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Two step capture and purification of IgG 2 using multicolumn countercurrent solvent gradient purification (MCSGP)
Author(s) -
MüllerSpäth T.,
Aumann L.,
Ströhlein G.,
Kornmann H.,
Valax P.,
Delegrange L.,
Charbaut E.,
Baer G.,
Lamproye A.,
Jöhnck M.,
Schulte M.,
Morbidelli M.
Publication year - 2010
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.22887
Subject(s) - chromatography , chemistry , yield (engineering) , elution , countercurrent exchange , solvent , ion exchange , process (computing) , batch processing , ion chromatography , ion , materials science , organic chemistry , thermodynamics , physics , computer science , metallurgy , programming language , operating system
A two‐step chromatography process for monoclonal antibody (mAb) purification from clarified cell culture supernatant (cCCS) was developed using cation exchange Multicolumn Countercurrent Solvent Gradient Purification (MCSGP) as a capture step. After an initial characterization of the cell culture supernatant the capture step was designed from a batch gradient elution chromatogram. A variety of chromatographic materials was screened for polishing of the MCSGP‐captured material in batch mode. Using multi‐modal anion exchange in bind‐elute mode, mAb was produced consistently within the purity specification. The benchmark was a state‐of‐the‐art 3‐step chromatographic process based on protein A, anion and cation exchange stationary phases. The performance of the developed 2‐step process was compared to this process in terms of purity, yield, productivity and buffer consumption. Finally, the potential of the MCSGP process was investigated by comparing its performance to that of a classical batch process that used the same stationary phase. Biotechnol. Bioeng. 2010;107: 974–984. © 2010 Wiley Periodicals, Inc.