Journal of Chemistry and Chemical Engineering

Abstract

We have previously shown that the diphtheria toxin variant CRM197 (cross-reacting material 197) can be overexpressed
\nin Escherichia coli at high levels, yielding insoluble aggregates, which were solubilized using urea. This study reports a comparison
\nof three matrices suitable for the purification and refolding of recombinant CRM197 by metal-chelating affinity chromatography.
\nMoreover, we show that refolded CRM197 features enzymatic activity.

Identifiers

DOI

10.17265/1934-7375

Citations and references