Kinetics of inactivation of staphylolytic enzymes: Qualitative and quantitative description.

Lysin 2638aR and chimeric Ply187AN-KSH3b fusion protein are capable of lysing antibiotic-resistant strains of Staphylococcus aureus and are promising alternatives to antibiotics. Studies on the stability and structure of lysins 2638aR and Ply187AN-KSH3b are important for assessing the feasibility of their practical use. Both lysins are highly active at physiological pH (7.

A Chimeric LysK-Lysostaphin Fusion Enzyme Lysing Staphylococcus aureus Cells: a Study of Both Kinetics of Inactivation and Specifics of Interaction with Anionic Polymers.

A staphylolytic fusion protein (chimeric enzyme K-L) was created, harboring three unique lytic activities composed of the LysK CHAP endopeptidase, and amidase domains, and the lysostaphin glycyl-glycine endopeptidase domain. To assess the potential of possible therapeutic applications, the kinetic behavior of chimeric enzyme K-L was investigated. As a protein antimicrobial, with potential antigenic properties, the biophysical effect of including chimeric enzyme K-L in anionic polymer matrices that might help reduce the immunogenicity of the enzyme was tested.

Bacteriophage phi11 lysin: Physicochemical characterization and comparison with phage phi80α lysin.

Phage lytic enzymes are promising antimicrobial agents. Lysins of phages phi11 (LysPhi11) and phi80α (LysPhi80α) can lyse (destroy) cells of antibiotic-resistant strains of Staphylococcus aureus. Stability of enzymes is one of the parameters making their practical use possible.

Peptidoglycan degrading activity of the broad-range Salmonella bacteriophage S-394 recombinant endolysin.

The use of bacteriophage endolysins as specific antibacterial agents is a prospective strategy to treat bacterial infections caused by antibiotic-resistant pathogens. In case of Gram-negative species this strategy has limited applications since outer membrane shields the enzyme target and prevents bacteria lysis. We aimed to obtain and characterize the endolysin of the newly discovered anti-Salmonella bacteriophage S-394 (Lys394) and to choose an appropriate permeabilizing agent to disrupt Escherichia coli cells suspended in buffer solution and grown on agar surface.