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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.
PETase exhibits a high degradation activity for polyethylene terephthalate (PET) plastic under moderate temperatures. However, the effect of non-active site residues in the second shell of PETase on the catalytic performance remains unclear. Herein, we proposed a crystal structure- and sequence-based strategy to identify the key non-active site residue. D186 in the second shell of PETase was found to be capable of modulating the enzyme activity and stability. The most active PETaseD186N improved both the activity and thermostability with an increase in Tm by 8.89 °C. The PET degradation product concentrations were 1.86 and 3.69 times higher than those obtained with PETaseWT at 30 and 40 °C, respectively. The most stable PETaseD186V showed an increase in Tm of 12.91 °C over PETaseWT. Molecular dynamics (MD) simulations revealed that the D186 mutations could elevate the substrate binding free energy and change substrate binding mode, and/or rigidify the flexible Loop 10, and lock Loop 10 and Helix 6 by hydrogen bonding, leading to the enhanced activity and/or thermostability of PETase variants. This work unraveled the contribution of the key second-shell residue in PETase in influencing the enzyme activity and stability, which would benefit in the rational design of efficient and thermostable PETase.
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Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review
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This systematic review examined the role of mutations in engineering PET-degrading enzymes including TfCut2, IsPETase, and LCC across 20 studies, integrating molecular dynamics simulations with experimental findings. The review identifies key residue hotspots enhancing catalytic performance and thermostability, demonstrating MD simulations as powerful tools guiding targeted mutation strategies for enzymatic plastic degradation.
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.
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.
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
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