Sourcing thermotolerant poly(ethylene terephthalate) hydrolase scaffolds from natural diversity

Erika Erickson, Japheth E. Gado, Luisana Avilán, Felicia Bratti, Richard K. Brizendine, Paul A. Cox, Raj Gill, Rosie Graham, Dong-Jin Kim, Gerhard König, William E. Michener, Saroj Poudel, Kelsey J. Ramirez, Thomas J. Shakespeare, Michael Zahn, Eric S. Boyd, Christina M. Payne, Jennifer L. DuBois, Andrew R. Pickford, Gregg T. Beckham () and John E. McGeehan ()
Additional contact information
Erika Erickson: National Renewable Energy Laboratory
Japheth E. Gado: National Renewable Energy Laboratory
Luisana Avilán: University of Portsmouth
Felicia Bratti: National Renewable Energy Laboratory
Richard K. Brizendine: National Renewable Energy Laboratory
Paul A. Cox: University of Portsmouth
Raj Gill: University of Portsmouth
Rosie Graham: University of Portsmouth
Dong-Jin Kim: BOTTLE Consortium
Gerhard König: University of Portsmouth
William E. Michener: National Renewable Energy Laboratory
Saroj Poudel: Montana State University
Kelsey J. Ramirez: National Renewable Energy Laboratory
Thomas J. Shakespeare: University of Portsmouth
Michael Zahn: University of Portsmouth
Eric S. Boyd: Montana State University
Christina M. Payne: National Science Foundation
Jennifer L. DuBois: BOTTLE Consortium
Andrew R. Pickford: BOTTLE Consortium
Gregg T. Beckham: National Renewable Energy Laboratory
John E. McGeehan: BOTTLE Consortium

Nature Communications, 2022, vol. 13, issue 1, 1-15

Abstract: Abstract Enzymatic deconstruction of poly(ethylene terephthalate) (PET) is under intense investigation, given the ability of hydrolase enzymes to depolymerize PET to its constituent monomers near the polymer glass transition temperature. To date, reported PET hydrolases have been sourced from a relatively narrow sequence space. Here, we identify additional PET-active biocatalysts from natural diversity by using bioinformatics and machine learning to mine 74 putative thermotolerant PET hydrolases. We successfully express, purify, and assay 51 enzymes from seven distinct phylogenetic groups; observing PET hydrolysis activity on amorphous PET film from 37 enzymes in reactions spanning pH from 4.5–9.0 and temperatures from 30–70 °C. We conduct PET hydrolysis time-course reactions with the best-performing enzymes, where we observe differences in substrate selectivity as function of PET morphology. We employed X-ray crystallography and AlphaFold to examine the enzyme architectures of all 74 candidates, revealing protein folds and accessory domains not previously associated with PET deconstruction. Overall, this study expands the number and diversity of thermotolerant scaffolds for enzymatic PET deconstruction.

Date: 2022
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DOI: 10.1038/s41467-022-35237-x

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