(27w) Metabolic Engineered Escherichia coli Strains to Express Flavoprotein Monooxygenases from Actinomycetes Isolated from the Atacama Desert for Industrial Applications.

Flavoprotein monooxygenases (FPMOs) are redox enzymes that catalyze the incorporation of one oxygen atom into a variety of substrates with excellent chemo-, regio-, and enantioselectivity [1]. FPMOs are involved in various biological processes including lignin degradation, enantioselective conversion of ketones to esters or lactones, sulfoxidations, biosynthesis of natural products and detoxification of xenobiotic compounds [2]. Despite the interesting activity of these enzymes, their usually low stability has been a limitation for their industrial application [1]. Therefore, the search and production of new FPMOs with improved stability and attractive substrate and product selectivity are of great interest. The Atacama Desert is a source of microorganisms that grow in extreme environmental conditions and produce many secondary metabolites and enzymes with novel activities. The work we will present include the results of the bioinformatic search and the selection of four putative FMOs in Streptomyces and Micromonospora strains isolated from the Atacama Desert, their heterologous expression and characterization, as well as their potential use in industrial applications.

[1] Romero, E., Gómez Castellanos, J.R., Mattevi, A., Fraaije, M.W. 2016. Characterization and crystal structure of a robust cyclohexanone monooxygenase. Angewandte Chemie International Edition. 55(51): 15852-15855.

[2] Huijbers, M.M., Montersino, S., Westphal, A.H., Tischler, D., van Berkel, W.J.H. 2014. Flavin dependent monooxygenases. Archives of biochemistry and biophysics. 544: 2-17.