ArticleNature communications2022
Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers, 2 of them syntheses that pooled it.
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Who cites it
80 citing papers in PubMed, 2 syntheses or guidelines pooled it.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- Potential routes of plastics biotransformation involving novel plastizymes revealed by global multi-omic analysis of plastic associated microbes.Scientific reports · 2024Pooled it
- Predicting Functional Diversity Within Enzyme Families: A Practical Perspective.Chembiochem : a European journal of chemical biology · 2026Review
- A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation.Applied microbiology and biotechnology · 2026Article
- Molecular bioindicators for assessing environmental impacts of emerging contaminants.Fundamental research · 2026Review
- Structure-Guided Extremophile Genome Mining Expands the PETase Landscape and Reveals PET-Hydrolysing True Lipase Lineages.Microbial biotechnology · 2026Article
- Polyesterase activity and thermostability of carboxylesterases from Thermoleophilum album YS-3.The FEBS journal · 2026Article
- To Biotic or Abiotic: Biohybrid Systems for Artificial Photosynthesis.Chemical reviews · 2026Review
- Reaction Optimization for Enzymatic Deconstruction of Industrially Relevant Nylon Composites.Chembiochem : a European journal of chemical biology · 2026Article
- Challenges and opportunities in the enzymatic recycling of nylons.Nature chemical biology · 2026Review
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Engineering and Application of a Thermostable MHETase for PET Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Amplicon sequence collection of putative polyethylene terephthalate hydrolases from two different composts in Japan.Microbiology resource announcements · 2026Article
- Decoding extremophiles: insights from bioinformatics, machine learning, and data-driven approaches.Briefings in bioinformatics · 2026Review
- Engineering a robust IsPETase for energy-efficient PET depolymerization in natural seawater at ambient temperatures.Advanced biotechnology · 2026Article
- Molecular Dynamics Insights into the Biodegradation of Synthetic Polymers byJournal of chemical information and modeling · 2026Article
- Lignocellulose-mediated selection of potential halophilic PET-degrading enzymes from mangrove soil.Nature communications · 2026Article
- Production and Evaluation of Fluorophore-Doped Polymer Substrates to Screen for Plastic-Degrading Enzymes.ACS sustainable chemistry & engineering · 2026Article
- Structural and oligomeric characterization of substrate- and product-selective nylon hydrolases.bioRxiv : the preprint server for biology · 2026Article
- Reflections on bio-based PET and plastic waste management: a responsible research and innovation approach.Nature communications · 2026Review
20 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
21 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Enzymatic deconstruction of poly(ethylene terephthalate) (PET) is under intense investigation, given the ability of hydrolase enzymes to depolymerize PET to its constituent monomers near the polymer glass transition temperature. To date, reported PET hydrolases have been sourced from a relatively narrow sequence space. Here, we identify additional PET-active biocatalysts from natural diversity by using bioinformatics and machine learning to mine 74 putative thermotolerant PET hydrolases. We successfully express, purify, and assay 51 enzymes from seven distinct phylogenetic groups; observing PET hydrolysis activity on amorphous PET film from 37 enzymes in reactions spanning pH from 4.5-9.0 and temperatures from 30-70 °C. We conduct PET hydrolysis time-course reactions with the best-performing enzymes, where we observe differences in substrate selectivity as function of PET morphology. We employed X-ray crystallography and AlphaFold to examine the enzyme architectures of all 74 candidates, revealing protein folds and accessory domains not previously associated with PET deconstruction. Overall, this study expands the number and diversity of thermotolerant scaffolds for enzymatic PET deconstruction.
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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.