ArticleCommunications chemistry2023
An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate.
Article in Communications chemistry, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers, 1 of them a synthesis that pooled it.
What it found
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The trial behind it
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Who cites it
33 citing papers in PubMed, 1 synthesis or guideline pooled it, 59 citations in OpenAlex.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation.Applied microbiology and biotechnology · 2026Article
- Archaea-driven bioremediation of polyolefins and polyesters in extreme environments.Biodesign research · 2026Review
- Acinetobacter guillouiae, a lipolytic strain isolated from sludge capable of partially depolymerising polyethylene terephthalate: genomic, proteomic, and biochemical insights.BMC microbiology · 2026Article
- Experimental, Genomic, and Structural Evidence Supporting Putative PET-Hydrolases in Thermophilic Bacteria Isolated From Hot Springs in Cajamarca, Peru.MicrobiologyOpen · 2026Article
- Polyesterase activity and thermostability of carboxylesterases from Thermoleophilum album YS-3.The FEBS journal · 2026Article
- Engineering and Application of a Thermostable MHETase for PET Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Lignocellulose-mediated selection of potential halophilic PET-degrading enzymes from mangrove soil.Nature communications · 2026Article
- Unveiling a catalytically promiscuous feruloyl esterase from Clostridium acetobutylicum.Applied microbiology and biotechnology · 2026Article
- Discovering PETases: An Interlink Between Engineering Enzymes and Microbiomes.Environmental microbiology · 2026Review
- Cold-adapted carboxylesterases from Alcanivoracaceae active with a wide range of synthetic polyesters.Applied microbiology and biotechnology · 2026Article
- Gut microbial signatures in schizophrenia: exploring archaea, fungi, and bacteria.BMC psychiatry · 2026Article
- Identification and characterization of R75estA, a halophilic polyester-degrading enzyme from a marine bacterium.Frontiers in microbiology · 2026Article
- Microbial plastic degradation: enzymes, pathways, challenges, and perspectives.Microbiology and molecular biology reviews : MMBR · 2025Review
- Plastic Type and Condition Have Minimal Impact on Associated Marine Biofilm Communities.Environmental microbiology · 2025Article
- Degradation of polyethylene terephthalate by microorganisms and their enzymes: A review of experimental and in silico research.World journal of microbiology & biotechnology · 2025Review
- A third type of PETase from the marine Halopseudomonas lineage.Protein science : a publication of the Protein Society · 2025Article
- Genomic and transcriptomic characterization of carbohydrate-active enzymes in the anaerobic fungus Neocallimastix cameroonii var. constans.G3 (Bethesda, Md.) · 2025Article
- Degradation of Synthetic Restoration Materials by Xerotolerant/Xerophilic Fungi Contaminating Canvas Paintings.Journal of fungi (Basel, Switzerland) · 2025Article
- Standardization guidelines and future trends for PET hydrolase research.Nature communications · 2025Review
Corrections and comments
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Authors and funding
19 authors at 4 institutions in 1 country.
Funding
Abstract
Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 80 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme had been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46 (RLI42440.1), an archaeal promiscuous feruloyl esterase exhibiting degradation activity on semi-crystalline PET powder comparable to IsPETase and LCC (wildtypes), and higher activity on bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, is 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 widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a plant cell wall-degrading esterase.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.