Comparative biochemistry of four polyester (PET) hydrolases

Jenny Arnling Bååth, Kim Borch, Kenneth Jensen, Jesper Brask, Peter Westh*

*Corresponding author for this work

Research output: Contribution to journalJournal articleResearchpeer-review

Abstract

The potential of bioprocessing in a circular plastic economy has strongly stimulated research in enzymatic degradation of different synthetic polymers. Particular interest has been devoted to the commonly used polyester, poly(ethylene terephthalate) (PET), and  a number of PET hydrolases have been described. However, a kinetic framework for comparisons of PET hydrolases (or other plastic degrading enzymes) acting on the insoluble substrate, has not been established. Here, we propose such a framework and test it against kinetic measurements on four PET hydrolases. The analysis provided values of kcat and KM, as well as an apparent specificity constant in the conventional units of M-1s-1. These parameters, together with experimental values for the number of enzyme attack sites on the PET surface, enabled comparative analyses. A variant of the PET hydrolase from Ideonella sakaiensis was the most efficient enzyme at ambient conditions, which relied on a high kcat rather than a low KM. Moreover, both soluble and insoluble PET fragments were consistently hydrolyzed much faster than intact PET. This suggests that interactions between polymer strands slow down PET degradation, while the chemical steps of catalysis and the low accessibility associated with solid substrate were less important for the overall rate. Finally, the investigated enzymes showed a remarkable substrate affinity, and reached half the saturation rate on PET, when the concentration of attack sites in the suspensi.
Original languageEnglish
JournalChembiochem
ISSN1439-4227
DOIs
Publication statusAccepted/In press - 2021

Keywords

  • Enzyme kinetics
  • Michaelis-menten
  • Cutinase
  • PET hydrolase
  • Serine esterase
  • Enzyme turnover
  • Enzyme degradation
  • Biotechnology
  • Interfacial enzymology
  • Heterogeneous catalysis

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