Abstract
The ability of alkylhydroxybenzenes to change the enzyme activity of hen egg white lysozyme and its efficiency in the catalyzed hydrolysis of nonspecific substrates (chitin and yeasts) was demonstrated. A homolog, C7-AHB, was used as a modifier; this substance increased the lysozyme enzymatic activity over the entire studied range of concentrations. The effect of C7-AHB concentration (0.125–4.0 mg/ml), species (initial or oxidized), and the time (1–24 h) of lysozyme incubation with C7-AHB at 25°C in 0.05 M phosphate buffer (pH 7.4) on the lysozyme activity were studied by differential scanning microcalorimetry, as well as the thermodynamic parameters of its denaturation. The kinetic parameters of chitin hydrolysis by the C7-AHB-modified lysozyme were determined.
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