Hydrophobic interaction chromatography (HIC) is widely used for large scale separation of proteins based on differences in surface hydrophobicity. A new HIC resin produced by GE Healthcare's custom designed media group on the rigid CaptoTM backbone was evaluated as a replacement for a SepharoseTM HIC resin. This change was investigated as a means of increasing downstream productivity for a recombinant Fc-fusion protein. Several Capto HIC resins with varying hydrophobicities were evaluated and the optimal resin was shown to reduce aggregates and host cell proteins to comparable levels as the SepharoseTM media. The new resin allowed for an increase in capacity and operating flow rate. To characterize the Capto HIC media, linear retention and capacity studies were completed with model proteins and the Fc-fusion protein of interest. Resin morphology and mass transport properties were studied by inverse size exclusion chromatography (ISEC) and unretained HETP studies. The preparative and characterization results will be discussed.

Characterization of a new HIC media

239th National Meeting (2010)

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