Harnessing a versatile robust lactonase for biotechnological applications
September 24-28, 2017
Extremozymes have gained considerable interest as they could meet industrial requirements. Among these, SsoPox is a hyperthermostable enzyme isolated from the archaeon Sulfolobus solfataricus1. This enzyme is a lactonase catalyzing the hydrolysis of acyl-homoserine lactones; these molecules are involved in Gram-negative bacterial communication referred to as quorum sensing2. SsoPox exhibits promiscuous phosphotriesterase activity for the degradation of organophosphorous chemicals including insecticides and chemical warfare agents3. Owing to its bi-functional catalytic abilities as well as its intrinsic stability, SsoPox is appealing for many applications, having potential uses in the agriculture, defense, food and health industries. This enzyme have been rationally engineered and highly improved lactonase and phosphotriesterase variants were isolated4. Their biotechnological properties were investigated and their resistance against diverse process-like and operating conditions such as heat resistance, contact with organic solvents, sterilization, storage and immobilization were underlined5.
Lactonase improved variants were shown to drastically reduce virulence and biofilm formation in clinical isolates of Pseudomonas aeruginosa and to decrease mortality in rat pneumonia model6,7. The antibiofilm capacity of the enzyme was also proved to be of outmost interest for antifouling applications.
Enhanced phosphotriesterase variants were shown to efficiently decontaminate a broad panel of organophosphorus insecticides and were successfully incorporated into filtration devices for bioremediation purposes8. The degradation products generated through enzyme hydrolysis drastically reduced toxicity and increased regeneration capacity in planarian, an original Plathelmintes model.
Regarding their tremendous stability these variants are currently used to develop antibacterial medical devices, antifouling paintings and insecticide bioremediation tools.
1. Elias, M. et al. Structural Basis for Natural Lactonase and Promiscuous Phosphotriesterase Activities. J. Mol. Biol. 379, 1017–1028 (2008).
2. Bzdrenga, J. et al. Biotechnological applications of quorum quenching enzymes. Chem. Biol. Interact. (2016). doi:10.1016/j.cbi.2016.05.028
3. Jacquet, P. et al. Current and emerging strategies for organophosphate decontamination: special focus on hyperstable enzymes. Environ. Sci. Pollut. Res. 1–19 (2016). doi:10.1007/s11356-016-6143-1
4. Hiblot, J., Gotthard, G., Elias, M. & Chabriere, E. Differential Active Site Loop Conformations Mediate Promiscuous Activities in the Lactonase SsoPox. PLoS ONE 8, e75272 (2013).
5. Rémy, B. et al. Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications. Sci. Rep. 6, (2016).
6. Guendouze, A. et al. Effect of quorum quenching lactonase in clinical isolates of Pseudomonas aeruginosa and comparison with quorum sensing inhibitors. Front. Microbiol. 8, (2017).
7. Hraiech, S. et al. Inhaled Lactonase Reduces Pseudomonas aeruginosa Quorum Sensing and Mortality in Rat Pneumonia. PLoS ONE 9, e107125 (2014).
8. Hiblot, J., Gotthard, G., Chabriere, E. & Elias, M. Characterisation of the organophosphate hydrolase catalytic activity of SsoPox. Sci. Rep. 2, (2012).
David Daudé, Pauline Jacquet, Benjamin Rémy, Laetitia Poirier, Laure Plener, Mikael Elias, and Eric Chabrière, "Harnessing a versatile robust lactonase for biotechnological applications" in "Enzyme Engineering XXIV", Pierre Monsan, Toulouse White Biotechnology, France Magali Remaud-Simeon, LISBP-INSA, University of Toulouse, France Eds, ECI Symposium Series, (2017). http://dc.engconfintl.org/enzyme_xxiv/123