We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Molecular dynamics simulations of temperature-dependent PET binding in PETase, ThermoPETase, and FAST-PETase
AI summary Read the abstract
Molecular dynamics simulations comparing wild-type IsPETase with two engineered variants (ThermoPETase and FAST-PETase) showed that FAST-PETase exhibited the highest thermal stability and preserved PET binding at elevated temperatures where the wild-type enzyme lost substrate contact. Engineering thermostable PET-degrading enzymes is a promising strategy for biological treatment of PET microplastic pollution at industrial scales.
Polyethylene terephthalate (PET) biodegradation has gained significant attention following the 2016 discovery of the PET-hydrolyzing enzyme IsPETase from Ideonella sakaiensis 201-F6. Although IsPETase operates under mild temperature conditions, its limited catalytic activity and poor thermal stability restrict large-scale industrial applications. To overcome these limitations, several engineered variants have been developed. In this study, the wild-type IsPETase was systematically compared with two engineered variants, ThermoPETase and FAST-PETase, under four temperature conditions (300, 313, 323, and 333 K) using fully detailed atomistic molecular dynamics (MD) simulations. A PET dimer was docked into the active site of each enzyme, followed by 150 ns of restrained and unrestrained MD simulations to evaluate structural stability and substrate interactions. Both engineered variants exhibited improved thermal stability relative to IsPETase, with FAST-PETase demonstrating the highest stability across all temperatures. Increased flexibility of the catalytic triad was observed in both engineered variants, suggesting enhanced catalytic adaptability compared to IsPETase. Key residues, Tyr87 and Met161, were identified as essential for stabilizing the PET dimer within the active-site cavity. At elevated temperature (333 K), IsPETase showed increased flexibility, leading to disrupted PET dimer binding. In contrast, ThermoPETase and FAST-PETase preserved stable PET dimer positioning at elevated temperatures, with FAST-PETase displaying the most favourable structural characteristics across all temperature conditions. Furthermore, binding energy calculations revealed a correlation between structural stability and reduced enthalpic binding energies at each enzyme's optimal temperature. Based on these analyses, the optimal temperatures for PET degradation were found to be 323 K for IsPETase, 333 K for ThermoPETase, and 300-313 K for FAST-PETase. These findings provide molecular-level insights into the structure-stability-activity relationships of PETase variants and highlight key determinants for the rational design of improved PET-degrading enzymes.
More Papers Like This
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
AI summary Read the abstract
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.
The Action of Plastic Degrading Enzyme is Accelerated Mainly Due to an Increase in Thermal Stability Rather Than by Inherent Catalytic Effect
AI summary Read the abstract
Researchers used computational simulations to investigate why the engineered FAST-PETase enzyme breaks down PET plastic more efficiently than its wild-type counterpart, finding that enhanced thermal stability — rather than direct catalytic improvements — is the primary driver of its superior performance at elevated temperatures.
Temperature-Dependent Active-Site Rearrangements of PETaseSM14: Insights from Molecular Dynamics Simulations
AI summary Read the abstract
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.
Computer-guided enzyme engineering of PET hydrolase mutants towards improved PET affinity
AI summary Read the abstract
Researchers applied computer-guided enzyme engineering to improve the affinity of PETase mutants from Ideonella sakaiensis for PET plastic, identifying structural modifications that enhance substrate binding and degradation efficiency. The work advances the development of enzymatic plastic recycling as a sustainable alternative to mechanical and chemical methods.
Temperature-Dependent Reorganization of Conformational Dynamics and Interaction Networks Underlies Thermostability in PET-Degrading Enzymes
AI summary Read the abstract
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
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.