This paper discusses the unique patterns evolved through phase separation of a bulk liquid crystal (LC) from the self-assembly of lysozyme induced by evaporation of de-ionized water only. Each domain shows a central dark region surrounded by bright regions (randomly oriented LC droplets). The birefringence intensity reveals three regimes (a slow increase, rapid rise, then saturation) not seen without LC droplets. The textural study exhibits a simple exponential behavior that changes as a function of LC concentration. Furthermore, in the presence of LC, the crack patterns are found to be different near the drop edge than those in the central region.

The drying process, self-assembly of the proteins and the phase separation of a thermotropic liquid crystal (LC) from an initial aqueous solution represent a rich area of study. A focus of this work is to compare the behavior of two different proteins, bovine serum albumin [BSA] and lysozyme [Lys] in the ternary system through optical microscopy. During the drying process, the intensity profile shows three regimes in the presence of LC whereas no intensity variation is observed in its absence in both protein drops. The striking outcome is the presence of an umbilical defect of [+1] strength in every domain near the edge of BSA drop, whereas, each domain has a central dark region surrounded by a bright region in the dried Lys drop. Finally, the crack spacing in the dried Lys drop is reduced in the presence of LC whereas, no significant difference is found in the dried BSA drop.