A closer look at arrested spinodal decomposition in protein solutions.

Concentrated aqueous solutions of the protein lysozyme undergo a liquid-solid transition upon a temperature quench into the unstable spinodal region below a characteristic arrest temperature of T(f) = 15 °C. We use video microscopy and ultra-small angle light scattering in order to investigate the arrested structures as a function of initial concentration, quench temperature and rate of the temperature quench. We find that the solid-like samples show all the features of a bicontinuous network that is formed through an arrested spinodal decomposition process. We determine the correlation length ξ and demonstrate that ξ exhibits a temperature dependence that closely follows the critical scaling expected for density fluctuations during the early stages of spinodal decomposition. These findings are in agreement with an arrest scenario based on a state diagram where the arrest or gel line extends far into the unstable region below the spinodal line. Arrest then occurs when during the early stage of spinodal decomposition the volume fraction φ(2) of the dense phase intersects the dynamical arrest threshold φ(2,Glass), upon which phase separation gets pinned into a space-spanning gel network with a characteristic length ξ.