I am extracting protéines by isoelectrique precipitation at pH 4. I don't know if I have to resolubilise the proteins at pH7 before freez-drying or I can freez-dry them directly after precipiattion ( at pH4).
Generally, after the protein obtained by isoelectric precipitation, redissolution, neutralization of the redissolved protein solution to pH7, and dialysis before lyophilization are necessary.
Yes, it would be crucial to dissolve the obtained protein in buffer to neutralise the pH and partially purify and then freeze dry it. Specially if you want to characterise its functionality at different concentrations.
Dear Yakoub, If you don't dissolve your proteins and neutralise the pH, it will be very hard to dissolve them again even at pH>>IP. Also, as Mr Mirzapour mentioned, the functionality would be different as you will deal with aggregates of proteins instead of protein crystals (when in powder form). Removing the excess salts by dialysis would be good as well.