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The species <jats:italic>Lysobacter capsici<\/jats:italic> VKM B-2533<jats:sup>T<\/jats:sup> possesses a potent antimicrobial action against a number of bacteria, fungi and yeasts. Its activity can be due to the impact of bacteriolytic enzymes, antibiotics and peptides. This work isolated four homogeneous bacteriolytic enzymes and a mixture of two proteins, which also had a bacteriolytic activity. The isolates included proteins identical to <jats:italic>L. enzymogenes<\/jats:italic> \u03b1- and \u03b2-lytic proteases and lysine-specific protease. The proteases of 26\u2009kDa and 29\u2009kDa and a protein identified as N-acetylglycosaminidase had not been isolated in <jats:italic>Lysobacter<\/jats:italic> earlier. The isolated \u03b2-lytic protease digested live methicillin-resistant staphylococcal cells with high efficiency (minimal inhibitory concentration, 2.85\u2009\u03bcg\/mL). This property makes the enzyme deserving special attention. A recombinant \u03b2-lytic protease was produced. The antimicrobial potential of the bacterium was contributed to by outer membrane vesicles (OMVs). <jats:italic>L. capsici<\/jats:italic> cells were found to form a group of OMVs responsible for antifungal activity. The data are indicative of a significant antimicrobial potential of this bacterium that requires thorough research.<\/jats:p>","DOI":"10.1038\/s41598-020-67122-2","type":"journal-article","created":{"date-parts":[[2020,6,19]],"date-time":"2020-06-19T10:03:27Z","timestamp":1592561007000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":42,"title":["Lytic potential of Lysobacter capsici VKM B-2533T: bacteriolytic enzymes and outer membrane vesicles"],"prefix":"10.1038","volume":"10","author":[{"given":"A. S.","family":"Afoshin","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"I. 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