The Role of Binding Modules in Enzymatic Poly(ethylene Terephthalate) Hydrolysis at High Solids Loadings

Rosie Graham, Erika Erickson, Richard Brizendine, Davinia Salvachua, William Michener, Yaohao Li, Zhongping Tan, Gregg Beckham, John McGeehan, Andrew Pickford

Research output: Contribution to journalArticlepeer-review

19 Scopus Citations

Abstract

In nature, enzymes that deconstruct biological polymers, such as cellulose and chitin, often exhibit multi-domain architectures, comprising a catalytic domain and a non-catalytic binding module; the latter serves to increase the enzyme concentration at the substrate surface. This multi-domain architecture has been shown to improve the hydrolysis of poly(ethylene terephthalate) (PET) using engineered cutinase enzymes. Here, we examine the role of accessory binding modules at industrially relevant PET solids loadings necessary for cost-effective enzymatic recycling. Using a thermostable variant of leaf compost cutinase (LCC), we produced synthetic fusion constructs of LCC with five type A carbohydrate-binding modules (CBMs). At solids loadings below 10 wt %, the CBMs improve aromatic monomer yield from PET, but above this threshold, conversion extents up to 97% are reached with no added benefits from the presence of CBM fusions. This suggests that fusion constructs with the herein studied CBMs are not necessary for industrial enzymatic PET recycling.

Original languageAmerican English
Pages (from-to)2644-2657
Number of pages14
JournalChem Catalysis
Volume2
Issue number10
DOIs
StatePublished - 2022

Bibliographical note

Publisher Copyright:
© 2022 The Author(s)

NREL Publication Number

  • NREL/JA-2800-83097

Keywords

  • carbohydrate-binding module
  • chemical recycling
  • cutinase
  • enzymatic recycling
  • enzyme chimera
  • interfacial biocatalysis
  • PETase
  • plastics
  • polyester
  • SDG9: Industry innovation and infrastructure

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