{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,30]],"date-time":"2026-10-30T15:15:42Z","timestamp":1793373342769,"version":"4.5.0"},"reference-count":62,"publisher":"Springer Science and Business Media LLC","issue":"1","license":[{"start":{"date-parts":[[2025,5,5]],"date-time":"2025-05-05T00:00:00Z","timestamp":1746403200000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"},{"start":{"date-parts":[[2025,5,5]],"date-time":"2025-05-05T00:00:00Z","timestamp":1746403200000},"content-version":"vor","delay-in-days":0,"URL":"https:\/\/creativecommons.org\/licenses\/by-nc-nd\/4.0"}],"content-domain":{"domain":["link.springer.com"],"crossmark-restriction":false},"short-container-title":["Sci Rep"],"DOI":"10.1038\/s41598-025-99141-2","type":"journal-article","created":{"date-parts":[[2025,5,5]],"date-time":"2025-05-05T03:14:47Z","timestamp":1746414887000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":7,"title":["From discovery to potential application: engineering a novel M23 peptidase to combat Listeria monocytogenes"],"prefix":"10.1038","volume":"15","author":[{"given":"Magdalena","family":"Kaus-Drobek","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marzena","family":"Nowacka","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Magdalena","family":"Gewartowska","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Ma\u0142gorzata","family":"Korzeniowska nee Wiweger","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Merete Rus\u00e5s","family":"Jensen","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Trond","family":"M\u00f8retr\u00f8","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Even","family":"Heir","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"El\u017cbieta","family":"Nowak","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Izabela","family":"Saba\u0142a","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2025,5,5]]},"reference":[{"key":"99141_CR1","doi-asserted-by":"publisher","first-page":"e00060","DOI":"10.1128\/cmr.00060-19","volume":"36","author":"MM Koopmans","year":"2023","unstructured":"Koopmans, M. M., Brouwer, M. C., V\u00e1zquez-Boland, J. A. & Van De Beek, D. Human listeriosis. Clin. Microbiol. Rev. 36, e00060\u2013e00019. https:\/\/doi.org\/10.1128\/cmr.00060-19 (2023).","journal-title":"Clin. Microbiol. Rev."},{"key":"99141_CR2","doi-asserted-by":"publisher","first-page":"632935","DOI":"10.3389\/fmicb.2021.632935","volume":"12","author":"B Zwirzitz","year":"2021","unstructured":"Zwirzitz, B. et al. Co-Occurrence of Listeria spp. And spoilage associated microbiota during meat processing due to Cross-Contamination events. Front. Microbiol. 12, 632935. https:\/\/doi.org\/10.3389\/fmicb.2021.632935 (2021).","journal-title":"Front. Microbiol."},{"key":"99141_CR3","doi-asserted-by":"publisher","unstructured":"Jarvis, N. A., Crandall, P. G., O\u2019Bryan, C. A. & Ricke, S. C. Antimicrobial resistance in Listeria spp. In Antimicrobial Resistance and Food Safety. 137\u2013153. https:\/\/doi.org\/10.1016\/B978-0-12-801214-7.00008-9. (Elsevier, 2015).","DOI":"10.1016\/B978-0-12-801214-7.00008-9"},{"key":"99141_CR4","doi-asserted-by":"publisher","first-page":"fnae060","DOI":"10.1093\/femsle\/fnae060","volume":"371","author":"J Wu","year":"2024","unstructured":"Wu, J., Wang, C. & O\u2019Byrne, C. Metabolic reprogramming in the food-borne pathogen Listeria monocytogenes as a critical defence against acid stress. FEMS Microbiol. Lett. 371, fnae060. https:\/\/doi.org\/10.1093\/femsle\/fnae060 (2024).","journal-title":"FEMS Microbiol. Lett."