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Being extremely soluble in water, ammonium sulfate can "salt out" (precipitate) proteins from aqueous solutions. [3] [4] Precipitation by ammonium sulfate is a result of a reduction in solubility rather than protein denaturation, thus the precipitated protein can be resolubilized through the use of standard buffers. [5]
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.
z i is the ion charge of the salt and c i is the salt concentration. The ideal salt for protein precipitation is most effective for a particular amino acid composition, inexpensive, non-buffering, and non-polluting. The most commonly used salt is ammonium sulfate. There is a low variation in salting out over temperatures 0 °C to 30 °C.
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.
Substance Formula 0 °C 10 °C 20 °C 30 °C 40 °C 50 °C 60 °C 70 °C 80 °C 90 °C 100 °C Barium acetate: Ba(C 2 H 3 O 2) 2: 58.8: 62: 72: 75: 78.5: 77: 75
All water-soluble salts and mixtures have characteristic critical humidities; it is a unique material property. The critical relative humidity of most salts decreases with increasing temperature. For instance, the critical relative humidity of ammonium nitrate decreases 22% with a temperature from 0 °C to 40 °C (32 °F to 104 °F).
Ammonium sulfate is the traditional kosmotropic salt for the salting out of protein from an aqueous solution. Kosmotropes are used to induce protein aggregation in pharmaceutical preparation and at various stages of protein extraction and purification.
Protein solubility is a complex function of physicochemical nature of the protein, pH, temperature, and the concentration of the salt used. It also depends on whether the salt is kosmotropic, whereby the salt will stabilize water. The solubility of proteins usually increases slightly in the presence of salt, referred to as "salting in".
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