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PreprintCited by 79Enzyme Production and CharacterizationEnzyme Catalysis and ImmobilizationEnzyme-mediated dye degradation

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The first archaeal PET-degrading enzyme belongs to the feruloyl-esterase family

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Perez-Garcia, Pablo, Chow, Jennifer, Costanzi, Elisa, Gurschke, Marno F., Dittrich, Jonas, Dierkes, Robert F., Applegate, Violetta, Feuerriegel, Golo, Tete, Prince, Danso, Dominik, Schumacher, Julia, Pfleger, Christopher, Gohlke, Holger, Smits, Sander H. J., Schmitz, Ruth A., Streit, Wolfgang R.·2022·Communications Chemistry
DOI 10.1101/2022.10.14.512230PMC PMC10495362

Preprint — published as 10.1038/s42004-023-00998-z

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Abstract

Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 40 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme has been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46, an archaeal promiscuous feruloyl esterase exhibiting degradation activitiy on PET, bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, was derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 Å. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study significantly widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a lignin-degrading esterase.

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Metadata

Authors
Perez-Garcia, P., Chow, J., Costanzi, E., Gurschke, M. F., Dittrich, J., Dierkes, R. F., Applegate, V., Feuerriegel, G., Tete, P., Danso, D., Schumacher, J., Pfleger, C., Gohlke, H., Smits, S. H. J., Schmitz, R. A., & Streit, W. R.
Affiliations
  • Universität Hamburg (DE)
  • Heinrich Heine University Düsseldorf (DE)
  • Forschungszentrum Jülich (DE)
  • Christian-Albrechts-Universität zu Kiel (DE)
Corresponding author
  • Schmitz, Ruth A.
  • Streit, Wolfgang R.
ORCID
Venue
Communications Chemistry
Publisher
openRxiv
Published
2022-10-14
Volume
6
Issue
1
Pages
193-193
ISSN
2399-3669 (ISSN-L)
DOI
10.1101/2022.10.14.512230
PMC
PMC10495362
OpenAlex
W4386608256
Cited by
79
References
1
Citations by year
2026: 25 · 2025: 26 · 2024: 23 · 2023: 4
FWCI
10.11
Type
journal article
Language
en
Open access
Licence
cc-by
Locations
  • Communications Chemistry (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion)
  • Research Square (acceptedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • JuSER Publikationsportal
Funders
  • European Commission (HORIZON2020, 101000327)
  • Deutsche Forschungsgemeinschaft (INST 208/740-1, INST 208/740‐1 FUGG, 417919780)
  • European Synchrotron Radiation Facility (ID23‐1)
  • Bundesministerium für Bildung und Forschung (031B0837B, 417919780, 031B0562A, 031B0571B, 031B0571A, 031B867B, 031B0837A, 031B867F)
  • Heinrich-Heine-Universität Düsseldorf
  • Universität Hamburg
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Enzyme Catalysis and Immobilization
  • Life Sciences › Immunology and Microbiology › Applied Microbiology and Biotechnology › Enzyme-mediated dye degradation
Keywords
polyethylene terephthalate degradation, feruloyl esterase, archaeal enzyme, alpha/beta hydrolase fold, PET depolymerization, bis(2-hydroxyethyl) terephthalate, deep-sea archaea, plastic pollution, enzyme crystal structure, substrate binding

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