},{"key":"99141_CR5","doi-asserted-by":"publisher","first-page":"e01253","DOI":"10.1128\/AEM.01253-19","volume":"85","author":"A Roedel","year":"2019","unstructured":"Roedel, A. et al. Biocide-Tolerant Listeria monocytogenes isolates from German food production plants do not show Cross-Resistance to clinically relevant antibiotics. Appl. Environ. Microbiol. 85, e01253\u2013e01219. https:\/\/doi.org\/10.1128\/AEM.01253-19 (2019).","journal-title":"Appl. Environ. Microbiol."},{"key":"99141_CR6","doi-asserted-by":"publisher","first-page":"215","DOI":"10.1016\/j.ijfoodmicro.2016.10.025","volume":"241","author":"T M\u00f8retr\u00f8","year":"2017","unstructured":"M\u00f8retr\u00f8, T. et al. Tolerance to quaternary ammonium compound disinfectants May enhance growth of Listeria monocytogenes in the food industry. Int. J. Food Microbiol. 241, 215\u2013224. https:\/\/doi.org\/10.1016\/j.ijfoodmicro.2016.10.025 (2017).","journal-title":"Int. J. Food Microbiol."},{"key":"99141_CR7","doi-asserted-by":"publisher","first-page":"181","DOI":"10.3390\/microorganisms9010181","volume":"9","author":"T Mazaheri","year":"2021","unstructured":"Mazaheri, T., Cervantes-Huam\u00e1n, B. R. H., Berm\u00fadez-Capdevila, M., Ripolles-Avila, C. & Rodr\u00edguez-Jerez, J. J. Listeria monocytogenes biofilms in the food industry: is the current hygiene program sufficient to combat the persistence of the pathogen?? Microorganisms 9, 181. https:\/\/doi.org\/10.3390\/microorganisms9010181 (2021).","journal-title":"Microorganisms"},{"key":"99141_CR8","doi-asserted-by":"publisher","first-page":"792","DOI":"10.3390\/molecules25040792","volume":"25","author":"A Fagerlund","year":"2020","unstructured":"Fagerlund, A., Heir, E., M\u00f8retr\u00f8, T. & Langsrud, S. Listeria Monocytogenes biofilm removal using different commercial cleaning agents. Molecules 25, 792. https:\/\/doi.org\/10.3390\/molecules25040792 (2020).","journal-title":"Molecules"},{"key":"99141_CR9","doi-asserted-by":"publisher","unstructured":"European Food Safety Authority (EFSA), European Centre for Disease Prevention and Control (ECDC). The European Union One Health 2022 Zoonoses Report, EFS2 21. (2023). https:\/\/doi.org\/10.2903\/j.efsa.2023.8442","DOI":"10.2903\/j.efsa.2023.8442"},{"key":"99141_CR10","doi-asserted-by":"publisher","first-page":"525","DOI":"10.3390\/antibiotics13060525","volume":"13","author":"A Rippa","year":"2024","unstructured":"Rippa, A. et al. Antimicrobial resistance of Listeria monocytogenes strains isolated in food and food-Processing environments in Italy. Antibiotics 13, 525. https:\/\/doi.org\/10.3390\/antibiotics13060525 (2024).","journal-title":"Antibiotics"},{"key":"99141_CR11","doi-asserted-by":"publisher","unstructured":"Luque-Sastre, L. et al. Antimicrobial resistance in Listeria species. Microbiol. Spectr. 6, 6.4.19. https:\/\/doi.org\/10.1128\/microbiolspec.ARBA-0031-2017 (2018).","DOI":"10.1128\/microbiolspec.ARBA-0031-2017"},{"key":"99141_CR12","doi-asserted-by":"publisher","first-page":"605","DOI":"10.3389\/fmicb.2018.00605","volume":"9","author":"JA Gray","year":"2018","unstructured":"Gray, J. A. et al. Novel biocontrol methods for Listeria monocytogenes biofilms in food production facilities. Front. Microbiol. 9, 605. https:\/\/doi.org\/10.3389\/fmicb.2018.00605 (2018).","journal-title":"Front. Microbiol."},{"key":"99141_CR13","doi-asserted-by":"publisher","first-page":"480","DOI":"10.1016\/j.mib.2005.06.002","volume":"8","author":"MJ Loessner","year":"2005","unstructured":"Loessner, M. J. Bacteriophage endolysins \u2014 current state of research and applications. Curr. Opin. Microbiol. 8, 480\u2013487. https:\/\/doi.org\/10.1016\/j.mib.2005.06.002 (2005).","journal-title":"Curr. Opin. Microbiol."