A dynamic model of the effect of methyl resorcinol on the enzymatic activity of lysozyme

The lower boundary of the enzymatic activity of lysozyme is associated with the melting temperature of the liquid crystal formed by fringelike surface-layer loops and water; the upper boundary is related to transition of the fringelike surface layer from the glassy state to the coiled state. An analysis of the amino acid composition of the fringelike surface-layer loops reveals the active site cleft of lysozyme and the amino acid residues responsible for the capture and hydrolysis of the substrate. The modeling of the system of methyl resorcinol and fringelike surface-layer loops via the use of a system of two coupled oscillators affords grounds for describing the dependence of the activity of the lysozyme and methyl resorcinol system on the molar ratio of the components and makes it possible to determine the model parameters from experimental data. The analysis of the effect of the methyl resorcinol concentration on the enzymatic activity of lysozyme shows that the activity can increase relative to that of pure lysozyme within a narrow limit (no more than a factor of 3).