Bovine lactoferrin (LF) and �-lactoglobulin (BLG) are among the protein pairs that exhibit heteroprotein coacervation, a unique and relatively unexamined type of liquid-liquid phase separation (LLPS).   In contrast to coacervation involving polyelectrolytes here, coacervates only form at I < 20 mM. The range of pH at which coacervation occurs is similarly narrow, ca. 5.7-6.2. However, suppression of coacervation is observed at high CP, which is similar to the behavior of some polyelectrolyte-colloid systems. At a 1:1 weight ratio, the coacervate composition  is consistent with an average structure of LF(BLG2)2.The precise balance of repulsive and attractive forces among these units, thought to stabilize the coacervate, is achieved only at limited conditions of pH and salt. Recent work suggests that the charge anisotropy of the two proteins stabilize the primary unit of the coacervate, while interactions among these complexes govern the viscoelastic properties of the coacervate.

Heteroprotein coacervation

248th National Meeting (2014)

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