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Temperature-Dependent Reorganization of Conformational Dynamics and Interaction Networks Underlies Thermostability in PET-Degrading Enzymes
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Scientists are studying how to engineer sturdier enzymes that can break down plastic bottles (PET) into reusable materials, since natural plastic-eating enzymes tend to fall apart at the high temperatures needed for efficient recycling. By using computer simulations to compare a natural enzyme with two engineered, heat-resistant versions, researchers pinpointed exactly what structural features let the improved enzymes stay stable and functional under heat. This matters because better plastic-recycling enzymes could help reduce the massive amount of plastic waste that breaks down into microplastics — tiny particles increasingly found in our food
Polyethylene terephthalate (PET) is one of the most widely used synthetic plastics and a major contributor to global plastic pollution because of its high resistance to degradation. Enzymatic degradation by PET hydrolases (PETase) has emerged as a sustainable strategy for PET recycling; however, the limited thermostability of wild-type PETase restricts its industrial application. To elucidate the molecular basis underlying the different thermal behaviors of PET hydrolases, long-timescale molecular dynamics simulations were performed on WT-PETase, FAST-PETase, and the thermostable cutinase variant LCC-ICCG at 30 °C, 50 °C, and 70 °C. Comparative analyses integrating structural stability, residue flexibility, rigidity networks, free energy landscapes, and neural relational inference models revealed that FAST-PETase and LCC-ICCG exhibited enhanced conformational stability and reduced structural flexibility compared with WT-PETase, particularly under elevated temperatures. The improved thermostability was associated with more compact free energy landscapes, strengthened residue interaction networks, and better preservation of the catalytic architecture during thermal perturbation. These results suggest that an optimal balance between structural rigidity and conformational flexibility is critical for maintaining enzyme stability at elevated temperatures. Overall, this study provides molecular-level insights into the structural determinants of PETase thermostability and offers a theoretical framework for the rational engineering of efficient and heat-resistant plastic-degrading enzymes.
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On the Role of Temperature in the Depolymerization of PET by FAST‐PETase: An Atomistic Point of View on Possible Active Site Pre‐Organization and Substrate‐Destabilization Effects
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Researchers used molecular simulations to understand why the plastic-degrading enzyme FAST-PETase works better at 50°C than at lower temperatures when breaking down PET plastic. They found that at the optimal temperature the enzyme's active site pre-organizes itself to bind PET more efficiently, and the enzyme forces the plastic into a more reactive shape. Understanding these mechanisms can guide the engineering of even more effective enzymes for breaking down PET microplastics and plastic waste at practical scales.
Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations
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Researchers used molecular dynamics simulations at multiple temperatures to investigate how PETaseSM14 — a marine-derived PET-degrading enzyme — changes conformation at its active site, finding that moderate warming exposes the catalytic residue to enable substrate binding while excessive heat disrupts the catalytic triad, providing targets for enzyme engineering.
Molecular Insights into the Enhanced Activity and/or Thermostability of PET Hydrolase by D186 Mutations
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This study used molecular simulations to analyze how D186 mutations in PETase affect its activity and thermostability, revealing that non-active-site residues in the enzyme's second shell play an important role in PET plastic degradation efficiency.
Simulation Assisted Improvement of Plastic Degradation Enzyme PETase based Machine Learning Tools
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Machine learning tools combined with molecular simulation were used to improve the performance of PETase, a plastic-degrading enzyme, for polyethylene terephthalate (PET) biodegradation. The approach identified key structural mutations that enhanced enzyme stability and catalytic efficiency, advancing enzymatic PET recycling.
MPNN-guided redesign of PET hydrolases with enhanced catalytic activity below the PET glass transition temperature
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A structured PFAS risk matrix for EU food packaging compliance shows that fibre-based materials with grease- or water-resistant coatings carry the highest PFAS relevance, while glass and untreated PET present lower risk, with total fluorine serving as a material-specific rather than standalone compliance indicator. Because PFAS from food packaging leach into food and waterways, systematic risk-based screening frameworks directly support efforts to reduce the chemical contamination load associated with plastic and coated-paper packaging waste.
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