},{"key":"99141_CR14","doi-asserted-by":"publisher","first-page":"331","DOI":"10.3389\/fmicb.2019.00331","volume":"10","author":"A Vermassen","year":"2019","unstructured":"Vermassen, A. et al. Cell wall hydrolases in bacteria: insight on the diversity of cell wall amidases, glycosidases and peptidases toward peptidoglycan. Front. Microbiol. 10, 331. https:\/\/doi.org\/10.3389\/fmicb.2019.00331 (2019).","journal-title":"Front. Microbiol."},{"key":"99141_CR15","doi-asserted-by":"publisher","first-page":"29","DOI":"10.3390\/antibiotics7020029","volume":"7","author":"C S\u00e3o-Jos\u00e9","year":"2018","unstructured":"S\u00e3o-Jos\u00e9, C. Engineering of Phage-Derived lytic enzymes: improving their potential as antimicrobials. Antibiotics 7, 29. https:\/\/doi.org\/10.3390\/antibiotics7020029 (2018).","journal-title":"Antibiotics"},{"key":"99141_CR16","doi-asserted-by":"publisher","unstructured":"Eichenseher, F. et al. Linker-Improved chimeric endolysin selectively kills Staphylococcus aureus in vitro, on reconstituted human epidermis, and in a murine model of skin infection. Antimicrob. Agents Chemother.  e0227321. https:\/\/doi.org\/10.1128\/aac.02273-21 (2022).","DOI":"10.1128\/aac.02273-21"},{"key":"99141_CR17","doi-asserted-by":"publisher","first-page":"461","DOI":"10.1089\/mdr.2016.0053","volume":"22","author":"E Jagielska","year":"2016","unstructured":"Jagielska, E., Chojnacka, O. & Saba\u0142a, I. LytM fusion with SH3b-Like domain expands its activity to physiological conditions. Microb. Drug Resist. 22, 461\u2013469. https:\/\/doi.org\/10.1089\/mdr.2016.0053 (2016).","journal-title":"Microb. Drug Resist."},{"key":"99141_CR18","doi-asserted-by":"publisher","first-page":"e03546","DOI":"10.1128\/spectrum.03546-23","volume":"12","author":"P Mitkowski","year":"2024","unstructured":"Mitkowski, P., Jagielska, E. & Saba\u0142a, I. Engineering of chimeric enzymes with expanded tolerance to ionic strength. Microbiol. Spectr. 12, e03546\u2013e03523. https:\/\/doi.org\/10.1128\/spectrum.03546-23 (2024).","journal-title":"Microbiol. Spectr."},{"key":"99141_CR19","doi-asserted-by":"publisher","first-page":"2169","DOI":"10.3390\/cells12172169","volume":"12","author":"A Nazir","year":"2023","unstructured":"Nazir, A., Xu, X., Liu, Y. & Chen, Y. Phage endolysins: advances in the world of food safety. Cells 12, 2169. https:\/\/doi.org\/10.3390\/cells12172169 (2023).","journal-title":"Cells"},{"key":"99141_CR20","doi-asserted-by":"publisher","first-page":"76","DOI":"10.1016\/j.copbio.2015.10.005","volume":"37","author":"M Schmelcher","year":"2016","unstructured":"Schmelcher, M. & Loessner, M. J. Bacteriophage endolysins: applications for food safety. Curr. Opin. Biotechnol. 37, 76\u201387. https:\/\/doi.org\/10.1016\/j.copbio.2015.10.005 (2016).","journal-title":"Curr. Opin. Biotechnol."},{"key":"99141_CR21","doi-asserted-by":"publisher","first-page":"47","DOI":"10.3168\/jdsc.2020-0013","volume":"2","author":"MJ Holle","year":"2021","unstructured":"Holle, M. J. & Miller, M. J. Lytic characterization and application of Listerial endolysins PlyP40 and PlyPSA in Queso fresco. JDS Commun. 2, 47\u201350. https:\/\/doi.org\/10.3168\/jdsc.2020-0013 (2021).","journal-title":"JDS Commun."},{"key":"99141_CR22","doi-asserted-by":"publisher","first-page":"651","DOI":"10.1111\/j.1751-7915.2011.00263.x","volume":"4","author":"M Schmelcher","year":"2011","unstructured":"Schmelcher, M., Tchang, V. S. & Loessner, M. J. Domain shuffling and module engineering of Listeria phage endolysins for enhanced lytic activity and binding affinity. Microb. Biotechnol. 4, 651\u2013662. https:\/\/doi.org\/10.1111\/j.1751-7915.2011.00263.x (2011).","journal-title":"Microb. Biotechnol."