Premium
Customization of copolymers to optimize selectivity and yield in polymer‐driven antibody purification processes
Author(s) -
Capito Florian,
Skudas Romas,
Stanislawski Bernd,
Kolmar Harald
Publication year - 2013
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1002/btpr.1813
Subject(s) - copolymer , precipitation , polymer , selectivity , ionic strength , yield (engineering) , chemistry , chemical engineering , chromatography , coprecipitation , materials science , organic chemistry , aqueous solution , catalysis , physics , meteorology , engineering , metallurgy
This manuscript describes customization of copolymers to be used for polymer‐driven protein purification in bioprocessing. To understand how copolymer customization can be used for fine‐tuning, precipitation behavior was analyzed for five target antibodies (mAbs) and BSA as model impurity protein, at ionic strength similar to undiluted cell culture fluid. In contrast to the use of standardized homopolymers, customized copolymers, composed of 2‐acrylamido‐2‐methylpropane sulfonic acid (AMPS) and 4‐(acryloylamino)benzoic acid (ABZ), exhibited antibody precipitation yields exceeding 90%. Additionally, copolymer average molecular weight ( M w ) was varied and its influence on precipitation yield and contaminant coprecipitation was investigated. Results revealed copolymer composition as the major driving force for precipitation selectivity, which was also dependent on protein hydrophobicity. By adjusting ABZ content and M w of the precipitant for each of the mAbs, conditions were found that allowed for high precipitation yield and selectivity. These findings may open up new avenues for using polymers in antibody purification processes. © 2013 American Institute of Chemical Engineers Biotechnol. Prog ., 29:1484–1493, 2013