Surface modification using interfacial assembly of the Streptomyces chaplin proteinsEkkers, D. M., Claessen, D., Galli, F. & Stamhuis, E., May-2014, In : Applied Microbiology and Biotechnology. 98, 10, p. 4491-4501 11 p.
Research output: Contribution to journal › Article › Academic › peer-review
The chaplin proteins are instrumental in the formation of reproductive aerial structures by the filamentous bacterium Streptomyces coelicolor. They lower the water surface tension thereby enabling aerial growth. In addition, chaplins provide surface hydrophobicity to the aerial hyphae by assembling on the cell surface into an amphipathic layer of amyloid fibrils. We here show that mixtures of cell wall-extracted chaplins can be used to modify a variety of hydrophilic and hydrophobic surfaces in vitro thereby changing their nature. Assembly on glass leads to a protein coating that makes the surface hydrophobic. Conversely, the assembly of chaplins on hydrophobic surfaces renders them hydrophilic. Furthermore, we show that chaplins can stabilize emulsions of oil into water and have an unprecedented surface activity at high pH. Interestingly, this high surface activity coincides with the interfacial assembly of chaplins into a semi-liquid membrane, as opposed to the rigid membrane formed at neutral pH. This semi-liquid membrane possibly represents a trapped intermediate in the assembly process towards the more rigid amyloidal conformation. Taken together, our data shows that chaplins are suitable candidate proteins for a wide range of biotechnological applications.
|Number of pages||11|
|Journal||Applied Microbiology and Biotechnology|
|Publication status||Published - May-2014|
- Chaplins, Surface modification, Hydrophobins, Surfactant, Functional amyloid, Application, AERIAL MORPHOGENESIS, FUNCTIONAL AMYLOIDS, RODLET LAYER, SP-NOV., HYDROPHOBINS, COELICOLOR, RODLINS, FUNGI, STATE, PH