ArticleACS catalysis2022
Multiple Substrate Binding Mode-Guided Engineering of a Thermophilic PET Hydrolase.
Article in ACS catalysis, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers, 1 of them a synthesis that pooled it.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
79 citing papers in PubMed, 1 synthesis or guideline pooled it, 169 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
- Deep Learning-driven synergistic engineering of PET hydrolase for post-consumer PET depolymerization.Synthetic and systems biotechnology · 2027Article
- Cooperative Amidase Systems Control Product Selectivity During Enzymatic Nylon Depolymerization.Macromolecular bioscience · 2026Article
- Isosteric Engineering of Enzymes: Overcoming Activity-Stability Trade-Offs by Site-Selective CH → N Substitutions.Angewandte Chemie (International ed. in English) · 2026Article
- Bridging the accuracy-speed divide in reactive molecular dynamics with QuantaMind MD.Science advances · 2026Article
- Robust cellular transformations of PET deconstruction products by import of glycol esters.Science advances · 2026Article
- Polyesterase activity and thermostability of carboxylesterases from Thermoleophilum album YS-3.The FEBS journal · 2026Article
- Mechanistic insights into modulation of productive substrate accessibility for efficient PET depolymerization.Nature communications · 2026Article
- Inactivation of PETase at Interfaces Inhibits PET Plastic Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Computational engineering of the polyester hydrolase PHL7 for efficient poly(ethylene terephthalate) degradation in biocatalytic recycling processes.Nature communications · 2026Article
- Directed Evolution of an Efficient Polycarbonate Depolymerase With Exceptional Operational Stability.Angewandte Chemie (International ed. in English) · 2026Article
- Biological Degradation of Phthalates: From Bioremediation to Plastic Waste Valorization.ChemSusChem · 2026Review
- Enzymatic degradation of biopolymers in amorphous and molten states: mechanisms and applications.FEBS open bio · 2026Review
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- EngineeringiScience · 2026Article
- Dynamic shift of internal electric field accelerates enzymatic polyethylene terephthalate depolymerization.Communications chemistry · 2026Article
- RCSB PDB web portal RCSB.org for biotechnology research: exploration and visualization of plastic-degrading enzymes at the atomic level in 3D.Frontiers in bioengineering and biotechnology · 2026Article
- Development of a highly active engineered PETase enzyme for polyester degradation.The FEBS journal · 2026Article
- A Structural Landscape Depiction of Dynamic Stability Centers of Local Structure in Protein Thermostability Engineering.Research (Washington, D.C.) · 2026Article
- Degradation of polyethylene terephthalate by microorganisms and their enzymes: A review of experimental and in silico research.World journal of microbiology & biotechnology · 2025Review
19 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
20 authors at 8 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Thermophilic polyester hydrolases (PES-H) have recently enabled biocatalytic recycling of the mass-produced synthetic polyester polyethylene terephthalate (PET), which has found widespread use in the packaging and textile industries. The growing demand for efficient PET hydrolases prompted us to solve high-resolution crystal structures of two metagenome-derived enzymes (PES-H1 and PES-H2) and notably also in complex with various PET substrate analogues. Structural analyses and computational modeling using molecular dynamics simulations provided an understanding of how product inhibition and multiple substrate binding modes influence key mechanistic steps of enzymatic PET hydrolysis. Key residues involved in substrate-binding and those identified previously as mutational hotspots in homologous enzymes were subjected to mutagenesis. At 72 °C, the L92F/Q94Y variant of PES-H1 exhibited 2.3-fold and 3.4-fold improved hydrolytic activity against amorphous PET films and pretreated real-world PET waste, respectively. The R204C/S250C variant of PES-H1 had a 6.4 °C higher melting temperature than the wild-type enzyme but retained similar hydrolytic activity. Under optimal reaction conditions, the L92F/Q94Y variant of PES-H1 hydrolyzed low-crystallinity PET materials 2.2-fold more efficiently than LCC ICCG, which was previously the most active PET hydrolase reported in the literature. This property makes the L92F/Q94Y variant of PES-H1 a good candidate for future applications in industrial plastic recycling processes.
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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.