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61,005 resultsShowing papers similar to Molecular Insights into the Enhanced Activity and/or Thermostability of PET Hydrolase by D186 Mutations
ClearOn 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
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
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
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.
From Bulk to Binding: Decoding the Entry of PET into Hydrolase Binding Pockets
Researchers used molecular dynamics simulations and free energy analysis to decode the complete pathway by which PET polymer chains enter the binding pockets of plastic-degrading hydrolase enzymes at the atomic level. The study aims to deepen mechanistic understanding needed to guide protein engineering of PET hydrolases toward sufficient activity for industrial biocatalytic recycling.
Rational redesigning the Acinetobacter haemolyticus lipase KV1 for improved polyethylene terephthalate degradation via molecular docking and dynamics simulations
Researchers redesigned the Acinetobacter haemolyticus lipase KV1 enzyme to improve its ability to degrade polyethylene terephthalate (PET), using computational modeling to identify beneficial mutations. Engineered variants showed significantly enhanced PET hydrolysis activity, advancing the development of enzymatic plastic degradation tools.
An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
This review examines the discovery and engineering of PET-degrading enzymes including PETase and cutinase variants, discussing protein engineering strategies to improve catalytic efficiency and thermostability for practical biodegradation of polyethylene terephthalate plastic waste.
Rational redesigning the Acinetobacter haemolyticus lipase KV1 for improved polyethylene terephthalate degradation via molecular docking and dynamics simulations
This study evaluated engineered variants of lipase KV1 for improved PET degradation, using binding mode analysis and molecular simulations to understand enzymatic PET hydrolysis mechanisms. Optimized variants demonstrated improved degradation efficiency, contributing to biotechnological solutions for plastic waste.
Characterization and engineering of a two-enzyme system for plastics depolymerization
A 1.6 Å resolution crystal structure of MHETase — the second enzyme in Ideonella sakaiensis's PET-degrading two-enzyme system — revealed a PETase-like core capped by a lid domain, and computational and biochemical analysis confirmed a canonical serine hydrolase mechanism, enabling rational engineering of the PET recycling pathway.
Dynamic docking assisted engineering of hydrolase for efficient PET depolymerization
Researchers developed a computational protein engineering strategy called Affinity analysis based on Dynamic Docking (ADD) to enhance the PET-degrading enzyme leaf-branch-compost cutinase (LCC), producing a variant (LCC-A2) that degraded over 90% of post-consumer PET waste into monomers within 3.3 hours.
Advancing PET-Degrading Enzymes through Directed Evolution to Combat Plastic Pollution
This review examines advances in directed evolution of PET-degrading enzymes including PETases and cutinases, describing how techniques such as error-prone PCR, DNA shuffling, and saturation mutagenesis have produced enzyme variants with improved catalytic efficiency and thermostability for enzymatic plastic recycling applications.
Computational redesign of a PETase for plastic biodegradation by the GRAPE strategy
Researchers engineered a more stable version of the enzyme PETase, which breaks down PET plastic, using a computational protein design strategy. The improved enzyme could enable more efficient industrial biodegradation of PET plastic waste, including microplastics.
Current advances in the structural biology and molecular engineering of PETase
The study reviews advances in the structural biology and molecular engineering of PETase, an enzyme from the bacterium Ideonella sakaiensis that can break down PET plastic at moderate temperatures. Researchers discuss efforts to enhance the enzyme's activity and thermal stability through protein engineering, which could lead to more efficient and environmentally friendly PET recycling strategies.
Molecular docking analysis of PET with MHET
Researchers performed molecular docking analysis of PET polymer with mono(2-hydroxyethyl) terephthalic acid (MHET), investigating how the enzyme from Ideonella sakaiensis 201-F6 — a bacterium capable of degrading a thin PET film in six weeks — might be optimized to improve catalytic efficiency and expand substrate specificity for enzymatic plastic degradation.