},{"key":"99141_CR23","doi-asserted-by":"publisher","first-page":"W116","DOI":"10.1093\/nar\/gki442","volume":"33","author":"E Quevillon","year":"2005","unstructured":"Quevillon, E. et al. InterProScan: protein domains identifier. Nucleic Acids Res. 33, W116\u2013120. https:\/\/doi.org\/10.1093\/nar\/gki442 (2005).","journal-title":"Nucleic Acids Res."},{"key":"99141_CR24","doi-asserted-by":"publisher","first-page":"4112","DOI":"10.1111\/febs.12929","volume":"281","author":"I Sabala","year":"2014","unstructured":"Sabala, I. et al. Crystal structure of the antimicrobial peptidase lysostaphin from Staphylococcus simulans. FEBS J. 281, 4112\u20134122. https:\/\/doi.org\/10.1111\/febs.12929 (2014).","journal-title":"FEBS J."},{"key":"99141_CR25","doi-asserted-by":"publisher","first-page":"578","DOI":"10.1016\/j.jmb.2005.09.082","volume":"354","author":"M Firczuk","year":"2005","unstructured":"Firczuk, M., Mucha, A. & Bochtler, M. Crystal structures of active LytM. J. Mol. Biol. 354, 578\u2013590. https:\/\/doi.org\/10.1016\/j.jmb.2005.09.082 (2005).","journal-title":"J. Mol. Biol."},{"key":"99141_CR26","doi-asserted-by":"publisher","first-page":"719689","DOI":"10.3389\/fmicb.2021.719689","volume":"12","author":"A Wysocka","year":"2021","unstructured":"Wysocka, A., Jagielska, E., \u0141\u0119\u017cniak, \u0141. & Saba\u0142a, I. Two new M23 peptidoglycan hydrolases with distinct net charge. Front. Microbiol. 12, 719689. https:\/\/doi.org\/10.3389\/fmicb.2021.719689 (2021).","journal-title":"Front. Microbiol."},{"key":"99141_CR27","doi-asserted-by":"publisher","unstructured":"Wysocka, A., \u0141\u0119\u017cniak, \u0141., Jagielska, E. & Saba\u0142a, I. Electrostatic interaction with the bacterial cell envelope Tunes the lytic activity of two novel peptidoglycan hydrolases. Microbiol. Spectr. e0045522. https:\/\/doi.org\/10.1128\/spectrum.00455-22 (2022).","DOI":"10.1128\/spectrum.00455-22"},{"key":"99141_CR28","doi-asserted-by":"publisher","first-page":"585","DOI":"10.3390\/foods2040585","volume":"2","author":"M Hussain","year":"2013","unstructured":"Hussain, M. & Dawson, C. Economic impact of food safety outbreaks on food businesses. Foods 2, 585\u2013589. https:\/\/doi.org\/10.3390\/foods2040585 (2013).","journal-title":"Foods"},{"key":"99141_CR29","doi-asserted-by":"publisher","first-page":"1198124","DOI":"10.3389\/fmicb.2023.1198124","volume":"14","author":"S Karanth","year":"2023","unstructured":"Karanth, S., Feng, S., Patra, D. & Pradhan, A. K. Linking microbial contamination to food spoilage and food waste: the role of smart packaging, spoilage risk assessments, and date labeling. Front. Microbiol. 14, 1198124. https:\/\/doi.org\/10.3389\/fmicb.2023.1198124 (2023).","journal-title":"Front. Microbiol."},{"key":"99141_CR30","doi-asserted-by":"publisher","first-page":"298","DOI":"10.1016\/j.meatsci.2013.05.023","volume":"97","author":"E Giaouris","year":"2014","unstructured":"Giaouris, E. et al. Attachment and biofilm formation by foodborne bacteria in meat processing environments: causes, implications, role of bacterial interactions and control by alternative novel methods. Meat Sci. 97, 298\u2013309. https:\/\/doi.org\/10.1016\/j.meatsci.2013.05.023 (2014).","journal-title":"Meat Sci."},{"key":"99141_CR31","doi-asserted-by":"publisher","first-page":"e01046","DOI":"10.1128\/AEM.01046-17","volume":"83","author":"A Fagerlund","year":"2017","unstructured":"Fagerlund, A., M\u00f8retr\u00f8, T., Heir, E., Briandet, R. & Langsrud, S. Cleaning and disinfection of biofilms composed of Listeria monocytogenes and background microbiota from meat processing surfaces. Appl. Environ. Microbiol. 83, e01046\u2013e01017. https:\/\/doi.org\/10.1128\/AEM.01046-17 (2017).","journal-title":"Appl. Environ. Microbiol."