Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase

The accumulation of plastics in the environment has become a serious concern for the entire society. In recent years, enzyme-based biodegradation has emerged as a promising and sustainable strategy for the recycling of polyethylene terephthalate (PET), one of the most widely used polyester plastics....

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Autores: López Teijeiro, Adrián, Barreiro Piñeiro, Natalia, Eibes González, Gemma María, Martínez Costas, José Manuel
Tipo de recurso: artículo
Fecha de publicación:2025
País:España
Institución:Universidad de Santiago de Compostela (USC)
Repositorio:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
Idioma:inglés
OAI Identifier:oai:minerva.usc.gal:10347/41980
Acceso en línea:https://hdl.handle.net/10347/41980
Access Level:acceso abierto
Palabra clave:Polyethylene terephthalate (PET)
Plastic biodegradation
Post-consumer PET
PET hydrolase
LCCICCG
Enzyme immobilization
Enzyme reutilization
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spelling Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolaseLópez Teijeiro, AdriánBarreiro Piñeiro, NataliaEibes González, Gemma MaríaMartínez Costas, José ManuelPolyethylene terephthalate (PET)Plastic biodegradationPost-consumer PETPET hydrolaseLCCICCGEnzyme immobilizationEnzyme reutilizationThe accumulation of plastics in the environment has become a serious concern for the entire society. In recent years, enzyme-based biodegradation has emerged as a promising and sustainable strategy for the recycling of polyethylene terephthalate (PET), one of the most widely used polyester plastics. However, the translation of these technologies to the industrial field faces several underexplored challenges, including the immobilization and reusability of the biocatalysts. Here, we present the use of IC-Tagging as a novel one-step methodology for the “in cellulo” self-immobilization of the benchmark PET-degrading enzyme LCCICCG in protein nanospheres. The immobilized enzyme showed to be active against soluble substrates and exhibited improved thermal resistance and long-term storage stability, retaining 58 % of relative activity after 3 months at room temperature. Immobilized LCCICCG also demonstrates remarkable reusability, with minor activity loss up to 10 reuse cycles. Most importantly, nearly complete depolymerization (>90 %) of various untreated amorphous post-consumer PET materials was achieved at a wide range of temperatures (50–70 °C) by removing the products and reusing the enzyme repeatedly. Furthermore, reutilization led to almost full degradation of two consecutive batches of post-consumer PET in 6 days, outperforming all immobilized biocatalysts reported at laboratory scale. Overall, IC-Tagging emerges as a promising and versatile platform for the production, immobilization and reutilization of top-performing PET hydrolases, contributing to sustainable management of plastic waste.ElsevierUniversidade de Santiago de Compostela. Departamento de Bioquímica e Bioloxía MolecularUniversidade de Santiago de Compostela. Departamento de Enxeñaría Química20252025-05-3020252025-05-30journal articlehttp://purl.org/coar/resource_type/c_6501VoRhttp://purl.org/coar/version/c_970fb48d4fbd8a85info:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10347/41980reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostelainstname:Universidad de Santiago de Compostela (USC)InglésengAgencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-139720OB-I00 EVOLUCION DE LA TECNOLOGIA IC-TAGGING PARA LA PRODUCCION DE VACUNAS Y ENZIMAS ESTABILIZADASopen accesshttp://purl.org/coar/access_right/c_abf2© 2025 The Author(s). Published by Elsevier B.V. This is an open access article under the CC BY-NC-ND license. Attribution-NonCommercial-NoDerivatives 4.0 Internationalhttp://creativecommons.org/licenses/by-nc-nd/4.0/info:eu-repo/semantics/openAccessoai:minerva.usc.gal:10347/419802026-06-15T12:47:27Z
dc.title.none.fl_str_mv Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
title Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
spellingShingle Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
López Teijeiro, Adrián
Polyethylene terephthalate (PET)
Plastic biodegradation
Post-consumer PET
PET hydrolase
LCCICCG
Enzyme immobilization
Enzyme reutilization
title_short Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
title_full Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
