ArticleCommunications biology2023
Computational design of highly efficient thermostable MHET hydrolases and dual enzyme system for PET recycling.
Article in Communications biology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers, 2 of them syntheses that pooled it.
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Who cites it
28 citing papers in PubMed, 2 syntheses or guidelines pooled it, 53 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
- Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review.International journal of molecular sciences · 2025Pooled it
- A versatile Bacillus esterase reveals a carboxylesterase blueprint for PET intermediate degradation.Applied microbiology and biotechnology · 2026Article
- Enhancing Enzyme Activity With Mutation Combinations Guided by Few-Shot Learning and Causal Inference.Angewandte Chemie (International ed. in English) · 2026Article
- Marine bacteria and fungi: the hidden treasure of oceans in the biodegradation of microplastics and hydrocarbons integrated with omics technologies.Archives of toxicology · 2026Review
- Engineering and Application of a Thermostable MHETase for PET Depolymerization.ACS sustainable chemistry & engineering · 2026Article
- Yeast MoClo Secretion and Surface Display Toolkit 2.0: Improvements and Applications for Analysis of protein-protein Interactions and Whole-Cell Biocatalysis.ACS synthetic biology · 2026Article
- Biological Degradation of Phthalates: From Bioremediation to Plastic Waste Valorization.ChemSusChem · 2026Review
- Rethinking plastic waste: innovations in enzymatic breakdown of oil-based polyesters and bioplastics.FEBS open bio · 2026Review
- Biochemical Upcycling of PET via Glycolysis and Engineered Microbial Consortia.Microbial biotechnology · 2026Article
- Article
- Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase.RSC advances · 2026Article
- Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Discovering PETases: An Interlink Between Engineering Enzymes and Microbiomes.Environmental microbiology · 2026Review
- Disordered N-termini enhance the thermostability of SGNH-hydrolase family polyesterases.Protein science : a publication of the Protein Society · 2026Article
- A Structural Landscape Depiction of Dynamic Stability Centers of Local Structure in Protein Thermostability Engineering.Research (Washington, D.C.) · 2026Article
- Microplastics in human body: accumulation, natural clearance, and biomedical detoxification strategies.Biomedical engineering letters · 2025Review
- It Is Dangerous to Go Alone: Strategies to Optimize PET Biocatalysis and Upcycling through Enzymatic Synergism.ACS omega · 2025Review
- Computational loop reconstruction based design of efficient PET hydrolases.Communications biology · 2025Article
- Complete Enzymatic Depolymerization of Polyethylene Terephthalate (PET) Plastic Using aEnvironmental science & technology letters · 2025Article
Corrections and comments
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Authors and funding
11 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Recently developed enzymes for the depolymerization of polyethylene terephthalate (PET) such as FAST-PETase and LCC-ICCG are inhibited by the intermediate PET product mono(2-hydroxyethyl) terephthalate (MHET). Consequently, the conversion of PET enzymatically into its constituent monomers terephthalic acid (TPA) and ethylene glycol (EG) is inefficient. In this study, a protein scaffold (1TQH) corresponding to a thermophilic carboxylesterase (Est30) was selected from the structural database and redesigned in silico. Among designs, a double variant KL-MHETase (I171K/G130L) with a similar protein melting temperature (67.58 °C) to that of the PET hydrolase FAST-PETase (67.80 °C) exhibited a 67-fold higher activity for MHET hydrolysis than FAST-PETase. A fused dual enzyme system comprising KL-MHETase and FAST-PETase exhibited a 2.6-fold faster PET depolymerization rate than FAST-PETase alone. Synergy increased the yield of TPA by 1.64 fold, and its purity in the released aromatic products reached 99.5%. In large reaction systems with 100 g/L substrate concentrations, the dual enzyme system KL36F achieved over 90% PET depolymerization into monomers, demonstrating its potential applicability in the industrial recycling of PET plastics. Therefore, a dual enzyme system can greatly reduce the reaction and separation cost for sustainable enzymatic PET recycling.
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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.