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Rational redesign of FAST-PETase via a "locking" strategy for efficient PET depolymerization.

Zhi Qu¹, Zongyang Tian¹, Zehui Guo¹

¹State Key Laboratory of Synthetic Biology, School of Synthetic Biology and Biomanufacturing, Frontiers Science Center for Synthetic Biology (MOE), and Key Laboratory of Systems Bioengineering (MOE), Tianjin University, Tianjin 300350, China.

Journal of Hazardous Materials

|April 3, 2026

Summary

This summary is machine-generated.

A new "locking" strategy enhances polyethylene terephthalate hydrolase (FAST-PETase) performance. The engineered variant shows significantly improved plastic degradation efficiency and thermostability, offering a promising solution for PET plastic waste recycling.

Keywords:

Locking strategy Molecular mechanism PET hydrolase Polyethylene terephthalate Rational design

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Area of Science:

Biotechnology
Enzyme Engineering
Environmental Science

Background:

Polyethylene terephthalate (PET) plastic waste poses a significant global environmental challenge.
Efficient enzymatic degradation and biorecycling of PET require superior PET hydrolases.

Purpose of the Study:

To improve the performance of FAST-PETase, a highly effective PET hydrolase, using a rational redesign strategy.
To engineer a variant with enhanced degradation efficiency and thermostability for PET plastic waste treatment.

Main Methods:

A "locking" strategy was employed to rationally redesign FAST-PETase.
The best variant, FAST-PETase^DC (A171C/S193C), was characterized for its degradation efficiency and thermal stability.
Molecular dynamics simulations were used to elucidate the structural basis for improved performance.

Main Results:

FAST-PETase^DC demonstrated a 1.9-fold increase in PET degradation efficiency at 50 °C compared to FAST-PETase.
The engineered variant exhibited a 4.1 °C higher melting temperature (T_m), indicating enhanced thermostability.
FAST-PETase^DC achieved near-complete depolymerization of untreated post-consumer PET film within 3 days, twice as fast as FAST-PETase.

Conclusions:

The "locking" strategy is an effective approach for enzyme redesign, leading to improved PET hydrolase performance.
The engineered FAST-PETase^DC variant shows significant promise for the enzymatic degradation and recycling of low-to-medium crystallinity PET plastic waste.
Structural modifications, including disulfide bond formation, rigidify the enzyme and enhance substrate interaction, boosting efficiency and stability.