{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,19]],"date-time":"2026-09-19T09:29:11Z","timestamp":1789810151724,"version":"4.0.1"},"reference-count":60,"publisher":"American Society for Microbiology","issue":"20","license":[{"start":{"date-parts":[[2016,10,15]],"date-time":"2016-10-15T00:00:00Z","timestamp":1476489600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/journals.asm.org\/non-commercial-tdm-license"}],"funder":[{"DOI":"10.13039\/100000181","name":"DOD | AF | Air Force Office of Scientific Research","doi-asserted-by":"publisher","award":["12RX14COR"],"award-info":[{"award-number":["12RX14COR"]}],"id":[{"id":"10.13039\/100000181","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["journals.asm.org"],"crossmark-restriction":true},"short-container-title":["Appl Environ Microbiol"],"published-print":{"date-parts":[[2016,10,15]]},"abstract":"<jats:title>ABSTRACT<\/jats:title>\n          <jats:p>\n            Polyester polyurethane (PU) coatings are widely used to help protect underlying structural surfaces but are susceptible to biological degradation. PUs are susceptible to degradation by\n            <jats:named-content content-type=\"genus-species\">Pseudomonas<\/jats:named-content>\n            species, due in part to the degradative activity of secreted hydrolytic enzymes. Microorganisms often respond to environmental cues by secreting enzymes or secondary metabolites to benefit their survival. This study investigated the impact of exposing several\n            <jats:named-content content-type=\"genus-species\">Pseudomonas<\/jats:named-content>\n            strains to select carbon sources on the degradation of the colloidal polyester polyurethane Impranil DLN (Impranil). The prototypic\n            <jats:named-content content-type=\"genus-species\">Pseudomonas protegens<\/jats:named-content>\n            strain Pf-5 exhibited Impranil-degrading activities when grown in sodium citrate but not in glucose-containing medium. Glucose also inhibited the induction of Impranil-degrading activity by citrate-fed Pf-5 in a dose-dependent manner. Biochemical and mutational analyses identified two extracellular lipases present in the Pf-5 culture supernatant (PueA and PueB) that were involved in degradation of Impranil. Deletion of the\n            <jats:italic>pueA<\/jats:italic>\n            gene reduced Impranil-clearing activities, while\n            <jats:italic>pueB<\/jats:italic>\n            deletion exhibited little effect. Removal of both genes was necessary to stop degradation of the polyurethane. Bioinformatic analysis showed that putative Cbr\/Hfq\/Crc-mediated regulatory elements were present in the intergenic sequences upstream of both\n            <jats:italic>pueA<\/jats:italic>\n            and\n            <jats:italic>pueB<\/jats:italic>\n            genes. Our results confirmed that both PueA and PueB extracellular enzymes act in concert to degrade Impranil. Furthermore, our data showed that carbon sources in the growth medium directly affected the levels of Impranil-degrading activity but that carbon source effects varied among\n            <jats:named-content content-type=\"genus-species\">Pseudomonas<\/jats:named-content>\n            strains. This study uncovered an intricate and complicated regulation of\n            <jats:named-content content-type=\"genus-species\">P. protegens<\/jats:named-content>\n            PU degradation activity controlled by carbon catabolite repression.\n          <\/jats:p>\n          <jats:p>\n            <jats:bold>IMPORTANCE<\/jats:bold>\n            Polyurethane (PU) coatings are commonly used to protect metals from corrosion. Microbiologically induced PU degradation might pose a substantial problem for the integrity of these coatings. Microorganisms from diverse genera, including pseudomonads, possess the ability to degrade PUs via various means. This work identified two extracellular lipases, PueA and PueB, secreted by\n            <jats:named-content content-type=\"genus-species\">P. protegens<\/jats:named-content>\n            strain Pf-5, to be responsible for the degradation of a colloidal polyester PU, Impranil. This study also revealed that the expression of the degradative activity by strain Pf-5 is controlled by glucose carbon catabolite repression. Furthermore, this study showed that the Impranil-degrading activity of many other\n            <jats:named-content content-type=\"genus-species\">Pseudomonas<\/jats:named-content>\n            strains could be influenced by different carbon sources. This work shed light on the carbon source regulation of PU degradation activity among pseudomonads and identified the polyurethane lipases in\n            <jats:named-content content-type=\"genus-species\">P. protegens<\/jats:named-content>\n            .\n          <\/jats:p>","DOI":"10.1128\/aem.01448-16","type":"journal-article","created":{"date-parts":[[2016,8,6]],"date-time":"2016-08-06T02:48:40Z","timestamp":1470451720000},"page":"6080-6090","update-policy":"https:\/\/doi.org\/10.1128\/asmj-crossmark-policy-page","source":"Crossref","is-referenced-by-count":110,"title":["Carbon Catabolite Repression and Impranil Polyurethane Degradation in Pseudomonas protegens Strain Pf-5"],"prefix":"10.1128","volume":"82","author":[{"given":"Chia-Suei","family":"Hung","sequence":"first","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"},{"name":"UES, Inc., Dayton, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sandra","family":"Zingarelli","sequence":"additional","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"},{"name":"UES, Inc., Dayton, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lloyd J.","family":"Nadeau","sequence":"additional","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Justin C.","family":"Biffinger","sequence":"additional","affiliation":[{"name":"Chemistry Division, U.S. Naval Research Laboratory, Washington, DC, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Carrie A.","family":"Drake","sequence":"additional","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"},{"name":"UES, Inc., Dayton, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Audra L.","family":"Crouch","sequence":"additional","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"},{"name":"UES, Inc., Dayton, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Daniel E.","family":"Barlow","sequence":"additional","affiliation":[{"name":"Chemistry Division, U.S. Naval Research Laboratory, Washington, DC, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"suffix":"Jr.","given":"John N.","family":"Russell","sequence":"additional","affiliation":[{"name":"Chemistry Division, U.S. Naval Research Laboratory, Washington, DC, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Wendy J.","family":"Crookes-Goodson","sequence":"additional","affiliation":[{"name":"Soft Matter Materials Branch, Materials and Manufacturing Directorate, Air Force Research Laboratory, Wright-Patterson Air Force Base, Ohio, USA"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"235","reference":[{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.biotechadv.2013.08.011"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1007\/978-3-642-23789-8_14"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.02536-13"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0964-8305(98)00051-1"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0964-8305(01)00042-7"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1016\/0265-3036(91)90012-G"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1007\/s11356-014-2647-8"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.ibiod.2013.05.019"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1111\/j.1574-6968.2000.tb09056.x"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0922-338X(99)89001-1"},{"key":"e_1_3_3_12_2","doi-asserted-by":"publisher","DOI":"10.1016\/S0964-8305(99)00074-8"},{"key":"e_1_3_3_13_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.soilbio.2004.09.014"},{"key":"e_1_3_3_14_2","doi-asserted-by":"publisher","DOI":"10.1128\/AEM.00097-07"},{"key":"e_1_3_3_15_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.soilbio.2012.11.009"},{"key":"e_1_3_3_16_2","doi-asserted-by":"crossref","first-page":"3","DOI":"10.1007\/978-1-61779-600-5_1","volume-title":"Lipases and phospholipases","author":"Casas-Godoy L","year":"2012","unstructured":"Casas-Godoy L, Duquesne S, Bordes F, Sandoval G, Marty A. 2012. 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