Complexation between porcine gastric mucin (PGM) and lysozyme: Influence of heat treatment of lysozyme on the tribological properties

The influence of complexation between porcine gastric mucin (PGM) and lysozyme (LYZ) solutions (pH⁓7.0) on their lubricating properties was studied at a hydrophobic self-mated polydimethylsiloxane (PDMS) tribopair. To this end, LYZ solutions with varying heating time, namely 1^hr, 3^hr-, and 6^hr at 90 °C, as well as unheated LYZ solution, were prepared. The lubricating capability of PGM and LYZ solutions and also their mixtures was characterized using pin-on-disk tribometry. In parallel, to precisely investigate the interaction between PGM and LYZ solutions, an array of the well-known experiments including electrophoretic-dynamic light scattering, circular dichroism spectroscopy and optical waveguide light-mode spectroscopy were employed. These experiments were utilized to elucidate the key features e.g. zeta potential, hydrodynamic diameter, conformational structure and mass adsorption. The tribometry results indicated that both PGM and unheated LYZ solutions had poor lubricating properties in the boundary lubrication regime (sliding speed lower than 10 mm/s). Mixing PGM with unheated LYZ led to a slight decrease in the friction coefficient, but no desirable lubricity was observed. An optimum slippery characteristic was achieved by incorporating 1^hr heated LYZ solution into PGM one. Excellent lubricity of PGM/1^hr heated LYZ may stem from surface charge compensation, tenaciously compact aggregation, unique conformational structure and considerable mass adsorption onto PDMS. This finding revealed that a strong interaction between PGM and LYZ molecules and as a result, the promising lubricating capability of PGM/LYZ mixtures, can be administered by varying heat-treatment duration of LYZ proteins.