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Directed Evolution of PET Hydrolase to Tackle Plastic Pollution
Summary
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.