Structure and dynamics of hagfish mucin in different saline environments.

The defense mechanism of hagfish against predators is based on its ability to form slime within a few milliseconds. Hagfish slime consists of two main components, namely mucin-like glycoproteins and long protein threads, which together entrap vast amounts of water and thus form a highly dilute hydrogel. Here, we investigate the mucin part of this hydrogel, in particular the role of the saline marine environment on the viscoelasticity and structure. By means of dynamic light scattering (DLS), shear and extensional rheology we probe the diffusion dynamics, the flow behavior, and the longest filament breaking time of hagfish mucin solutions. Using DLS we find a concentration-independent diffusion coefficient - characteristic for polyelectrolytes - up to the entanglement regime of 0.2 mg ml-1, which is about ten times higher than the natural concentration of hagfish mucin in hagfish slime. We also observe a slow relaxation process associated with clustering, probably due to electrostatic interactions. Shear rheology further revealed that hagfish mucin possesses pronounced viscoelastic properties at high concentrations (3 mg ml-1), showing that mucin alone achieves mechanical properties similar to those of natural hagfish slime (mucins and protein threads). The main effects of added seawater salts, and predominantly CaCl2 is to reduce the intensity of the slow relaxation process, which suggests that calcium ions lead to an ionotropic gelation of hagfish mucins.