title_fullStr Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
title_full_unstemmed Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
title_sort Nearly complete depolymerization of untreated post-consumer plastic with an immobilized and reusable PET hydrolase
dc.creator.none.fl_str_mv López Teijeiro, Adrián
Barreiro Piñeiro, Natalia
Eibes González, Gemma María
Martínez Costas, José Manuel
author López Teijeiro, Adrián
author_facet López Teijeiro, Adrián
Barreiro Piñeiro, Natalia
Eibes González, Gemma María
Martínez Costas, José Manuel
author_role author
author2 Barreiro Piñeiro, Natalia
Eibes González, Gemma María
Martínez Costas, José Manuel
author2_role author
author
author
dc.contributor.none.fl_str_mv Universidade de Santiago de Compostela. Departamento de Bioquímica e Bioloxía Molecular
Universidade de Santiago de Compostela. Departamento de Enxeñaría Química
dc.subject.none.fl_str_mv Polyethylene terephthalate (PET)
Plastic biodegradation
Post-consumer PET
PET hydrolase
LCCICCG
Enzyme immobilization
Enzyme reutilization
topic Polyethylene terephthalate (PET)
Plastic biodegradation
Post-consumer PET
PET hydrolase
LCCICCG
Enzyme immobilization
Enzyme reutilization
description The accumulation of plastics in the environment has become a serious concern for the entire society. In recent years, enzyme-based biodegradation has emerged as a promising and sustainable strategy for the recycling of polyethylene terephthalate (PET), one of the most widely used polyester plastics. However, the translation of these technologies to the industrial field faces several underexplored challenges, including the immobilization and reusability of the biocatalysts. Here, we present the use of IC-Tagging as a novel one-step methodology for the “in cellulo” self-immobilization of the benchmark PET-degrading enzyme LCCICCG in protein nanospheres. The immobilized enzyme showed to be active against soluble substrates and exhibited improved thermal resistance and long-term storage stability, retaining 58 % of relative activity after 3 months at room temperature. Immobilized LCCICCG also demonstrates remarkable reusability, with minor activity loss up to 10 reuse cycles. Most importantly, nearly complete depolymerization (>90 %) of various untreated amorphous post-consumer PET materials was achieved at a wide range of temperatures (50–70 °C) by removing the products and reusing the enzyme repeatedly. Furthermore, reutilization led to almost full degradation of two consecutive batches of post-consumer PET in 6 days, outperforming all immobilized biocatalysts reported at laboratory scale. Overall, IC-Tagging emerges as a promising and versatile platform for the production, immobilization and reutilization of top-performing PET hydrolases, contributing to sustainable management of plastic waste.
publishDate 2025
dc.date.none.fl_str_mv 2025
2025-05-30
2025
2025-05-30
dc.type.none.fl_str_mv journal article
http://purl.org/coar/resource_type/c_6501
VoR
http://purl.org/coar/version/c_970fb48d4fbd8a85
dc.type.openaire.fl_str_mv info:eu-repo/semantics/article
format article
dc.identifier.none.fl_str_mv https://hdl.handle.net/10347/41980
url https://hdl.handle.net/10347/41980
dc.language.none.fl_str_mv Inglés
eng
language_invalid_str_mv Inglés
language eng
dc.relation.none.fl_str_mv Agencia Estatal de Investigación http://dx.doi.org/10.13039/501100011033 Plan Estatal de Investigación Científica y Técnica y de Innovación 2021-2023 PID2022-139720OB-I00 EVOLUCION DE LA TECNOLOGIA IC-TAGGING PARA LA PRODUCCION DE VACUNAS Y ENZIMAS ESTABILIZADAS
dc.rights.none.fl_str_mv open access
http://purl.org/coar/access_right/c_abf2
http://creativecommons.org/licenses/by-nc-nd/4.0/
dc.rights.openaire.fl_str_mv info:eu-repo/semantics/openAccess
rights_invalid_str_mv open access
http://purl.org/coar/access_right/c_abf2
http://creativecommons.org/licenses/by-nc-nd/4.0/
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Elsevier
publisher.none.fl_str_mv Elsevier
dc.source.none.fl_str_mv reponame:Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
instname:Universidad de Santiago de Compostela (USC)
instname_str Universidad de Santiago de Compostela (USC)
reponame_str Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
collection Minerva. Repositorio Institucional de la Universidad de Santiago de Compostela
repository.name.fl_str_mv
repository.mail.fl_str_mv
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