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EN
In this review proteolytic enzymes of starter microflora involved in cheese ripening are described. The best known system is the proteolytic system of primary starter represented by mesophilic and thermophilic lactic acid bacteria. An important role in the ripening of some kind of cheeses is played by enzymes of secondary starter represented by propionic acid bacteria, Brevibacterium linens and some strains of fungi of Penicillium genus. The extent of proteolysis and flavour development in cheese depends on the activity and specificity of all these proteases.
EN
Lysostaphin is a zinc metalloproteinase extracted from Staphylococcus simulans biovar staphylolyticus that degrades the cell wall of almost all known staphylococcal species. The target of the lysostaphin activity is the pentaglycine interpeptide bridges of the unique staphylococcal peptidoglycan, where the enzyme cleaves the Gly-Gly bond and lyses cells in all metabolic states (growing, resting, or heat killed). The specificity of the pentaglycine peptide is very high and other gram-positive and gram?negative bacteria are not susceptible to this enzyme. The unique biological activity of lysostaphin presents numerous possibilities for applications of this enzyme in the medical, veterinary, food industry and research fields. Lysostaphin is frequently used as a staphylolytic agent for the liberation of intracellular enzymes, nucleic acids, and cell membrane and surface components. Lysostaphin was tested as a chemotherapeutic agent. Lysostaphin application was also shown to be effective in reducing the nasal carriage of S. aureus in humans. There are also examples for application of this enzyme in food protection.
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