Adsorption of Lysozyme on Living Cells of Escherichia coli and its Bacteriolytic Activity in the Presence of Glycine and Charged Amino Acids

For human and chicken lysozyme, the relationship between changes in the parameters of enzyme adsorption on living Escherichia coli bacterial cells and the value of its effective bacteriolytic activity in the presence of glycine and charged amino acids is studied. It is shown for both human and chicken lysozyme that free amino acids added to a concentration of 1.5 mM for glycine or 5.0 mM for glutamate, aspartate, histidine, arginine, and lysine reduce the desorption constant of the enzyme on bacterial cells by factors of 1.4 to 2.0. At the same time, an increase in the bacteriolytic activity of lysozyme by factors of 1.5 to 1.9 is also observed. Thus, the enhancement of antibacterial activity in the presence of glycine and charged amino acids can be explained by the improvement in the productive sorption of the enzyme on the substrate of the bacterial cells.