Lytic Enzymes of Staphylococcal Phages: Correlation between Secondary Structure and Stability
Lytic enzymes of bacteriophages K, phi11 and phi80α are able to lyse (destroy) cells of antibiotic resistant strains of Staphylococcus aureus, and they can be considered as promising antimicrobial agents. The stability of recombinant lysins of phages K, phi11 and phi80α was investigated in conditions of storage and functioning, and the relationship between the stability and the secondary structure of the enzymes was found. It was shown that the lower the content of disordered structures in the molecules of enzymes, the greater the stability of lysins (half-inactivation time). Beta-structural lysin of phage phi11 shows the best stability at storage temperature (22°C), both lysin of phage K with alpha-helical structure and lysin of phage phi80α with disordered secondary structure are less stable.