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Characterization and engineering of a two-enzyme system for plastics depolymerization.

Brandon C Knott1, Erika Erickson1, Mark D Allen2

  • 1Renewable Resources and Enabling Sciences Center, National Renewable Energy Laboratory, Golden, CO 80401.

Proceedings of the National Academy of Sciences of the United States of America
|September 29, 2020
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Summary
This summary is machine-generated.

Microbes can break down plastics like polyethylene terephthalate (PET) using enzymes. This study details the MHETase enzyme structure and function, crucial for PET deconstruction and plastic upcycling.

Keywords:
biodegradationpolyethylene terephthalaterecyclingserine hydrolaseupcycling

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Area of Science:

  • Biochemistry
  • Environmental Microbiology
  • Structural Biology

Background:

  • Plastic pollution is a major environmental issue.
  • Microorganisms are evolving to degrade synthetic polymers.
  • The bacterium *Ideonella sakaiensis* utilizes a two-enzyme system, PETase and MHETase, for polyethylene terephthalate (PET) degradation.

Purpose of the Study:

  • To elucidate the structure and function of MHETase, a key enzyme in PET deconstruction.
  • To understand the catalytic mechanism and evolutionary origins of MHETase.
  • To investigate the synergistic action of PETase and MHETase and optimize their performance for plastic upcycling.

Main Methods:

  • X-ray crystallography to determine the 1.6 Å resolution structure of MHETase.
  • Molecular simulations to predict the catalytic mechanism.
  • Bioinformatics analysis for evolutionary insights.
  • Enzyme activity assays with wild-type and mutant enzymes, and chimeric proteins.
  • Degradation assays using amorphous PET film.

Main Results:

  • The MHETase structure reveals a core domain similar to PETase, with a distinct lid domain.
  • MHETase follows a canonical two-step serine hydrolase mechanism.
  • MHETase evolved from ferulic acid esterases, with homologous enzymes showing MHET turnover.
  • The MHETase lid and active site residue S131 are critical for MHET hydrolysis.
  • PETase and MHETase exhibit strong synergy in PET monomer conversion.
  • Chimeric MHETase:PETase proteins show enhanced PET and MHET turnover.

Conclusions:

  • MHETase plays a vital role in the biological deconstruction of PET.
  • Understanding MHETase structure-function relationships informs enzyme engineering for plastic upcycling.
  • The synergistic action of PETase and MHETase offers a promising route for sustainable plastic waste management.