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http://dx.doi.org/10.18419/opus-14074
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DC Element | Wert | Sprache |
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dc.contributor.author | Zhang, Hongli | - |
dc.contributor.author | Perez-Garcia, Pablo | - |
dc.contributor.author | Dierkes, Robert F. | - |
dc.contributor.author | Applegate, Violetta | - |
dc.contributor.author | Schumacher, Julia | - |
dc.contributor.author | Chibani, Cynthia Maria | - |
dc.contributor.author | Sternagel, Stefanie | - |
dc.contributor.author | Preuss, Lena | - |
dc.contributor.author | Weigert, Sebastian | - |
dc.contributor.author | Schmeisser, Christel | - |
dc.contributor.author | Danso, Dominik | - |
dc.contributor.author | Pleiss, Juergen | - |
dc.contributor.author | Almeida, Alexandre | - |
dc.contributor.author | Höcker, Birte | - |
dc.contributor.author | Hallam, Steven J. | - |
dc.contributor.author | Schmitz, Ruth A. | - |
dc.contributor.author | Smits, Sander H. J. | - |
dc.contributor.author | Chow, Jennifer | - |
dc.contributor.author | Streit, Wolfgang R. | - |
dc.date.accessioned | 2024-03-15T13:03:37Z | - |
dc.date.available | 2024-03-15T13:03:37Z | - |
dc.date.issued | 2022 | de |
dc.identifier.issn | 1664-302X | - |
dc.identifier.other | 188377909X | - |
dc.identifier.uri | http://nbn-resolving.de/urn:nbn:de:bsz:93-opus-ds-140935 | de |
dc.identifier.uri | http://elib.uni-stuttgart.de/handle/11682/14093 | - |
dc.identifier.uri | http://dx.doi.org/10.18419/opus-14074 | - |
dc.description.abstract | Certain members of the Actinobacteria and Proteobacteria are known to degrade polyethylene terephthalate (PET). Here, we describe the first functional PET-active enzymes from the Bacteroidetes phylum. Using a PETase-specific Hidden-Markov-Model- (HMM-) based search algorithm, we identified several PETase candidates from Flavobacteriaceae and Porphyromonadaceae. Among them, two promiscuous and cold-active esterases derived from Aequorivita sp. (PET27) and Kaistella jeonii (PET30) showed depolymerizing activity on polycaprolactone (PCL), amorphous PET foil and on the polyester polyurethane Impranil® DLN. PET27 is a 37.8 kDa enzyme that released an average of 174.4 nmol terephthalic acid (TPA) after 120 h at 30°C from a 7 mg PET foil platelet in a 200 μl reaction volume, 38-times more than PET30 (37.4 kDa) released under the same conditions. The crystal structure of PET30 without its C-terminal Por-domain (PET30ΔPorC) was solved at 2.1 Å and displays high structural similarity to the IsPETase. PET30 shows a Phe-Met-Tyr substrate binding motif, which seems to be a unique feature, as IsPETase, LCC and PET2 all contain Tyr-Met-Trp binding residues, while PET27 possesses a Phe-Met-Trp motif that is identical to Cut190. Microscopic analyses showed that K. jeonii cells are indeed able to bind on and colonize PET surfaces after a few days of incubation. Homologs of PET27 and PET30 were detected in metagenomes, predominantly aquatic habitats, encompassing a wide range of different global climate zones and suggesting a hitherto unknown influence of this bacterial phylum on man-made polymer degradation. | en |
dc.description.sponsorship | BMBF | de |
dc.description.sponsorship | Deutsche Forschungsgemeinschaft | de |
dc.description.sponsorship | US Department of Energy (DOE) Joint Genome Institute | de |
dc.language.iso | en | de |
dc.relation.uri | doi:10.3389/fmicb.2021.803896 | de |
dc.rights | info:eu-repo/semantics/openAccess | de |
dc.rights.uri | https://creativecommons.org/licenses/by/4.0/ | de |
dc.subject.ddc | 540 | de |
dc.subject.ddc | 570 | de |
dc.title | The Bacteroidetes Aequorivita sp. and Kaistella jeonii produce promiscuous esterases with PET-hydrolyzing activity | en |
dc.type | article | de |
dc.date.updated | 2023-11-14T03:02:41Z | - |
ubs.fakultaet | Chemie | de |
ubs.fakultaet | Fakultätsübergreifend / Sonstige Einrichtung | de |
ubs.institut | Institut für Biochemie und Technische Biochemie | de |
ubs.institut | Fakultätsübergreifend / Sonstige Einrichtung | de |
ubs.publikation.seiten | 15 | de |
ubs.publikation.source | Frontiers in microbiology 12 (2022), No. 803896 | de |
ubs.publikation.typ | Zeitschriftenartikel | de |
Enthalten in den Sammlungen: | 03 Fakultät Chemie |
Dateien zu dieser Ressource:
Datei | Beschreibung | Größe | Format | |
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Data_Sheet_1.PDF | Supplement | 238,34 kB | Adobe PDF | Öffnen/Anzeigen |
fmicb-12-803896.pdf | Artikel | 3,46 MB | Adobe PDF | Öffnen/Anzeigen |
Image_1.JPEG | Supplementary Figure 1 | 338,34 kB | JPEG | Öffnen/Anzeigen |
Image_2.JPEG | Supplementary Figure 2 | 105,7 kB | JPEG | Öffnen/Anzeigen |
Image_3.JPEG | Supplementary Figure 3 | 798,54 kB | JPEG | Öffnen/Anzeigen |
Image_4.JPEG | Supplementary Figure 4 | 1,31 MB | JPEG | Öffnen/Anzeigen |
Image_5.JPEG | Supplementary Figure 5 | 407,9 kB | JPEG | Öffnen/Anzeigen |
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