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Among these,\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox is a hyperthermostable enzyme isolated from the archaeon\n                    <jats:italic>Sulfolobus solfataricus<\/jats:italic>\n                    . 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.\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox 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,\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox 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\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox-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\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox-W263I activity and could reactivate heat-inactivated enzyme.\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox showed resistance to harsh conditions demonstrating that it is an extremely attractive enzyme for many applications. Finally, the potential of\n                    <jats:italic>Sso<\/jats:italic>\n                    Pox-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.\n                  <\/jats:p>","DOI":"10.1038\/srep37780","type":"journal-article","created":{"date-parts":[[2016,11,23]],"date-time":"2016-11-23T05:18:33Z","timestamp":1479878313000},"update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":55,"title":["Harnessing hyperthermostable lactonase from Sulfolobus solfataricus for biotechnological applications"],"prefix":"10.1038","volume":"6","author":[{"given":"Benjamin","family":"R\u00e9my","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laure","family":"Plener","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Laetitia","family":"Poirier","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Mikael","family":"Elias","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"David","family":"Daud\u00e9","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eric","family":"Chabri\u00e8re","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"297","published-online":{"date-parts":[[2016,11,23]]},"reference":[{"key":"BFsrep37780_CR1","doi-asserted-by":"publisher","first-page":"185","DOI":"10.1038\/nature11117","volume":"485","author":"UT Bornscheuer","year":"2012","unstructured":"Bornscheuer, U. 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