[Importance of the chemical composition and chromatographic resins since the scaling up of a procedure for the purification of proteins]

Abstract

Despite having the same ionic character, ion exchangers for protein separation are not identical to each other hence differences in results are generally anticipated when scaling up operations from laboratory to production. This is illustrated by comparative studies presented in this article which shows the separation of an IgG-rich fraction from sweet whey using Q-resins. One resin, available in three different particle sizes for scale changes to avoid high back pressure when increasing the size of the column, was compared with a resin that does not have the corresponding larger size particles so that scale changes have to be performed using another chemically different sorbent. Investigation of dynamic binding capacity, resolution versus loading and scale changes, demonstrated the importance of maintaining consistency in the chemical composition for an ion exchanger to eliminate differences in separation properties and therefore reduce the process development time required for specific optimization of separation conditions and maximizing productivity.