},{"key":"99141_CR32","doi-asserted-by":"publisher","first-page":"D503","DOI":"10.1093\/nar\/gkt953","volume":"42","author":"ND Rawlings","year":"2014","unstructured":"Rawlings, N. D., Waller, M., Barrett, A. J. & Bateman, A. MEROPS: the database of proteolytic enzymes, their substrates and inhibitors. Nucleic Acids Res. 42, D503\u2013509. https:\/\/doi.org\/10.1093\/nar\/gkt953 (2014).","journal-title":"Nucleic Acids Res."},{"key":"99141_CR33","doi-asserted-by":"publisher","unstructured":"Razew, A., Schwarz, J. N., Mitkowski, P., Sabala, I. & Kaus-Drobek, M. One fold, many functions\u2014M23 family of peptidoglycan hydrolases. Front. Microbiol.  13.  https:\/\/www.frontiersin.org\/articles\/. https:\/\/doi.org\/10.3389\/fmicb.2022.1036964  (2022).  Accessed 28 Dec 2022.","DOI":"10.3389\/fmicb.2022.1036964"},{"key":"99141_CR34","doi-asserted-by":"publisher","first-page":"1072","DOI":"10.1111\/jam.14985","volume":"131","author":"J Jayakumar","year":"2021","unstructured":"Jayakumar, J., Kumar, V. A., Biswas, L. & Biswas, R. Therapeutic applications of lysostaphin against Staphylococcus aureus. J. Appl. Microbiol. 131, 1072\u20131082. https:\/\/doi.org\/10.1111\/jam.14985 (2021).","journal-title":"J. Appl. Microbiol."},{"key":"99141_CR35","doi-asserted-by":"publisher","first-page":"3449","DOI":"10.1007\/s00253-012-4252-4","volume":"97","author":"I Abaev","year":"2013","unstructured":"Abaev, I. et al. Staphylococcal phage 2638A endolysin is lytic for Staphylococcus aureus and harbors an inter-lytic-domain secondary translational start site. Appl. Microbiol. Biotechnol. 97, 3449\u20133456. https:\/\/doi.org\/10.1007\/s00253-012-4252-4 (2013).","journal-title":"Appl. Microbiol. Biotechnol."},{"key":"99141_CR36","doi-asserted-by":"publisher","first-page":"107","DOI":"10.1017\/S1479050504001322","volume":"1","author":"T M\u00f8retr\u00f8","year":"2004","unstructured":"M\u00f8retr\u00f8, T. & Langsrud, S. Listeria monocytogenes: biofilm formation and persistence in food-processing environments. Biofilms 1, 107\u2013121. https:\/\/doi.org\/10.1017\/S1479050504001322 (2004).","journal-title":"Biofilms"},{"key":"99141_CR37","doi-asserted-by":"publisher","unstructured":"EFSA Panel on Biological Hazards (BIOHAZ). Evaluation of the safety and efficacy of listex\u2122 P100 for reduction of pathogens on different ready-to-eat (RTE) food products. EFS2 14. https:\/\/doi.org\/10.2903\/j.efsa.2016.4565 (2016).","DOI":"10.2903\/j.efsa.2016.4565"},{"key":"99141_CR38","unstructured":"Kasra-Kermanshahi, R. & Mobarak-Qamsari, E. Inhibition Effect of Lactic Acid Bacteria Against Food Born Pathogen, Listeria monocytogenes. Vol.  2 (2015)."},{"key":"99141_CR39","doi-asserted-by":"publisher","first-page":"689","DOI":"10.1007\/s13197-017-2979-8","volume":"55","author":"P Castellano","year":"2018","unstructured":"Castellano, P. et al. Antilisterial efficacy of Lactobacillus bacteriocins and organic acids on frankfurters. Impact on sensory characteristics. J. Food Sci. Technol. 55, 689\u2013697. https:\/\/doi.org\/10.1007\/s13197-017-2979-8 (2018).","journal-title":"J. Food Sci. Technol."},{"key":"99141_CR40","doi-asserted-by":"publisher","first-page":"fuad023","DOI":"10.1093\/femsre\/fuad023","volume":"47","author":"D Field","year":"2023","unstructured":"Field, D., Fernandez de Ullivarri, M., Ross, R. P. & Hill, C. After a century of Nisin research - where are we now? FEMS Microbiol. Rev. 47, fuad023. https:\/\/doi.org\/10.1093\/femsre\/fuad023 (2023).","journal-title":"FEMS Microbiol. Rev."