Adsorption of enzymes with hydrolytic activity on polyethylene terephthalate

Silke Flindt Badino, Jenny Arnling Bååth, Kim Borch, Kenneth Jensen, Peter Westh*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

Polyethylene terephthalate (PET) degrading enzymes have recently obtained an increasing interest as a means to decompose plastic waste. Here, we have studied the binding of three PET hydrolases on a suspended PET powder under conditions of both enzyme- and substrate excess. A Langmuir isotherm described the binding process reasonably and revealed a prominent affinity for the PET substrate, with dissociation constants consistently below 150 nM. The saturated substrate coverage approximately corresponded to a monolayer on the PET surface for all three enzymes. No distinct contributions from specific ligand binding in the active site could be identified, which points towards adsorption predominantly driven by non-specific interactions in contrast to enzymes naturally evolved for the breakdown of insoluble polymers. However, we observed a correlation between the progression of enzymatic hydrolysis and increased binding capacity, probably due to surface modifications of the PET polymer over time. Our results provide functional insight, suggesting that rational design should target the specific ligand interaction in the active site rather than the already high, general adsorption capacity of these enzymes.
Original languageEnglish
Article number109937
JournalEnzyme and Microbial Technology
Volume152
Number of pages7
ISSN0141-0229
DOIs
Publication statusPublished - 2022

Keywords

  • Enzyme adsorption
  • PET hydrolysis
  • Langmuir isotherm
  • Cutinase
  • PET recycling
  • Plastic degradation

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