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<p>Enzymatic degradation of polyethylene terephthalate (PET) has garnered attention as a new PET decomposition technology because of its progression under mild conditions. However, the practical application of these enzymes is significantly hindered by their high purification costs. To address this, we developed an <i>Escherichia coli</i> strain with surface-engineered capabilities for efficient PET degradation by expressing PET-degrading enzymes. Several components were considered and optimized for the efficient degradation of PET using this microorganism catalyst. When comparing the expression systems, cells displaying PETase on the surface using the arabinose-inducible system showed a 2.9-fold improvement in PET degradation compared to those using the isopropyl β-<span>d</span>-1-thiogalactopyranoside-inducible system. Furthermore, cells with both surface-displayed FAST-PETase and localized MHETase in the periplasm exhibited a 6.6-fold increase in PET degradation efficiency compared to the initial pETDuet system. Notably, MHETase expression shifted the product profile toward predominantly terephthalic acid (TPA) formation. These results demonstrate that incorporating MHETase into a PET degradation system predominantly yields TPA, suggesting potential applications for efficient PET upcycling into valuable chemicals.</p>

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Escherichia coli with surface display of PETase and periplasmic localization of mhetase for enhanced terephthalic acid production from PET

  • 期刊论文

  • 发表日期：

    2025年11月25日

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  • Yuto Kurauchi,
  • Takuma Yamashita,
  • Takuya Matsumoto,
  • Ryosuke Yamada,
  • Hiroyasu Ogino

摘要

Enzymatic degradation of polyethylene terephthalate (PET) has garnered attention as a new PET decomposition technology because of its progression under mild conditions. However, the practical application of these enzymes is significantly hindered by their high purification costs. To address this, we developed an Escherichia coli strain with surface-engineered capabilities for efficient PET degradation by expressing PET-degrading enzymes. Several components were considered and optimized for the efficient degradation of PET using this microorganism catalyst. When comparing the expression systems, cells displaying PETase on the surface using the arabinose-inducible system showed a 2.9-fold improvement in PET degradation compared to those using the isopropyl β-d-1-thiogalactopyranoside-inducible system. Furthermore, cells with both surface-displayed FAST-PETase and localized MHETase in the periplasm exhibited a 6.6-fold increase in PET degradation efficiency compared to the initial pETDuet system. Notably, MHETase expression shifted the product profile toward predominantly terephthalic acid (TPA) formation. These results demonstrate that incorporating MHETase into a PET degradation system predominantly yields TPA, suggesting potential applications for efficient PET upcycling into valuable chemicals.