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2014-02-26 - Article/Dans un journal avec peer-review - Anglais - 16 page(s)

Ciesielska Katarzyna, Van Bogaert Inge, Chevineau Samia , Li Bing, Groeneboer Sara, Soetaert Wim, van de peer yves, devreese bart, "Exoproteome analysis of Starmerella bombicola results in the discovery of an esterase required for lactonization of sophorolipids." in Journal of Proteomics

  • Edition : Elsevier (Netherlands)
  • Codes CREF : Biochimie (DI3112)
Texte intégral :

Abstract(s) :

(Anglais) The yeast Starmerella bombicola secretes sophorolipids, a family of biosurfactants that find applications in green household products and cosmetics. Over the past years, a gene cluster was discovered that is responsible for the entire synthesis of the open (acidic) form of these molecules from glucose, fatty acids and acetyl-CoA building blocks. However, a significant fraction of the natural product is obtained as a ring closed form (lactonic). Both genetic and proteomic approaches hitherto failed to discover an enzyme responsible for the esterification reaction required for the ring closure step. We hypothesized that this enzyme is extracellularly secreted. Therefore, we characterized the composition of the S. bombicola exoproteome at different time points of the growth and compared it with known yeast exoproteomes. We identified 44 proteins, many of them commonly found in other fungi. Curiously, we discovered an enzyme with homology to Pseudozyma antarctica lipase A. A deletion mutation of its gene resulted in complete abolishment of the sophorolipid lactonization providing evidence that this might be the missing enzyme in the sophorolipid biosynthetic pathway.