Characterization of a Lyophilized Immunoaffinity Chromatography Matrix Employed to Purify Hepatitis B Surface Antigen for Pharmaceutical Use

by Miguel Castillo et al.
Volume 13, Issue 4 (Winter 2014/2015)

Immunoaffinity chromatography is an indispensable purification tool. However, its use has been limited by cost, purification cycle numbers, and storage requirements. Therefore, authors speculated that a possible solution to these problems could be CB.Hep-1 monoclonal antibody (mAb)-immunosorbent lyophilization. This study sought to assess the impact of the CB.Hep-1 mAb quantification by enzyme-linked immunoadsorbent assay and the CB.Hep-1 mAb-immunosorbent lyophilization process for its impact on hepatitis B virus surface antigen purification for pharmaceutical use. Study results found that CB.Hep-1 mAb lyophilization did not affect mAb purity and antigen recognition capacity. CB.Hep-1 mAb-immunosorbent lyophilization did not modify volume-weight factor, infrared spectrum, particle-size distribution, particle density and viscosity, antigen adsorption capacity, antigen elution capacity, antigen recovery, antigen purity, gamma immunoglobulin (IgG) leakage, and purification cycle number. Therefore, the lyophilized CB.Hep-1 mAb and CB.Hep-1 mAb-immunosorbents can be successfully used for hepatitis B vaccine production...

Castillo M et al. Characterization of a lyophilized immunoaffinity chromatography matrix employed to purify hepatitis B surface antigen for pharmaceutical use. BioProcess J, 2015; 13(4): 35–45.

Posted online January 20, 2015.