How can I improve protein stability during ion exchange?

One way to improve protein stability during ion exchange is by adding charged amino acids L-arginine and L-glutamate at a concentration of 50 mM to the buffer solution. This increases the maximum soluble protein concentrations by up to 8.7 times. These amino acids effectively prevent protein aggregation while significantly improving the sample’s long term stability. Another way is by optimizing the pH of the buffer solution to ensure it is within the protein’s solubility range. The salt concentration should also be set appropriately. Additionally, the eluent should be adjusted to retain stability. Another way is to use an ion exchange resin with high capacity. This increases binding capacity and minimizes protein interactions leading to precipitation.