},{"key":"99141_CR41","doi-asserted-by":"publisher","first-page":"1262","DOI":"10.1080\/10408398.2013.763765","volume":"56","author":"A Gharsallaoui","year":"2016","unstructured":"Gharsallaoui, A., Oulahal, N., Joly, C. & Degraeve, P. Nisin as a food preservative: part 1: physicochemical properties, antimicrobial activity, and main uses. Crit. Rev. Food Sci. Nutr. 56, 1262\u20131274. https:\/\/doi.org\/10.1080\/10408398.2013.763765 (2016).","journal-title":"Crit. Rev. Food Sci. Nutr."},{"key":"99141_CR42","doi-asserted-by":"publisher","first-page":"2041","DOI":"10.3168\/jds.2019-17498","volume":"103","author":"LA Ibarra-S\u00e1nchez","year":"2020","unstructured":"Ibarra-S\u00e1nchez, L. A., El-Haddad, N., Mahmoud, D., Miller, M. J. & Karam, L. Invited review: advances in Nisin use for preservation of dairy products. J. Dairy Sci. 103, 2041\u20132052. https:\/\/doi.org\/10.3168\/jds.2019-17498 (2020).","journal-title":"J. Dairy Sci."},{"key":"99141_CR43","doi-asserted-by":"publisher","first-page":"104207","DOI":"10.1016\/j.fm.2022.104207","volume":"111","author":"J Wu","year":"2023","unstructured":"Wu, J. et al. Nisin: from a structural and meat preservation perspective. Food Microbiol. 111, 104207. https:\/\/doi.org\/10.1016\/j.fm.2022.104207 (2023).","journal-title":"Food Microbiol."},{"key":"99141_CR44","doi-asserted-by":"publisher","first-page":"2873","DOI":"10.1128\/aem.61.8.2873-2878.1995","volume":"61","author":"HS Rollema","year":"1995","unstructured":"Rollema, H. S., Kuipers, O. P., Both, P., De Vos, W. M. & Siezen, R. J. Improvement of solubility and stability of the antimicrobial peptide Nisin by protein engineering. Appl. Environ. Microbiol. 61, 2873\u20132878. https:\/\/doi.org\/10.1128\/aem.61.8.2873-2878.1995 (1995).","journal-title":"Appl. Environ. Microbiol."},{"key":"99141_CR45","doi-asserted-by":"publisher","first-page":"171","DOI":"10.1016\/j.micpath.2019.01.002","volume":"128","author":"R Kumariya","year":"2019","unstructured":"Kumariya, R. et al. Bacteriocins: classification, synthesis, mechanism of action and resistance development in food spoilage causing bacteria. Microb. Pathog. 128, 171\u2013177. https:\/\/doi.org\/10.1016\/j.micpath.2019.01.002 (2019).","journal-title":"Microb. Pathog."},{"key":"99141_CR46","doi-asserted-by":"publisher","first-page":"fnad019","DOI":"10.1093\/femsle\/fnad019","volume":"370","author":"IB Jaskulski","year":"2023","unstructured":"Jaskulski, I. B. et al. Listeria monocytogenes from food and food industry environments with reduced susceptibility to Benzalkonium chloride, sodium hypochlorite, and peracetic acid. FEMS Microbiol. Lett. 370, fnad019. https:\/\/doi.org\/10.1093\/femsle\/fnad019 (2023).","journal-title":"FEMS Microbiol. Lett."},{"key":"99141_CR47","doi-asserted-by":"publisher","first-page":"100177","DOI":"10.1016\/j.bioflm.2024.100177","volume":"7","author":"ML Rolon","year":"2024","unstructured":"Rolon, M. L., Voloshchuk, O., Bartlett, K. V., LaBorde, L. F. & Kovac, J. Multi-species biofilms of environmental microbiota isolated from fruit packing facilities promoted tolerance of Listeria monocytogenes to Benzalkonium chloride. Biofilm 7, 100177. https:\/\/doi.org\/10.1016\/j.bioflm.2024.100177 (2024).","journal-title":"Biofilm"},{"key":"99141_CR48","doi-asserted-by":"publisher","unstructured":"Pennone, V. et al. Inhibition of L. monocytogenes biofilm formation by the amidase domain of the phage vB_LmoS_293 endolysin. Viruses 11. https:\/\/doi.org\/10.3390\/v11080722 (2019).","DOI":"10.3390\/v11080722"},{"key":"99141_CR49","doi-asserted-by":"publisher","unstructured":"Santativongchai, P. P., Tulayakul, P. P. & Jeon, B. Enhancement of the antibiofilm activity of Nisin against Listeria monocytogenes using food plant extracts. Pathogens 12, 444. https:\/\/doi.org\/10.3390\/pathogens12030444 (2023).","DOI":"10.3390\/pathogens12030444"},{"key":"99141_CR50","doi-asserted-by":"publisher","first-page":"1","DOI":"10.1007\/s12602-011-9084-5","volume":"4","author":"M Simmons","year":"2012","unstructured":"Simmons, M., Morales, C. A., Oakley, B. B. & Seal, B. S. Recombinant expression of a putative amidase cloned from the genome of Listeria monocytogenes that lyses the bacterium and its monolayer in conjunction with a protease. Probiotics Antimicro Prot. 4, 1\u201310. https:\/\/doi.org\/10.1007\/s12602-011-9084-5 (2012).","journal-title":"Probiotics Antimicro Prot."