Titlebar

Export bibliographic data
Literature by the same author
plus on the publication server
plus at Google Scholar

 

The Bacteroidetes Aequorivita sp. and Kaistella jeonii Produce Promiscuous Esterases With PET-Hydrolyzing Activity

Title data

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. Vol. 12 (5 January 2022) .
ISSN 1664-302X
DOI: https://doi.org/10.3389/fmicb.2021.803896

Project information

Project title:
Project's official titleProject's id
SFB 1357 Mikroplastik391977956
MarBiotech031B0562A
MetagenLig031B0571B
MethanoPEP031B0851B
LipoBiocat031B0837B
PlastiSea031B867B
MetagenLig031B0571A
The Center for Structural Studies was funded by the Deutsche Forschungsgemeinschaft (DFG Grant number 417919780; INST 208/740-1 FUGG; INST 208/761-1 FUGG)No information

Project financing: Bundesministerium für Bildung und Forschung
Deutsche Forschungsgemeinschaft
Further funding came from the US Department of Energy (DOE) Joint Genome Institute, an Office of Science User Facility, supported by the Office of Science of the U.S. Department of Energy under Contract DE-AC02-05CH11231, the Natural Sciences and Engineering Research Council (NSERC) of Canada, the G. Unger Vetlesen and Ambrose Monell Foundations, the Canada Foundation for Innovation (CFI) and Compute Canada through grants awarded to SH. AA was funded by EMBL core funds.

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Birte Höcker
Research Institutions > Collaborative Research Centers, Research Unit > SFB 1357 - MIKROPLASTIK
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 500 Natural sciences
500 Science > 570 Life sciences, biology
500 Science > 590 Animals (Zoology)
Date Deposited: 17 Jan 2022 09:23
Last Modified: 17 Jan 2022 09:23
URI: https://eref.uni-bayreuth.de/id/eprint/68369