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Ammonium sulfate is an inorganic salt with a high solubility that disassociates into ammonium (NH + 4) and sulfate (SO 2− 4) in aqueous solutions. [1] Ammonium sulfate is especially useful as a precipitant because it is highly soluble, stabilizes protein structure, has a relatively low density, is readily available, and is relatively inexpensive.
Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) [1] is a purification technique that utilizes the reduced solubility of certain molecules in a solution of very high ionic strength.
Ammonium sulfate precipitation is a common method for protein purification by precipitation. As the ionic strength of a solution increases, the solubility of proteins in that solution decreases. Being extremely soluble in water, ammonium sulfate can "salt out" (precipitate) proteins from aqueous solutions.
The "salting out" effect is commonly exploited in protein purification through the use of ammonium sulfate precipitation. [16] However, these salts also interact directly with proteins (which are charged and have strong dipole moments) and may even bind specifically (e.g., phosphate and sulfate binding to ribonuclease A).
Salting out is the most common method used to precipitate a protein. Addition of a neutral salt, such as ammonium sulfate, compresses the solvation layer and increases protein–protein interactions. As the salt concentration of a solution is increased, the charges on the surface of the protein interact with the salt, not the water, thereby ...
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It also aids in separation of proteins using purification techniques such as salting out, e.g. ammonium sulfate precipitation. [6] Centrifugation is also an important technique in waste treatment, being one of the most common processes used for sludge dewatering. [21]
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