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Engineering and Application of a Thermostable MHETase for PET Depolymerization.

Natasha P Murphy1,2,3, Japheth E Gado1,2,3, Tabea Neumann4

  • 1Renewable Resources and Enabling Sciences Center, National Laboratory of the Rockies, Golden, Colorado 80401, United States.

ACS Sustainable Chemistry & Engineering
|June 26, 2026
PubMed
Summary
This summary is machine-generated.

Researchers developed thermostable MHETase enzymes for efficient enzymatic poly-(ethylene terephthalate) (PET) recycling. These enzymes improve the hydrolysis of mono-(2-hydroxyethyl) terephthalate (MHET), a key intermediate in PET degradation.

Keywords:
EnzymesHigh-throughput assayInterfacial biocatalysisPolymersProtein engineering

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Area of Science:

  • Biotechnology and Industrial Microbiology
  • Enzyme Engineering and Biocatalysis
  • Polymer Science and Recycling

Background:

  • Enzymatic hydrolysis of poly-(ethylene terephthalate) (PET) produces mono-(2-hydroxyethyl) terephthalate (MHET).
  • MHET accumulation complicates PET recycling processes.
  • Existing PETases are often thermophilic, while the known MHETase from *Ideonella sakaiensis* is mesophilic, necessitating the development of thermostable MHETases.

Purpose of the Study:

  • To characterize novel thermostable MHET-active enzymes for improved enzymatic PET recycling.
  • To engineer enhanced MHETase activity and thermostability through structure-guided and evolution-informed design.

Main Methods:

  • Screening for thermostable MHET-active enzymes using a hidden Markov model based on archaeal ferulic acid esterase PET46.
  • Characterization of enzyme activity at 70 °C and determination of melting temperatures (Tm,app).
  • Structure-based site saturation mutagenesis and evolution-informed design (EID) to improve enzyme performance.
  • Bioreactor experiments using postconsumer PET waste to assess MHET reduction.

Main Results:

  • Identified novel thermostable MHET-active enzymes with higher stability than PET46.
  • MHT077 showed high MHETase activity and kinetic stability, with a Tm,app of 94.6 °C.
  • Evolution-informed design yielded EV-MHT043-5 with comparable thermostability (Tm,app = 96.1 °C) and a 3-fold increase in MHETase activity.
  • A combination variant, MHT077LFK, significantly reduced MHET accumulation in bioreactor experiments.

Conclusions:

  • This study expands the repertoire of protein scaffolds for MHET hydrolysis in enzymatic PET recycling.
  • The developed thermostable MHETases offer promising solutions for more efficient and industrially viable PET degradation.
  • Engineered variants demonstrate enhanced activity and stability, crucial for practical application in plastic waste management.