title: Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications.
abstract: Extremozymes have gained considerable interest as they could meet industrial requirements. Among these, SsoPox is a hyperthermostable enzyme isolated from the archaeon Sulfolobus solfataricus. 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 sensing. SsoPox exhibits promiscuous phosphotriesterase activity for the degradation of organophosphorous chemicals including insecticides and chemical warfare agents. 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. Here we investigate the biotechnological properties of the mutant SsoPox-W263I, a variant with increased lactonase and phosphotriesterase activities. We tested enzyme resistance against diverse process-like and operating conditions such as heat resistance, contact with organic solvents, sterilization, storage and immobilization. Bacterial secreted materials from both Gram-negative and positive bacteria were harmless on SsoPox-W263I activity and could reactivate heat-inactivated enzyme. SsoPox showed resistance to harsh conditions demonstrating that it is an extremely attractive enzyme for many applications. Finally, the potential of SsoPox-W263I to be active at subzero temperature is highlighted and discussed in regards to the common idea that hyperthermophile enzymes are nearly inactive at low temperatures.
authors.affiliation: Aix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.|Gene&GreenTK, Faculté de Médecine, 27 boulevard Jean Moulin, 13385 Marseille Cedex 5, France.
authors.forename: Benjamin
authors.initials: B
authors.lastname: Rémy
authors.affiliation: Gene&GreenTK, Faculté de Médecine, 27 boulevard Jean Moulin, 13385 Marseille Cedex 5, France.
authors.forename: Laure
authors.initials: L
authors.lastname: Plener
authors.affiliation: Aix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.
authors.forename: Laetitia
authors.initials: L
authors.lastname: Poirier
authors.affiliation: University of Minnesota, Department of Biochemistry, Molecular Biology and Biophysics &Biotechnology Institute, St. Paul, MN 55108, USA.
authors.forename: Mikael
authors.initials: M
authors.lastname: Elias
authors.affiliation: Gene&GreenTK, Faculté de Médecine, 27 boulevard Jean Moulin, 13385 Marseille Cedex 5, France.
authors.forename: David
authors.initials: D
authors.lastname: Daudé
authors.affiliation: Aix Marseille Univ, INSERM, CNRS, IRD, URMITE, Marseille, France.
authors.forename: Eric
authors.initials: E
authors.lastname: Chabrière
mesh_terms: D000464:Alginates / Q000737:chemistry; D055162:Biocatalysis / Q000187:drug effects; D001709:Biotechnology / Q000379:methods*; D002265:Carboxylic Ester Hydrolases / Q000378:metabolism*; D003432:Cross-Linking Reagents / Q000737:chemistry; D004795:Enzyme Stability / Q000187:drug effects; D020723:Glucuronic Acid / Q000737:chemistry; D018869:Heat-Shock Response / Q000187:drug effects; D006603:Hexuronic Acids / Q000737:chemistry; D055767:Immobilized Proteins / Q000378:metabolism; D010261:Paraoxon / Q000633:toxicity; D012997:Solvents; D013242:Sterilization; D013312:Stress, Physiological / Q000187:drug effects; D048229:Sulfolobus solfataricus / Q000201:enzymology*; D013696:Temperature
chemical_list: D000464:Alginates; D003432:Cross-Linking Reagents; D006603:Hexuronic Acids; D055767:Immobilized Proteins; D012997:Solvents; D020723:Glucuronic Acid; D002265:Carboxylic Ester Hydrolases; C020579:gluconolactonase; D010261:Paraoxon