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An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate

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 iden...

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Autores principales: 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.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2023
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10495362/
https://www.ncbi.nlm.nih.gov/pubmed/37697032
http://dx.doi.org/10.1038/s42004-023-00998-z
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author 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.
author_facet 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.
author_sort Perez-Garcia, Pablo
collection PubMed
description 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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spelling pubmed-104953622023-09-13 An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate 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. Commun Chem Article 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. Nature Publishing Group UK 2023-09-11 /pmc/articles/PMC10495362/ /pubmed/37697032 http://dx.doi.org/10.1038/s42004-023-00998-z Text en © The Author(s) 2023 https://creativecommons.org/licenses/by/4.0/Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (https://creativecommons.org/licenses/by/4.0/) .
spellingShingle Article
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.
An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title_full An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title_fullStr An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title_full_unstemmed An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title_short An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
title_sort archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC10495362/
https://www.ncbi.nlm.nih.gov/pubmed/37697032
http://dx.doi.org/10.1038/s42004-023-00998-z
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