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Atomistic-Level Insights into the Role of Mutations in the Engineering of PET Hydrolases: A Systematic Review
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This systematic review examined the role of mutations in engineering PET-degrading enzymes including TfCut2, IsPETase, and LCC across 20 studies, integrating molecular dynamics simulations with experimental findings. The review identifies key residue hotspots enhancing catalytic performance and thermostability, demonstrating MD simulations as powerful tools guiding targeted mutation strategies for enzymatic plastic degradation.
Plastic pollution is a growing global challenge, and traditional plastic waste management methods are proving inadequate in tackling the issue. Enzymatic biodegradation has emerged as a promising alternative or addition to plastic waste management due to its environmentally friendly profile. Polyethylene terephthalate (PET) is among the most widely used polymers in packaging, and recent research has identified several PET-degrading enzymes, such as TfCut2, IsPETase, and LCC, as promising candidates for biodegradation applications at the industrial level. This has led to extensive efforts to improve their catalytic efficiency, with targeted mutagenesis being the preferred method employed for their modification. To this end, molecular dynamics (MD) simulations coupled with experimental validation have provided critical atomistic-level insights into the effect of mutations on enzymatic function. The present systematic review examines the role of mutations in determining enzymatic activity and thermostability, analyzing their structural and mechanistic contributions across 20 studies. The integration of MD simulations and experimental findings allows elucidation of the mechanistic details governing polymer degradation, as well as identification of key residue and enzyme hotspots that enhance catalytic performance. The review further highlights the role of MD simulations as powerful tools in providing valuable insights to guide targeted mutations for enzyme efficiency optimization.
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Researchers used computational and structural analyses to decode how PET polymer chains enter and bind within the active sites of plastic-degrading hydrolase enzymes, providing mechanistic insights that could guide engineering of more efficient PETase variants for industrial recycling applications.
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