Amplification of Salt-Induced Protein Diffusiophoresis by Varying Salt from Potassium to Sodium to Magnesium Chloride in Water.

Abstract

Salt-induced diffusiophoresis is the migration of a macromolecule or a colloidal particle induced by a concentration gradient of salt in water. Here, the effect of salt type on salt-induced diffusiophoresis of the protein lysozyme at pH 4.5 and 25 °C was examined as a function of salt concentration for three chloride salts: NaCl, KCl, and MgCl2. Diffusiophoresis coefficients were calculated from experimental ternary diffusion coefficients on lysozyme-salt-water mixtures. In all cases, diffusiophoresis of this positively charged protein occurs from high to low salt concentration. An appropriate mass transfer process was theoretically examined to show that concentration gradients of MgCl2 produce significant lysozyme diffusiophoresis. This is attributed to the relatively low mobility of Mg2+ ions compared to that of Cl- ions at low salt concentration and a strong thermodynamic nonideality of this salt at high salt concentration. These findings indicate that MgCl2 concentration gradients could be exploited for protein manipulation in solution (e.g., using microfluidic technologies) with applications to protein adsorption and purification. The dependence of lysozyme diffusiophoresis on salt type was theoretically examined and linked to protein charge. The effect of salts on hydrogen-ion titration curves was experimentally characterized to understand the role of salt type on protein charge. Our results indicate that binding of Mg2+ ions to lysozyme further enhances protein diffusiophoresis.