Rational Design of Disulfide Bridges in BbPETaseCD for Enhancing the Enzymatic Performance in PET Degradation
Researchers rationally designed disulfide bridges in BbPETase, a PET-degrading enzyme from a Burkholderiales bacterium, to enhance its thermostability and enzymatic performance, offering a promising avenue for more efficient biological recycling of PET plastic waste.
Efficient polyethylene terephthalate degradation at moderate temperature: a protein engineering study of LC ‐cutinase highlights the key role of residue 243
Researchers engineered variants of leaf-branch compost cutinase that efficiently degrade PET plastic at moderate temperatures (55°C), finding that the S101N/F243T variant could fully depolymerize postconsumer PET waste and that lower temperatures actually improved degradation by preventing plastic recrystallization.
Determinants for an Efficient Enzymatic Catalysis in Poly(Ethylene Terephthalate) Degradation
This review covers the current state of enzymatic PET degradation, examining which enzymes act on PET, how protein engineering has improved their activity, and what challenges remain before enzymatic recycling can be deployed at industrial scale.
Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyesters Depolymerization
Researchers characterized a marine enzyme (PET2) capable of breaking down PET plastic and related polyester materials under relatively mild conditions. Discovering and engineering enzymes that can degrade PET could help address the massive accumulation of PET microplastics in ocean environments.
Computational Redesign of a PETase for Plastic Biodegradation under Ambient Condition by the GRAPE Strategy
Researchers developed a computational protein engineering strategy called GRAPE to redesign a PET-degrading enzyme from Ideonella sakaiensis. The resulting DuraPETase variant showed a 31-degree-Celsius increase in thermal stability and over 300-fold improved degradation of PET films at mild temperatures, achieving complete biodegradation of 2 g/L microplastics into water-soluble products under ambient conditions.
Comparative biochemistry of PET hydrolase-carbohydrate-binding module fusion enzymes on a variety of PET substrates
Researchers systematically compared two leading PET-digesting enzymes fused with substrate-binding domains across a range of industrial plastic substrates, finding that binding domains can either boost or reduce enzyme activity by up to six-fold depending on the substrate type. These results can help match the right enzyme to the right industrial recycling scenario.
Microbial Polyethylene Terephthalate Hydrolases: Current and Future Perspectives
This review surveys microbial enzymes capable of breaking down PET plastic, focusing on the structure and function of key hydrolases like PETase and cutinases. Researchers found that while several enzymes show promising PET-degrading activity, most work slowly and under limited temperature conditions, with engineered variants showing improved performance. The study highlights both the potential and the current limitations of using biological approaches for plastic waste management.
Degradation of PET Nanoplastic Oligomers at the Novel PHL7 Target:Insights from Molecular Docking and Machine Learning
Researchers used computational molecular docking and machine learning to show that the enzyme PHL7 degrades PET nanoplastics most efficiently at shorter chain lengths, with binding affinity becoming unfavorable once PET oligomer chains exceed six repeat units in length.
In silico binding affinity analysis of microplastic compounds on PET hydrolase enzyme target of Ideonella sakaiensis
Researchers used computer simulations to test whether a bacterial enzyme (PET hydrolase from Ideonella sakaiensis) could break down six types of plastic, finding it most effective against polycarbonate and polyethylene terephthalate (PET) and least effective against PVC, informing which plastics this microbe might help degrade in the environment.
Protein-plastic interactions: The driving forces behind the high affinity of a carbohydrate-binding module for polyethylene terephthalate
This study investigated the molecular forces driving high-affinity binding of a carbohydrate-binding module protein to PET plastic surfaces, revealing that hydrophobic interactions and specific structural features of the protein-plastic interface are key determinants relevant to engineering better PET-degrading enzymes.
Whether the wobbling W156 is a pre-requisite for efficient PET biodegradation by IsPETase
Researchers engineered a thermostable variant of the PET-degrading enzyme IsPETase that achieves over 100-fold improvement in PET breakdown efficiency. More effective PET-degrading enzymes could enable industrial-scale recycling of PET plastic, reducing the amount of this common polymer that fragments into microplastics in the ocean.