Decomposition of the PET Film by MHETase Using Exo-PETase Function

Hye Young Sagong, Hogyun Seo, Taeho Kim, Hyeoncheol Francis Son, Seongjoon Joo, Seul Hoo Lee, Seongmin Kim, Jae Sung Woo, Sung Yeon Hwang, Kyung Jin Kim

Research output: Contribution to journalArticlepeer-review

50 Citations (Scopus)


Monohydroxyethyl terephthalate (MHET) hydrolase (MHETase) is an enzyme known to be involved in the final degradation step of poly(ethylene terephthalate) (PET) by hydrolyzing MHET into terephthalic acid and ethylene glycol in Ideonella sakaiensis. Here, we report the extracellular production of MHETase in an active form with a proper folding. Based on the structural observations and biochemical experiments, we reveal that MHETase also functions as exo-PETase by hydrolyzing the synthesized PET pentamer. We further present that MHETase has a hydrolysis activity against the termini-generated PET film, demonstrating the exo-PETase function of the enzyme. We also develop a MHETaseR411K/S416A/F424I variant with a higher BHET activity, and the variant exhibits an enhanced degradation activity against the PET film. Based on these results, we propose that MHETase plays several roles in the biodegradation of PET using the BHETase and exo-PETase activities as well as the MHET hydrolysis function.

Original languageEnglish
Pages (from-to)4805-4812
Number of pages8
JournalACS Catalysis
Issue number8
Publication statusPublished - 2020 Apr 17


  • Ideonella sakaiensis
  • MHETase
  • biodegradation
  • exo-PETase
  • extracellular production
  • polyethylene terephthalate (PET)

ASJC Scopus subject areas

  • Catalysis
  • Chemistry(all)


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