Ever increasing performance demands in protein purification require more selective chromatography methods to effectively remove aggregates and other impurities. At high titer levels, aggregates often present a unique purification challenge. One emerging approach to address this challenge is the use of new, smaller-particle chromatography resins that are optimized for high resolution and capacity. Such resins can be particularly productive in challenging situations and during final polishing steps (He at al. 2010). Nuvia HR-S is the latest member of this new class of high-resolution resins; it features a hydrophilic polymer matrix with an open-pore structure designed for fast and efficient mass transfer and superior flow properties at high flow rates. Here, we compare the performance of Nuvia HR-S to that of a high-resolution agarose-based resin. We also describe the relationship between elution buffer conductivity, monomer recovery, and aggregate content.
Improving Aggregate Removal from a Monoclonal Antibody Feedstream Using High-Resolution Cation Exchange Chromatography
Nuvia™ HR-S Resin, a hydrophilic open-pore, high-resolution cation exchange (CEX) resin (media), was shown to reduce aggregate content to <0.3% with >80% monomer recovery from a monoclonal antibody feedstream containing 8.9% aggregates. In a side-by-side comparison with a high-resolution agarose-based resin, Nuvia HR-S showed comparable aggregate removal but at significantly higher recovery levels. Furthermore, aggregate content and overall recovery were shown to be functions of the conductivity of the elution buffer at the end of collection.