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Zhang, Hongli ; Perez-Garcia, Pablo ; Dierkes, Robert F. ; Applegate, Violetta ; Schumacher, Julia ; Chibani, Cynthia Maria ; Sternagel, Stefanie ; Preuss, Lena ; Weigert, Sebastian ; Schmeisser, Christel ; Danso, Dominik ; Pleiss, Juergen ; Almeida, Alexandre ; Höcker, Birte ; Hallam, Steven J. ; Schmitz, Ruth A. ; Smits, Sander H. J. ; Chow, Jennifer ; Streit, Wolfgang R.:
The Bacteroidetes Aequorivita sp. and Kaistella jeonii Produce Promiscuous Esterases With PET-Hydrolyzing Activity.
In: Frontiers in Microbiology.
Bd. 12
(2021)
.
- 803896.
ISSN 1664-302X
DOI: https://doi.org/10.3389/fmicb.2021.803896
Angaben zu Projekten
| Projekttitel: |
Offizieller Projekttitel Projekt-ID MarBiotech 031B0562A MetagenLig 031B0571B MethanoPEP 031B0851B LipoBiocat 031B0837B PlastiSea 031B867B MetagenLig 031B0571A SFB 1357: MIKROPLASTIK – Gesetzmäßigkeiten der Bildung, des Transports, des physikalisch-chemischen Verhaltens sowie der biologischen Effekte: Von Modell- zu komplexen Systemen als Grundlage neuer Lösungsansätze 391977956 Zentrum für strukturelle Studien 417919780 |
|---|---|
| Projektfinanzierung: |
Bundesministerium für Bildung und Forschung Deutsche Forschungsgemeinschaft |
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.