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Advancing PET-Degrading Enzymes through Directed Evolution to Combat Plastic Pollution
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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.
Plastic pollution poses a significant environmental challenge due to its persistence and widespread distribution. Among various types of plastic, polyethylene terephthalate (PET) is especially problematic due to its resistance to natural degradation. PET-degrading enzymes, particularly PETases and cutinases, have emerged as promising solutions for enzymatic plastic recycling. However, their native catalytic efficiency and thermostability are limited. Directed evolution has enabled the development of improved enzyme variants through techniques such as error-prone PCR, DNA shuffling, and saturation mutagenesis. This review highlights recent advances in engineering Cutinase and PETases, focusing on enhancing catalytic efficiency and thermostability for PET plastic degradation by directed evolution. Key engineered variants, including HotPETase and optimized leaf-branch compost cutinase (LCC) mutants, demonstrate significant progress toward sustainable plastic recycling through enzymatic means.
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An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
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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.
Molecular Engineering of PET-Degrading Enzymes: Opportunities and Challenges
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Researchers reviewed advances in engineering PET-degrading enzymes for closed-loop plastic recycling, highlighting how directed evolution, rational design, and machine learning are pushing catalytic performance forward, while noting persistent barriers including poor activity at low temperatures and limited depolymerization of highly crystalline PET.
Tailoring enzymes for polyester-plastic depolymerization.
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Researchers reviewed recent advances in protein engineering of plastic-degrading enzymes targeting PET, polyurethane, PLA, and PBAT, summarizing how directed evolution and computational design have improved thermal stability, catalytic efficiency, and expression yield to make enzymatic plastic recycling more industrially viable.
Recent advances in enzyme engineering for improved deconstruction of poly(ethylene terephthalate) (PET) plastics
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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.
An Efficient Protein Evolution Workflow for the Improvement of Bacterial PET Hydrolyzing Enzymes.
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Researchers developed a protein engineering workflow to improve bacterial enzymes that degrade PET plastic, combining semi-rational design with high-throughput screening. The resulting engineered enzyme variant achieved over 80% depolymerization of PET nanoparticles within 1.5 hours using only small amounts of enzyme.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.