Kinetic analysis as an approach to studying specific features of lysozyme—pluronic complexes

A deviation of the dependence of the lysis rate of Micrococcus luteus cells from the Michaelis—Menten kinetics after lysozyme incubation with pluronic P123 for 2 days was observed by the study of the interaction of pluronic P123 and hen egg-white lysozyme (HEWL). The observed deviation is presumably induced by the formation of two complexes differed in catalytic properties in the system, depending on the cell concentration. The ratio of the formed complexes is determined by the substrate concentration. The interaction with the pluronic changes the catalytic properties of HEWL. An increase in the cell concentration results probably in the simultaneous binding of HEWL with the substrate and pluronic, inducing structural changes in the active site of the enzyme and changes in the bacteriolytic activity.