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61,005 resultsShowing papers similar to Efficient polyethylene terephthalate degradation at moderate temperature: a protein engineering study of LC ‐cutinase highlights the key role of residue 243
ClearAn 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.
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.
The Current State of Research on PET Hydrolyzing Enzymes Available for Biorecycling
This review summarizes the current state of PET-hydrolyzing enzymes, including thermophilic cutinases and engineered variants, that are candidates for enzymatic biorecycling of PET plastic waste back into reusable monomers.
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.
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.
Characterization and engineering of a plastic-degrading aromatic polyesterase
Researchers characterized and engineered an aromatic polyesterase enzyme capable of degrading plastic polymers, improving its activity through protein engineering and demonstrating its potential as a tool for biodegradation-based plastic cleanup.
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.
Discovery and rational engineering of PET hydrolase with both mesophilic and thermophilic PET hydrolase properties
Researchers discovered a new enzyme from a soil bacterium that can break down PET plastic — the material in most plastic bottles — at both room temperature and elevated heat, then engineered an improved version that degrades PET powder almost completely within half a day at 55°C. This dual-temperature capability makes it more practical than existing enzymes for industrial-scale plastic recycling and could help address the global PET waste problem.
Recent advances in enzyme engineering for improved deconstruction of poly(ethylene terephthalate) (PET) plastics
This review covers recent progress in engineering enzymes that can break down PET plastic, the material used in water bottles and food containers. While natural enzymes that digest PET have been discovered, they are not yet fast or durable enough for industrial-scale recycling. Advances in protein engineering, directed evolution, and computational design are steadily improving these enzymes, which could eventually provide a sustainable way to recycle PET and reduce microplastic pollution at its source.
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
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.
Hydrolytic Degradation of Polyethylene Terephthalate by Cutinase Enzyme Derived from Fungal Biomass–Molecular Characterization
Researchers isolated cutinase and lipase enzymes from Aspergillus tamarii and Penicillium crustosum fungi and demonstrated their ability to catalyze hydrolytic degradation of PET plastic, offering a potential biological route for plastic waste breakdown.
An efficient strategy to tailor PET hydrolase: Simple preparation with high yield and enhanced hydrolysis to micro-nano plastics
This study developed a simplified, high-yield preparation method for PET-degrading hydrolase enzymes to improve their ability to break down PET nano- and microplastics. The engineered enzyme showed enhanced hydrolysis activity against PET microplastics, offering a more practical route to enzymatic plastic waste treatment.
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.
Structural decay of poly(ethylene terephthalate) by enzymatic degradation
Researchers examined the structural decay of poly(ethylene terephthalate) through enzymatic degradation as a sustainable recycling strategy, finding this approach requires neither energy nor harsh solvents, offering a promising path for addressing microplastic pollution from PET products.
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.
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.
An archaeal lid-containing feruloyl-esterase degrades polyethylene terephthalate (PET)
This study identified the first archaeal enzyme capable of degrading PET plastic, characterizing its structure and biochemical properties. Expanding the diversity of organisms with PET-degrading enzymes could accelerate the development of biological strategies for breaking down the microplastics contaminating marine and terrestrial environments.
Enzymatic Remediation of Polyethylene Terephthalate (PET)–Based Polymers for Effective Management of Plastic Wastes: An Overview
Enzymatic approaches for remediating PET-based plastic waste were reviewed, covering PETase and related enzymes that can break PET into reusable monomers. Enzyme engineering strategies to improve thermostability and catalytic efficiency are discussed as a pathway to scalable biological PET recycling.
Engineered polyethylene terephthalate hydrolases: perspectives and limits
This review examines progress in engineering enzymes that can break down PET plastic, the material used in most beverage bottles and synthetic textiles. Researchers found that while significant advances have been made through protein engineering and machine learning, no enzyme yet exists that can efficiently degrade the crystalline form of PET found in real-world waste. The study outlines the key challenges remaining before enzymatic plastic recycling can work at industrial scale, including handling microplastic contamination.
Molecular Insights into the Enhanced Activity and/or Thermostability of PET Hydrolase by D186 Mutations
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.
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.
Current Knowledge on Polyethylene Terephthalate Degradation by Genetically Modified Microorganisms
This review covers genetically modified microorganisms engineered to degrade polyethylene terephthalate, examining how bioengineering of enzymes such as PETase and enhanced expression systems can overcome the low biodegradation rates of wild-type microorganisms toward this ubiquitous plastic.
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.