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Anion exchange membrane adsorbers for flow-through polishing steps: Part II. Virus, host cell protein, DNA clearance, and antibody recovery

Authors

  • Justin Weaver,

    1. Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, Colorado 80523
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  • Scott M. Husson,

    1. Department of Chemical and Biomolecular Engineering, Clemson University, Clemson, South Carolina
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  • Louise Murphy,

    1. Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, Colorado 80523
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  • S. Ranil Wickramasinghe

    Corresponding author
    1. Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, Colorado 80523
    2. Ralph E. Martin Department of Chemical Engineering, University of Arkansas, Fayetteville, Arkansas 72701; telephone: +1 479 575 8475; fax: +1 479 575 4937
    • Department of Chemical and Biological Engineering, Colorado State University, Fort Collins, Colorado 80523.
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Abstract

Anion exchange membrane adsorbers are used for contaminant removal in flow-through polishing steps in the manufacture of biopharmaceuticals. This contribution describes the clearance of minute virus of mice, DNA, and host cell proteins by three commercially available anion-exchange membranes: Sartobind Q, Mustang Q, and ChromaSorb. The Sartobind Q and Mustang Q products contain quaternary amine ligands; whereas, ChromaSorb contains primary amine based ligands. Performance was evaluated over a range of solution conditions: 0–200 mM NaCl, pH 6.0–9.0, and flow rates of 4–20 membrane volumes/min in the presence and absence of up to 50 mM phosphate and acetate. In addition contaminant clearance was determined in the presence and absence of 5 g/L monoclonal antibody. The quaternary amine based ligands depend mainly on Coulombic interactions for removal of negatively charged contaminants. Consequently, performance of Sartobind Q and Mustang Q was compromised at high ionic strength. Primary amine based ligands in ChromaSorb enable high capacities at high ionic strength due to the presence of secondary, hydrogen bonding interactions. However, the presence of hydrogen phosphate ions leads to reduced capacity. Monoclonal antibody recovery using primary amine based anion-exchange ligands may be lower if significant binding occurs due to secondary interactions. The removal of a specific contaminant is affected by the level of removal of the other contaminants. The results of this study may be used to help guide selection of commercially available membrane absorbers for flow-through polishing steps. Biotechnol. Bioeng. 2013; 110: 500–510. © 2012 Wiley Periodicals, Inc.

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