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Salting in refers to the effect where increasing the
ionic strength The ionic strength of a solution is a measure of the concentration of ions in that solution. Ionic compounds, when dissolved in water, dissociate into ions. The total electrolyte concentration in solution will affect important properties such a ...
of a solution increases the
solubility In chemistry, solubility is the ability of a substance, the solute, to form a solution with another substance, the solvent. Insolubility is the opposite property, the inability of the solute to form such a solution. The extent of the solubi ...
of a solute, such as a protein. This effect tends to be observed at lower
ionic strength The ionic strength of a solution is a measure of the concentration of ions in that solution. Ionic compounds, when dissolved in water, dissociate into ions. The total electrolyte concentration in solution will affect important properties such a ...
s. Protein solubility is a complex function of
physicochemical Physical chemistry is the study of macroscopic and microscopic phenomena in chemical systems in terms of the principles, practices, and concepts of physics such as motion, energy, force, time, thermodynamics, quantum chemistry, statistical mecha ...
nature of the protein, pH, temperature, and the concentration of the salt used. It also depends on whether the salt is
kosmotropic Co-solvents (in water solvent) are defined as kosmotropic (order-making) if they contribute to the stability and structure of water-water interactions. In contrast, chaotropic (disorder-making) agents have the opposite effect, disrupting water str ...
, whereby the salt will stabilize water. The solubility of proteins usually increases slightly in the presence of salt, referred to as "salting in". However, at high concentrations of salt, the solubility of the proteins drop sharply and proteins can precipitate out, referred to as "salting out".


Anionic interactions

Initial salting in at low concentrations is explained by the Debye–Huckel theory. Proteins are surrounded by the salt
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s (ions of opposite net charge) and this screening results in decreasing electrostatic free energy of the protein and increasing activity of the solvent, which in turn leads to increasing solubility. This theory predicts that the logarithm of solubility is proportional to the square root of the ionic strength. The behavior of proteins in solutions at high salt concentrations is explained by
John Gamble Kirkwood John "Jack" Gamble Kirkwood (May 30, 1907, Gotebo, Oklahoma – August 9, 1959, New Haven, Connecticut) was a noted chemist and physicist, holding faculty positions at Cornell University, the University of Chicago, California Institute of Technol ...
. The abundance of the salt ions decreases the solvating power of salt ions, resulting in the decrease in the solubility of the proteins and precipitation results. At high salt concentrations, the solubility is given by the following empirical expression. :log S = B − KI where S is the solubility of the protein, B is a constant (function of protein, pH and temperature), K is the salting out constant (function of pH, mixing and salt), and I is the ionic strength of the salt. This expression is an approximation to that proposed by Long and McDevit.


See also

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Salting out Salting out (also known as salt-induced precipitation, salt fractionation, anti-solvent crystallization, precipitation crystallization, or drowning out) is a purification technique that utilizes the reduced solubility of certain molecules in a s ...
*
Solvation shell A solvation shell or solvation sheath is the solvent interface of any chemical compound or biomolecule that constitutes the solute. When the solvent is water it is called a hydration shell or hydration sphere. The number of solvent molecules sur ...


References


Further reading

* * Separation processes {{chem-stub