An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate

• Published in: Communications chemistry Vol. 6; no. 1; pp. 193 - 13
• Main Authors: Perez-Garcia, Pablo, Chow, Jennifer, Costanzi, Elisa, Gurschke, Marno, Dittrich, Jonas, Dierkes, Robert F., Molitor, Rebecka, Applegate, Violetta, Feuerriegel, Golo, Tete, Prince, Danso, Dominik, Thies, Stephan, Schumacher, Julia, Pfleger, Christopher, Jaeger, Karl-Erich, Gohlke, Holger, Smits, Sander H. J., Schmitz, Ruth A., Streit, Wolfgang R.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group 11.09.2023; Nature Publishing Group UK; Nature Portfolio
• Subjects: Bacteria; Crystal structure; Deep sea; Degradation; Depolymerization; Enzymes; Esterases; Ferulic acid esterase; Fungi; Microorganisms; Polyethylene terephthalate; Structural analysis; Substrates; Terrestrial environments
• ISSN: 2399-3669; 2399-3669
• DOI: 10.1038/s42004-023-00998-z

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.