Development of a highly active engineered PETase enzyme for polyester degradation

Area of Science:

• Biotechnology
• Environmental Science
• Polymer Science

Background:

• Polyethylene terephthalate (PET) is a major contributor to global plastic waste.
• Enzymatic recycling of PET is a key strategy for a circular economy.
• Current PET-degrading enzymes have limitations in stability, efficiency, and product inhibition.

Purpose of the Study:

• To engineer a more stable and efficient PET-hydrolyzing enzyme.
• To overcome the limitations of existing enzymes for industrial PET recycling.

Main Methods:

• In silico protein design was used to engineer the LCC-ICCG enzyme.
• The engineered mutant, LCC-ICCG-C09, was characterized for thermal stability and catalytic activity.

Main Results:

• The LCC-ICCG-C09 mutant exhibited a 3.5°C increase in melting temperature compared to the parent enzyme.
• At 68°C, LCC-ICCG-C09 demonstrated a two-fold higher efficiency in hydrolyzing amorphous PET into terephthalic acid (TPA).

Conclusions:

• The engineered LCC-ICCG-C09 enzyme shows enhanced thermal stability and PET depolymerization activity.
• LCC-ICCG-C09 is a promising candidate for advancing industrial PET recycling processes.