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Directed Evolution of PET Hydrolase to Tackle Plastic Pollution
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Scientists are studying a bacterial enzyme that can break down PET plastic (the kind used in water bottles) and engineering it to work faster and better for recycling. This matters because plastic waste breaks down into microplastics that end up in our water, food, and even our bodies, so more efficient plastic recycling could mean less plastic pollution overall. Note that this is an educational case study for teaching bioinformatics methods, not a report of new experimental results, so it doesn't introduce a novel enzyme breakthrough itself.
Scientists are actively exploring whether mutations to PETase can make it efficient enough for industrial recycling. This case study consists of several parts which can be used separately or together. After a brief introduction (Part 1), in Parts 2 and 3 bioinformatics resources are used to put PETase in a metabolic context and compare it to closely related enzymes. In Part 4, structural resources are used to investigate important features of this enzyme and relate it to common course content about the model serine protease chymotrypsin. In Part 5, the structure of one literature example of an engineered PETase is explored in detail, and options are suggested for how to use bioinformatics resources to explore others. Finally, Part 6 uses a popular press article to explore some context and background for the directed evolution of this enzyme. Molecules explored: The primary molecule studied in this case is a polyethylene terephthalate hydrolase (PETase) from Ideonella sakaiensis. Exploration of the structure-function relationship will include comparison of several mutants and related enzymes.
More Papers Like This
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.
Overcoming catalytic barriers to reprogram acyltransferases for bis(2-hydroxyethyl) terephthalate hydrolysis
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Scientists engineered a bacterial enzyme to break down plastic waste more efficiently, turning PET (the plastic in water bottles) into valuable, reusable chemical building blocks instead of just breaking it into low-value pieces. This matters because better plastic recycling technology could reduce the mountains of plastic waste that eventually break down into microplastics—tiny particles increasingly found in our water, food, and even our bodies, where researchers are still studying their potential health effects.
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.
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.
Rational redesign of FAST-PETase via a "locking" strategy for efficient PET depolymerization
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Scientists engineered a new version of a plastic-eating enzyme that breaks down PET (the plastic used in water bottles and food packaging) nearly twice as fast as the previous best version, by adding a molecular "lock" that makes the enzyme sturdier and more effective. This matters because faster, more efficient plastic recycling could help reduce the mountains of PET waste that eventually break down into microplastics—tiny particles increasingly found in our food, water, and even our bodies, with still-unclear health effects.
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