An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate.
Journal
Communications chemistry
ISSN: 2399-3669
Titre abrégé: Commun Chem
Pays: England
ID NLM: 101725670
Informations de publication
Date de publication:
11 Sep 2023
11 Sep 2023
Historique:
received:
22
02
2023
accepted:
31
08
2023
medline:
12
9
2023
pubmed:
12
9
2023
entrez:
11
9
2023
Statut:
epublish
Résumé
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.
Identifiants
pubmed: 37697032
doi: 10.1038/s42004-023-00998-z
pii: 10.1038/s42004-023-00998-z
pmc: PMC10495362
doi:
Types de publication
Journal Article
Langues
eng
Pagination
193Subventions
Organisme : European Commission (EC)
ID : 101000327
Organisme : Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)
ID : 031B867B
Organisme : Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)
ID : 031B867F
Organisme : Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)
ID : 031B0837B
Organisme : Bundesministerium für Bildung und Forschung (Federal Ministry of Education and Research)
ID : 031B0837A
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : 417919780
Organisme : Deutsche Forschungsgemeinschaft (German Research Foundation)
ID : INST 208/740-1 FUGG
Informations de copyright
© 2023. Springer Nature Limited.
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