Engineered Enzymes—Design for Safe, Targeted Microplastic Therapeutics

  • Enzyme engineering uses mutations, fusion domains, and glycosylation for optimal PETase variants.
  • Design advances increase activity, thermostability, and substrate specificity.
  • Delivery technologies boost circulation, targeting, and immune evasion.
  • Safety (low cytotoxicity) and tissue targeting are top design priorities.
  • The future is custom-designed biocatalysts for microplastic remediation in medicine.
  1. Current PETase engineering advances (2023)
  2. Glycan engineering for PETase stability (2023)
  3. PETase serum paper (2024)
  4. Delivery of cytotoxic enzymes (2022)
  5. Cytochrome P450 enzyme design (2024)

Engineering enzymes for therapeutic microplastic removal combines rational mutagenesis, fusion protein technologies, and controlled glycosylation to create PETase variants with enhanced activity, stability, and safety. Loop and surface mutations optimize enzyme-substrate interactions, while fusion with CBMs or hydrophobins improves targeting and affinity for plastics found in the bloodstream. Glycosylation modulates enzyme resilience against blood proteases and immune recognition.

Delivery techniques, including encapsulation, PEGylation, and cell-surface anchoring, further improve distribution, reduce cytotoxicity, and enable organ targeting. Hybrid designs allow for companion domains to process a wider array of microplastics. Customized biocatalysts tailored to the patient’s plastic burden are on the horizon, transforming landfill enzymes into medical microplastic eliminators.