8.11.3 Salting-out of macromolecule 3.1 Salting in and salting out salting out( Can be used for Fractionation) Addition of salt at low ionic strength If the concentration of neutral salts is at a can increase solubility of a protein by high level(>0. 1 mol dm- ), in many instances neutralizing charges on the surface of the the protein precipitates. This phenomenon protein, reducing the ordered water around results because the excess ions(not bound to the protein and increasing entropy of the the protein) compete with proteins for the system solvent. The decrease in solvation and netralization of the repulsive forces allows the proteins to aggregate and precipitate Nacl
Addition of salt at low ionic strength can increase solubility of a protein by neutralizing charges on the surface of the protein, reducing the ordered water around the protein and increasing entropy of the system. 8.11.3 Salting-out of macromolecule 3.1 Salting in and salting out Salting out (Can be used for Fractionation) If the concentration of neutral salts is at a high level (> 0.1 mol dm-3 ), in many instances the protein precipitates. This phenomenon results because the excess ions (not bound to the protein) compete with proteins for the solvent. The decrease in solvation and neturalization of the repulsive forces allows the proteins to aggregate and precipitate
8. 11.3 Salting-out of macromolecule 3.1 Salting in and salting out Adjusting ph of the solution to isoelectric point can weaken the repulsion between color idal particles, helping for pH> I.E.P. pH <I.E.P. coagulation of colloidal particles L.E. P Solubility of a globulin-type protein close to its isoelectric point(IEP
Adjusting pH of the solution to isoelectric point can weaken the repulsion between colloidal particles, helping for coagulation of colloidal particles. 8.11.3 Salting-out of macromolecule 3.1 Salting in and salting out