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

Authors
  • Zhang, Hongli1
  • Perez-Garcia, Pablo1, 2
  • Dierkes, Robert F.1
  • Applegate, Violetta3
  • Schumacher, Julia3
  • Chibani, Cynthia Maria2
  • Sternagel, Stefanie4
  • Preuss, Lena1
  • Weigert, Sebastian5
  • Schmeisser, Christel1
  • Danso, Dominik1
  • Pleiss, Juergen6
  • Almeida, Alexandre7, 8
  • Höcker, Birte5
  • Hallam, Steven J.4, 9, 10, 11, 12
  • Schmitz, Ruth A.2
  • Smits, Sander H. J.3, 13
  • Chow, Jennifer1
  • Streit, Wolfgang R.1
  • 1 Department of Microbiology and Biotechnology, University of Hamburg, Hamburg , (Germany)
  • 2 Molecular Microbiology, Institute for General Microbiology, Kiel University, Kiel , (Germany)
  • 3 Center for Structural Studies, Heinrich-Heine-University, Düsseldorf , (Germany)
  • 4 Department of Microbiology and Immunology, University of British Columbia, Vancouver, BC , (Canada)
  • 5 Department of Biochemistry, University of Bayreuth, Bayreuth , (Germany)
  • 6 Institute of Biochemistry and Technical Biochemistry, University of Stuttgart, Stuttgart , (Germany)
  • 7 European Bioinformatics Institute (EMBL-EBI), Hinxton , (United Kingdom)
  • 8 Wellcome Sanger Institute, Hinxton , (United Kingdom)
  • 9 Graduate Program in Bioinformatics, University of British Columbia, Vancouver, BC , (Canada)
  • 10 Genome Science and Technology Program, University of British Columbia, Vancouver, BC , (Canada)
  • 11 Life Sciences Institute, University of British Columbia, Vancouver, BC , (Canada)
  • 12 ECOSCOPE Training Program, University of British Columbia, Vancouver, BC , (Canada)
  • 13 Institute of Biochemistry, Heinrich-Heine-University, Düsseldorf , (Germany)
Type
Published Article
Journal
Frontiers in Microbiology
Publisher
Frontiers Media SA
Publication Date
Jan 05, 2022
Volume
12
Identifiers
DOI: 10.3389/fmicb.2021.803896
Source
Frontiers
Keywords
Disciplines
  • Microbiology
  • Original Research
License
Green

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.

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