Abstract
The effect of glycine, glutamate, aspartate, lysine, histidine, and arginine on the adsorption of lysozyme on living Escherichia coli bacterial cells under conditions close to those for the functioning of the enzyme in saliva was studied. It was shown that the addition of the listed amino acids at concentrations of 1.5 mM for glycine and 5 mM for charged amino acids reduced the desorption constant of lysozyme by 1.4–2.0 times, while the rate of cell lysis (lysozyme activity) increased by 1.4–1.9 times. The maximum amount of lysozyme that can bind to bacteria (adsorption capacity) did not change. An increase in the efficiency of cell lysis in the presence of glycine and charged amino acids can be explained by an increase in the productive adsorption of the enzyme on the surface of bacterial cells.
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