Applied Microbiology and Biotechnology

, Volume 97, Issue 24, pp 10321–10328 | Cite as

Nisin-activated hydrophobic and hydrophilic surfaces: assessment of peptide adsorption and antibacterial activity against some food pathogens

  • Layal Karam
  • Charafeddine Jama
  • Anne-Sophie Mamede
  • Samir Boukla
  • Pascal Dhulster
  • Nour-Eddine Chihib
Biotechnological products and process engineering


An effective antimicrobial packaging or food contact surface should be able to kill or inhibit micro-organisms that cause food-borne illnesses. Setting up such systems, by nisin adsorption on hydrophilic and hydrophobic surfaces, is still a matter of debate. For this purpose, nisin was adsorbed on two types of low-density polyethylene: the hydrophobic native film and the hydrophilic acrylic acid-treated surface. The antibacterial activity was compared for those two films and it was highly dependent on the nature of the surface and the nisin-adsorbed amount. The hydrophilic surfaces presented higher antibacterial activity and higher amount of nisin than the hydrophobic surfaces. The effectiveness of the activated surfaces was assessed against Listeria innocua and the food pathogens Listeria monocytogenes, Bacillus cereus, and Staphylococcus aureus. S. aureus was more sensitive than the three other test bacteria toward both nisin-functionalized films. Simulation tests to mimic refrigerated temperature showed that the films were effective at 20 and 4 °C with no significant difference between the two temperatures after 30 min of exposure to culture media.


Antibacterial activity Nisin adsorption Listeria Bacillus Staphylococcus Hydrophilic surface 

Supplementary material

253_2013_5259_MOESM1_ESM.pdf (236 kb)
ESM 1(PDF 236 kb)


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Copyright information

© Springer-Verlag Berlin Heidelberg 2013

Authors and Affiliations

  • Layal Karam
    • 1
    • 2
  • Charafeddine Jama
    • 2
  • Anne-Sophie Mamede
    • 3
  • Samir Boukla
    • 1
  • Pascal Dhulster
    • 1
  • Nour-Eddine Chihib
    • 1
  1. 1.Laboratoire ProBioGEM, Polytech’LilleVilleneuve d’AscqFrance
  2. 2.Laboratoire UMET, UMR-CNRS 8207, Ecole Nationale Supérieure de Chimie de LilleVilleneuve d’AscqFrance
  3. 3.Unité de Catalyse et de Chimie du Solide, UMR-CNRS 8181, Ecole Nationale Supérieure de Chimie de LilleVilleneuve d’AscqFrance

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