Effect of proteases on biofilm formation of the plastic-degrading actinomycete Rhodococcus ruber C208

Irit Gilan, Alex Sivan

Research output: Contribution to journalArticlepeer-review

44 Scopus citations


In most habitats, the vast majority of microbial populations form biofilms on solid surfaces, whether natural or artificial. These biofilms provide either increased physical support and/or a source of nutrients. Further modifications and development of biofilms are regulated by signal molecules secreted by the cells. Because synthetic polymers are not soluble in aqueous solutions, biofilm-producing bacteria may biodegrade such materials more efficiently than planktonic strains. Bacterial biofilms comprise bacterial cells embedded in self-secreted extracellular polymeric substances (EPS). Revealing the roles of each component of the EPS will enable further insight into biofilm development and the EPS structure-function relationship. A strain of Rhodococcus ruber (C208) displayed high hydrophobicity and formed a dense biofilm on the surface of polyethylene films while utilizing the polyolefin as carbon and energy sources. This study investigated the effects of several proteases on C208 biofilm formation and stability. The proteolysis of C208 biofilm gave conflicting results. Trypsin significantly reduced biofilm formation, and the resultant biofilm appeared monolayered. In contrast, proteinase K enhanced biofilm formation, which was robust and multilayered. Presumably, proteinase K degraded self-secreted proteases or quorum-sensing peptides, which may be involved in biofilm detachment processes, leading to a multilayered, nondispersed biofilm.

Original languageEnglish
Pages (from-to)18-23
Number of pages6
JournalFEMS Microbiology Letters
Issue number1
StatePublished - 1 May 2013


  • Biofilm detachment
  • Microbial adhesion
  • Proteinase K
  • Rhodococcus ruber
  • Trypsin

ASJC Scopus subject areas

  • Microbiology
  • Molecular Biology
  • Genetics


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