Thursday, May 4, 2017

Salting out and Salting In






Salting Out and Salting In


Salting out is a purification method that uses reduced solubility of certain molecules in a solution with a very high ionic strength. Salting out occurs in aqueous solutions that have a very high ionic strength. Salting out is typically used for the precipitation of large biomolecules such as proteins. The large biomolecules are typically controlled with hydrophobic and hydrophilic interactions with the cell's environment. In the aqueous solution that has a very strong ionic strength, the water molecules surround the charges of the ions and proteins. When the aqueous solution reaches a certain strength, the water molecules are no longer able to support the charges of both the ions and proteins. This results in the precipitation of the least soluble solute.Salting out occurs in an aqueous solution of high ionic strength that reduces the solubility while salting in increases the solubility by adding more salt. “The solubility of a protein at low ion concentrations increases as salt is added”, basically increasing its solubility, is known as salting in. In Salting in when salt is added the protein’s solubility at a low ion concentration increases. Also when the salt is added, it adds additional ion shields to the proteins multiple ionic charges. This causes the attractive forces to weaken between other proteins. An example of salting out purpose is to separate the glycerin from the soap. The contents of the kettle salt out into an upper layer that is a mass of impure soap and underneath that is the aqueous salt solution with the dissolved glycerin.

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