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The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function

  • Nitay Ahituv
  • , Dekel Freund
  • , Raul Mireles
  • , Lianet Noda-García*
  • *Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

2 Scopus citations

Abstract

Polyethylene terephthalate (PET) is one of the most significant plastic pollutants. Unlike other plastic polymers, PET can be degraded by PET-hydrolytic enzymes (PETases). Over the past two decades, numerous publications have reported the discovery, characterization, and engineering of PETases. This review thoroughly examines the sequence, structure, and functional diversity of naturally occurring PETases. To achieve this, we compiled data from 48 publications into a single table. The resulting dataset enabled us to contextualize previously reported features and shed light on the sequence–structure–function relationships of PETases. Finally, we review selected engineering campaigns and suggest future directions for the enzymatic recycling of PET under mesophilic and thermophilic conditions, aiming to understand the gaps to tackle the PET pollution crisis.

Original languageEnglish
Article numbere70282
JournalProtein Science
Volume34
Issue number10
DOIs
StatePublished - Oct 2025

Bibliographical note

Publisher Copyright:
© 2025 The Author(s). Protein Science published by Wiley Periodicals LLC on behalf of The Protein Society.

UN SDGs

This output contributes to the following UN Sustainable Development Goals (SDGs)

  1. SDG 12 - Responsible Consumption and Production
    SDG 12 Responsible Consumption and Production

Keywords

  • PET biodegradation
  • PET-hydrolytic enzymes (PETase)
  • dataset
  • polyethylene terephthalate
  • recycling

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