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Bio-guided Purification and Mass Spectrometry Characterisation Exploring the Lysozyme-like Protein from Enterococcus lactis Q1, an Unusual Marine Bacterial Strain

  • Olfa Ben Braïek
  • Slim Smaoui
  • Yannick Fleury
  • Stefano Morandi
  • Khaled Hani
  • Taoufik Ghrairi
Article

Abstract

Lactic acid bacteria produce various antibacterial peptides such as bacteriocins that are active against pathogenic and spoilage microorganisms. Very little attention has been paid to the production of lysozyme as an antimicrobial enzyme. The present work represents one of the few studies reporting lysozyme production by enterococci. Indeed, this study was first conducted to evaluate the antimicrobial activity of Enterococcus lactis Q1, an enterocin P-producing strain previously isolated from fresh shrimp (Penaeus vannamei), against multidrug-resistant clinical isolates. Results showed significant inhibitory activity (P < 0.05) towards diverse pathogens. The purification of the antimicrobial substances produced by Q1 strain leads to the isolation of two active fractions. The SDS-PAGE and mass spectrometry analyses of fraction number 2 (fraction 2) revealed the presence of a protein with molecular mass of 14.3 kDa. Additionally, the experimental results are consistent with mass spectra of industrial lysozyme (Fluka ref. 62970). The lysozyme produced by Enterococcus lactis Q1 strain was confirmed by a plate method against Micrococcus luteus ATCC 4698. Also, sensitivity of the Q1 strain to different concentrations of lysozyme was investigated. For the first time, this study shows that E. lactis Q1 produces lysozyme which could be an excellent candidate in food biopreservation or production of functional foods to promote health benefits.

Keywords

Antimicrobial activity Enterococcus lactis Lysozyme Mass spectrometry RP-HPLC 

Notes

Funding Information

This work was supported by a grant from the Ministry of High Education, Tunisia.

Compliance with Ethical Standards

Conflict of Interest

The authors declare that they have no conflict of interest.

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Copyright information

© Springer Science+Business Media, LLC, part of Springer Nature 2018

Authors and Affiliations

  • Olfa Ben Braïek
    • 1
    • 2
  • Slim Smaoui
    • 3
  • Yannick Fleury
    • 4
  • Stefano Morandi
    • 5
  • Khaled Hani
    • 6
  • Taoufik Ghrairi
    • 1
    • 2
  1. 1.Laboratory of Microorganisms and Active Biomolecules (LMBA), Faculty of Sciences of TunisUniversity of Tunis El-ManarTunisTunisia
  2. 2.Research Laboratory of Environmental Science and Technology (RLEST)ISSTETechnopole de Borj CedriaTunisia
  3. 3.Laboratory of Microorganisms and Biomolecules of the Centre of Biotechnology of SfaxSfaxTunisia
  4. 4.Université de Brest, EA3882, Laboratoire Universitaire de Biodiversité et d’Écologie MicrobienneIUT de QuimperQuimperFrance
  5. 5.Italian National Research Council (CNR ISPA)Institute of Sciences of Food ProductionMilanItaly
  6. 6.Department of Biochemistry, UR12-ES03Faculty of Medicine Ibn El JazzarSousseTunisia

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