Cell surface properties of Lactococcus lactis reveal milk protein binding specifically evolved in dairy isolates

Mariya Tarazanova, Thom Huppertz, Marke Beerthuyzen, Saskia van Schalkwijk, Patrick W. M. Janssen, Michiel Wels, Jan Kok, Herwig Bachmann

Research output: Contribution to JournalArticleAcademicpeer-review


Surface properties of bacteria are determined by the molecular composition of the cell wall and they are important for interactions of cells with their environment. Well known examples of bacterial interactions with surfaces are biofilm formation and the fermentation of solid materials like food and feed. Lactococcus lactis is broadly used for the fermentation of cheese and buttermilk and it is primarily isolated from either plant material or the dairy environment. In this study, we characterized surface hydrophobicity, charge, emulsification properties and the attachment to milk proteins of 55 L. lactis strains in stationary and exponential growth phases. The attachment to milk protein was assessed through a newly developed flow cytometry-based protocol. Besides finding a high degree of biodiversity, phenotype-genotype matching allowed the identification of candidate genes involved in the modification of the cell surface. Overexpression and gene deletion analysis allowed to verify the predictions for three identified proteins that altered surface hydrophobicity and attachment of milk proteins. The data also showed that lactococci isolated from a dairy environment bind higher amounts of milk proteins when compared to plant isolates. It remains to be determined whether the alteration of surface properties also has potential to alter starter culture functionalities.
Original languageEnglish
Article number1691
JournalFrontiers in Microbiology
Issue numberSEP
Publication statusPublished - 7 Sept 2017


  • Attachment to milk proteins
  • Bacteria-protein interactions
  • Cell surface hydrophobicity
  • Cell wall composition
  • Emulsion stability
  • Gene-trait matching
  • Lactococcus lactis
  • Surface charge


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