Salting out

Salting out (also known as antisolvent crystallization, precipitation crystallization, or drowning out) is an effect based on the electrolyte-nonelectrolyte interaction, in which the non-electrolyte could be less soluble at high salt concentrations. It is used as method of separating proteins. The salt concentration needed for the protein to precipitate out of the solution differs from protein to protein. This process is also used to concentrate solutions of proteins. Dialysis can be used to remove the salt if needed.

There are hydrophobic amino acids and hydrophilic amino acids in protein molecules. After protein folding in aqueous solution, hydrophobic amino acids usually form protected hydrophobic areas while hydrophilic amino acids interact with the molecules of solvation and allow proteins to form hydrogen bonds with the surrounding water molecules. If enough of the protein surface is hydrophilic, the protein can be dissolved in water.

When the salt concentration is increased, some of the water molecules are attracted by the salt ions, which decreases the number of water molecules available to interact with the charged part of the protein. As a result of the increased demand for solvent molecules, the protein–protein interactions are stronger than the solvent-solute interactions; the protein molecules coagulate by forming hydrophobic interactions with each other. This process is known as salting out.

Soaps are easily precipitated by concentrated salt solution, the metal ion in the salt reacts with the fatty acids forming back the soap and glycerol.

As different proteins have different compositions of amino acids, different protein molecules precipitate at different concentrations of salt solution.

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