Directed Evolution of PET Hydrolase to Tackle Plastic Pollution

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.