Protein Purification by Complex Coacervation

Proteins are an important class of biomolecules with applications across many industries, including as therapeutics and biocatalysts. Their use in some industries, such as the food and pharmaceutical industries, require a high degree of protein purity for their products. Therefore, a highly selective, yet high throughput and low-cost purification method is of great interest to purify proteins from cell lysate. Complex coacervation, the liquid-liquid phase separation of oppositely charged polyelectrolytes, shows promise as a protein purification technique. Previous work in the field, however, has only addressed separating a protein of interest from a relatively simple mixture. In this work, we demonstrate the utility of complex coacervation as a platform to purify proteins from cell lysate. Using a spectroscopic method, we designed a high throughput approach to screen protein purity and recovery from cell lysate. We were then able to assess how protein and polymer design properties and solution conditions impact protein purity and recovery from cell lysate.