},{"key":"99141_CR51","doi-asserted-by":"publisher","first-page":"2572","DOI":"10.3390\/foods11172572","volume":"11","author":"E Tirloni","year":"2022","unstructured":"Tirloni, E. et al. Bacillus cereus in dairy products and production plants. Foods 11, 2572. https:\/\/doi.org\/10.3390\/foods11172572 (2022).","journal-title":"Foods"},{"key":"99141_CR52","doi-asserted-by":"publisher","first-page":"110827","DOI":"10.1016\/j.ijfoodmicro.2024.110827","volume":"423","author":"A Perdomo","year":"2024","unstructured":"Perdomo, A. & Calle, A. Assessment of microbial communities in a dairy farm from a food safety perspective. Int. J. Food Microbiol. 423, 110827. https:\/\/doi.org\/10.1016\/j.ijfoodmicro.2024.110827 (2024).","journal-title":"Int. J. Food Microbiol."},{"key":"99141_CR53","doi-asserted-by":"publisher","first-page":"235","DOI":"10.1016\/j.fm.2012.09.022","volume":"33","author":"IC Fern\u00e1ndez-No","year":"2013","unstructured":"Fern\u00e1ndez-No, I. C. et al. Characterisation and profiling of Bacillus subtilis, Bacillus cereus and Bacillus licheniformis by MALDI-TOF mass fingerprinting. Food Microbiol. 33, 235\u2013242. https:\/\/doi.org\/10.1016\/j.fm.2012.09.022 (2013).","journal-title":"Food Microbiol."},{"key":"99141_CR54","doi-asserted-by":"publisher","first-page":"1022","DOI":"10.1111\/1541-4337.12283","volume":"16","author":"T M\u00f8retr\u00f8","year":"2017","unstructured":"M\u00f8retr\u00f8, T. & Langsrud, S. Residential Bacteria on surfaces in the food industry and their implications for food safety and quality. Comp. Rev. Food Sci. Food Safe. 16, 1022\u20131041. https:\/\/doi.org\/10.1111\/1541-4337.12283 (2017).","journal-title":"Comp. Rev. Food Sci. Food Safe"},{"key":"99141_CR55","doi-asserted-by":"publisher","first-page":"91","DOI":"10.1007\/978-1-59745-196-3_6","volume-title":"High Throughput Protein Expression and Purification: Methods and Protocols","author":"HE Klock","year":"2009","unstructured":"Klock, H. E. & Lesley, S. A. The polymerase incomplete primer extension (PIPE) method applied to High-Throughput cloning and Site-Directed mutagenesis, in: (ed Doyle, S. A.) High Throughput Protein Expression and Purification: Methods and Protocols, Humana, Totowa, NJ, : 91\u2013103. https:\/\/doi.org\/10.1007\/978-1-59745-196-3_6. (2009)."},{"key":"99141_CR56","doi-asserted-by":"publisher","unstructured":"Kabsch, W.  XDS. Acta Crystallogr. D Biol. Crystallogr. 66,  125\u2013132. (2010). https:\/\/doi.org\/10.1107\/S0907444909047337","DOI":"10.1107\/S0907444909047337"},{"key":"99141_CR57","doi-asserted-by":"publisher","first-page":"568","DOI":"10.1107\/S0021889812011715","volume":"45","author":"M Krug","year":"2012","unstructured":"Krug, M., Weiss, M. S., Heinemann, U. & Mueller, U. XDSAPP: a graphical user interface for the convenient processing of diffraction data using XDS. J. Appl. Cryst. 45, 568\u2013572. https:\/\/doi.org\/10.1107\/S0021889812011715 (2012).","journal-title":"J. Appl. Cryst."},{"key":"99141_CR58","doi-asserted-by":"publisher","first-page":"658","DOI":"10.1107\/S0021889807021206","volume":"40","author":"AJ McCoy","year":"2007","unstructured":"McCoy, A. J. et al. Phaser crystallographic software. J. Appl. Crystallogr. 