Abstract
The possibilities of bacteriophage SPZ7 endolysin functioning in the lysis of gram-negative bacteria “from without” were studied. A significant 1.5–3-fold increase in bacteriophage SPZ7 endolysin activity during the lysis of S. enteritidis N60 and E. coli TG1 cells in the presence of high-molecular surfactants, pluronics with a large hydrophobic block, hen’s egg lysozyme, and low concentrations of a peptide antibiotic (colistin), was shown. The developed approach may be promising for improving the efficiency of pharmaceutical bacteriophage enzyme-based antibacterials working against gram-negative microorganisms.
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