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Papers
61,005 resultsShowing papers similar to A computational approach to optimising laccase-mediated polyethylene oxidation through carbohydrate-binding module fusion
ClearMachine Learning-Driven Multi-Objective Optimization of Enzyme Combinations for Plastic Degradation: An Ensemble Framework Integrating Sequence Features and Network Topology
Researchers developed a machine learning framework to identify optimal enzyme combinations for breaking down polyester plastics. The study integrated kinetic data, protein sequence features, and network analysis to predict effective enzyme-substrate relationships, offering a computational approach to accelerating the discovery of enzymatic solutions for plastic waste degradation.
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.
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.
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.
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.
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 Optimization of Biocatalysts for New Recycling Technologies
Researchers investigated the characterisation and optimisation of enzymatic biocatalysts capable of degrading synthetic plastics, addressing the limitations of conventional mechanical recycling that has proven largely ineffective at curbing plastic and microplastic accumulation in terrestrial and aquatic ecosystems. The work explores how enzyme engineering and directed evolution can improve the efficiency of biological plastic breakdown as a pathway toward circular plastic recycling.
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.
Engineering Plastic Eating Enzymes Using Structural Biology
This review examines how structural biology approaches are being used to engineer plastic-degrading enzymes with improved efficiency and industrial scalability. Understanding the molecular interactions between enzymes and plastic substrates at an atomic level is guiding the design of more effective biocatalysts for plastic biodegradation.
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.
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.
Enhanced degradation of microplastics by laccase under ambient conditions: Analysis of underlying molecular mechanisms
This study demonstrated that the enzyme laccase can degrade three types of microplastics — polyethylene (PE), PET, and PLA — by breaking apart polymer chains and transforming surface chemical groups, with biodegradable PLA showing the highest degradation efficiency. The mechanistic insights into how reactive oxygen species and electron transfer drive enzymatic degradation provide a foundation for developing enzyme-based treatments to remove microplastics from water and soil.
Microplastic Degradation using Laccase Enzyme from Trametes hirsuta: In the Silico Study
Using molecular docking simulations, researchers investigated whether laccase enzymes from the fungus Trametes hirsuta could interact with and potentially degrade common microplastic compounds. In silico results showed binding interactions between laccase and several plastic polymers, suggesting enzymatic degradation pathways worth pursuing in wet-lab validation studies.
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.
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.
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.
Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer
Researchers used computer modeling to test whether a fungal enzyme called cutinase could break down nine types of synthetic plastics, finding strong binding affinity for PET, PCL, and several biodegradable plastics — pointing toward biological tools that could help degrade plastic waste in the environment.
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.
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.
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.
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.
Discovery and Biochemical Characterization of a Novel Polyesterase for the Degradation of Synthetic Plastics
Researchers used bioinformatics to discover a new enzyme from soil bacteria capable of breaking down synthetic plastics like PET and polyurethane. The enzyme was successfully expressed and characterized in the lab, offering a promising lead for developing biological plastic recycling approaches.
Enhancing PET Degrading Enzymes: A Combinatory Approach
Scientists worked on improving enzymes that can break down PET plastic, one of the most common plastics in consumer products. Using a combinatory approach, researchers enhanced the performance of a naturally occurring PET-degrading enzyme from the bacterium Piscinibacter sakaiensis. The study suggests that engineered enzymes could eventually help create a circular economy for plastic waste by enabling efficient recycling at the molecular level.
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.