40, 658\u2013674. https:\/\/doi.org\/10.1107\/S0021889807021206 (2007).","journal-title":"J. Appl. Crystallogr."},{"key":"99141_CR59","doi-asserted-by":"publisher","first-page":"352","DOI":"10.1107\/S0907444912001308","volume":"68","author":"PV Afonine","year":"2012","unstructured":"Afonine, P. V. et al. Towards automated crystallographic structure refinement with phenix.refine. Acta Cryst. D. 68, 352\u2013367. https:\/\/doi.org\/10.1107\/S0907444912001308 (2012).","journal-title":"Acta Cryst. D"},{"key":"99141_CR60","doi-asserted-by":"publisher","first-page":"2126","DOI":"10.1107\/S0907444904019158","volume":"60","author":"P Emsley","year":"2004","unstructured":"Emsley, P. & Cowtan, K. Coot: model-building tools for molecular graphics. Acta Crystallogr. D Biol. Crystallogr. 60, 2126\u20132132. https:\/\/doi.org\/10.1107\/S0907444904019158 (2004).","journal-title":"Acta Crystallogr. D Biol. Crystallogr."},{"key":"99141_CR61","doi-asserted-by":"publisher","first-page":"3132","DOI":"10.1128\/AAC.00124-10","volume":"54","author":"M Hartmann","year":"2010","unstructured":"Hartmann, M. et al. Damage of the bacterial cell envelope by antimicrobial peptides Gramicidin S and PGLa as revealed by transmission and scanning Electron microscopy. Antimicrob. Agents Chemother. 54, 3132\u20133142. https:\/\/doi.org\/10.1128\/AAC.00124-10 (2010).","journal-title":"Antimicrob. Agents Chemother."},{"key":"99141_CR62","doi-asserted-by":"publisher","unstructured":"OECD Guidelines for the Testing of Chemicals. Test No. 236: Fish Embryo Acute Toxicity (FET) Test, OECD Guidelines for the Testing of Chemicals, Section\u00a02 (OECD Publishing, 2013). https:\/\/doi.org\/10.1787\/9789264203709-en","DOI":"10.1787\/9789264203709-en"}],"container-title":["Scientific Reports"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-99141-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-99141-2","content-type":"text\/html","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-99141-2.pdf","content-type":"application\/pdf","content-version":"vor","intended-application":"similarity-checking"}],"deposited":{"date-parts":[[2025,5,5]],"date-time":"2025-05-05T03:14:49Z","timestamp":1746414889000},"score":1,"resource":{"primary":{"URL":"https:\/\/www.nature.com\/articles\/s41598-025-99141-2"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2025,5,5]]},"references-count":62,"journal-issue":{"issue":"1","published-online":{"date-parts":[[2025,12]]}},"alternative-id":["99141"],"URL":"https:\/\/doi.org\/10.1038\/s41598-025-99141-2","relation":{},"ISSN":["2045-2322"],"issn-type":[{"value":"2045-2322","type":"electronic"}],"subject":[],"published":{"date-parts":[[2025,5,5]]},"assertion":[{"value":"15 January 2025","order":1,"name":"received","label":"Received","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"17 April 2025","order":2,"name":"accepted","label":"Accepted","group":{"name":"ArticleHistory","label":"Article History"}},{"value":"5 May 2025","order":3,"name":"first_online","label":"First Online","group":{"name":"ArticleHistory","label":"Article History"}},{"order":1,"name":"Ethics","group":{"name":"EthicsHeading","label":"Declarations"}},{"value":"Magdalena Kaus-Drobek, Marzena Nowacka and Izabela Sabala are authors of a patent application filed with the Polish Patent Office (ID: ZP.261.018.2024.017), entitled \u201cRecombinant peptidoglycan hydrolase protein with antibacterial properties, compositions containing it, their applications, and methods of use\".\u00a0Izabela Saba\u0142a is an Editorial Board Member in Scientific Reports in Structural and Molecular Biology section.","order":2,"name":"Ethics","group":{"name":"EthicsHeading","label":"Competing interests"}}],"article-number":"15628"}}