Journal Article

FZJ-2023-03512

http://join2-wiki.gsi.de/foswiki/pub/Main/Artwork/join2_logo100x88.png An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate

Perez-Garcia, P. ; Chow, J. ; Costanzi, E. ; Gurschke, M. ; Dittrich, J. ; Dierkes, R. F. ; Molitor, R.FZJ* ; Applegate, V. ; Feuerriegel, G. ; Tete, P. ; Danso, D. ; Thies, S.FZJ* ; Schumacher, J. ; Pfleger, C. ; Jaeger, K.-E.FZJ* ; Gohlke, H.FZJ* ; Smits, S. H. J. ; Schmitz, R. A. (Corresponding author) ; Streit, W. R. (Corresponding author)

2023
Macmillan Publishers Limited, part of Springer Nature [London]

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Please use a persistent id in citations: doi:10.1038/s42004-023-00998-z  doi:10.34734/FZJ-2023-03512

Abstract: Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 80 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme had been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46 (RLI42440.1), an archaeal promiscuous feruloyl esterase exhibiting degradation activity on semi-crystalline PET powder comparable to IsPETase and LCC (wildtypes), and higher activity on bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, is derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 Å. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a plant cell wall-degrading esterase.

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Contributing Institute(s):

1. Bioinformatik (IBG-4)
2. Institut für Molekulare Enzymtechnologie (HHUD) (IMET)

Research Program(s):

1. 2171 - Biological and environmental resources for sustainable use (POF4-217) (POF4-217)
2. DFG project 417919780 - Zentrum für strukturelle Studien (417919780) (417919780)

Appears in the scientific report 2023

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