytical chemistry (journal) , ovotransferrin , ion chromatography , ion exchange , yield (engineering) , ion , egg white , materials science , capillary electrochromatography , stationary phase , biochemistry , physics , optoelectronics , organic chemistry , cmos , quantum mechanics , metallurgy
The ion‐exchange electrochromatography with an oscillatory electric field perpendicular to the mobile‐phase flow driven by pressure (pIEEC) was used to separate hen egg‐white (HEW) proteins. The results were compared with those of normal ion‐exchange chromatography (IEC). The column was designed as three‐compartment rectangular column of 2‐mL with dimensions (length×width×depth) of 40×10×5 mm 3 and the electric field was applied across the direction of column width. Q Sepharose FF was packed into the central compartment as the chromatographic bed. It was confirmed that the dynamic binding capacity (DBC) of different proteins (ovotransferrin and ovalbumin) in the HEW solution increased 2.3 times when an oscillatory electric current of 30 mA at 1/20 Hz was applied in the transverse column direction. Then, the HEW proteins were separated by the pIEEC at loading amounts 2.3‐fold higher than those by the IEC. When the feedstock of about one‐third of the DBC was applied to the columns ( i. e. , 7 mL for the pIEEC and 3 mL for the IEC), similar separation efficiencies of the two chromatographic modes were achieved. Both the recovery yield and purity reached 73% to over 90%. The results indicate that the pIEEC is promising for high‐capacity purification of proteins.