Original Research ARTICLE
Characterization of Milkisin, a novel lipopeptide with antimicrobial properties produced by Pseudomonas sp. UCMA 17988 isolated from bovine raw milk
- 1UNICAEN, UNIROUEN, ABTE, Normandie Université, France
- 2UNIROUEN, INSA Rouen, CNRS, COBRA, Normandie Université, France
- 3UNICAEN, SF ICORE 4206 Proteogen, Normandie Université, France
Biosurfactants such as lipopeptides are amphiphilic compounds produced by microorganisms such as bacteria of the genera of Pseudomonas and Bacillus. Some of these molecules proved to have interesting antimicrobial, antiviral, insecticide and/or tensio-active properties that are potentially useful for the agricultural, chemical, food and pharmaceutical industries. Raw milk provides a physicochemical environment that is favorable to the multiplication of a broad spectrum of microorganisms. Among them, psychrotrophic bacterial species, especially members of the genus Pseudomonas, are predominant and colonize milk during cold storage and/or processing. We isolated the strain Pseudomonas sp. UCMA 17988 from raw cow milk, with antagonistic activity against Listeria monocytogenes, Staphylococcus aureus and Salmonella enterica Newport. Antimicrobial molecules involved in the antagonistic activity of this strain were characterized. A mass spectrometry analysis highlighted the presence of 4 lipopeptides isoforms. The major isoform (1409 m/z), composed of 10 carbons in the lipidic chain, was named milkisin C. The three other isoforms detected at 1381 m/z, 1395 m/z and 1423 m/z, that are concomitantly produced, were named milkisin A, B and D, respectively. The structure of milkisin, as confirmed by NMR analyses, is closely related to amphisin family. Indeed, the peptidic chain was composed of 11 amino acids, 6 of which are conserved among the family. In conclusion, Pseudomonas sp. UCMA 17988 produces new members of the amphisin family which are responsible for the antagonistic activity of this strain.
Keywords: Antimicrobial activity, Pseudomonas, milkisin, Amphisin, lipopeptide
Received: 26 Jan 2018;
Accepted: 01 May 2018.
Edited by:Santi M. Mandal, Indian Institute of Technology Kharagpur, India
Reviewed by:Taoufik Ghrairi, Tunis El Manar University, Tunisia
Suresh Korpole, Institute of Microbial Technology (CSIR), India
Copyright: © 2018 Schlusselhuber, Godard, Sebban, Bernay, Garon, Seguin, Oulyadi and Desmasures. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
* Correspondence: PhD. Margot Schlusselhuber, Normandie Université, UNICAEN, UNIROUEN, ABTE, Caen, 14000, France, firstname.lastname@example.org