Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures
Polyethylene terephthalate (PET) is one of the most widely used synthetic plastics in the packaging industry, and consequently has become one of the main components of plastic waste found in the environment. However, several microorganisms have been described to encode enzymes that catalyze the depo...
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ftpubmed:oai:pubmedcentral.nih.gov:8752145 2023-05-15T13:38:34+02:00 Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures Blázquez-Sánchez, Paula Engelberger, Felipe Cifuentes-Anticevic, Jerónimo Sonnendecker, Christian Griñén, Aransa Reyes, Javiera Díez, Beatriz Guixé, Victoria Richter, P. Konstantin Zimmermann, Wolfgang Ramírez-Sarmiento, César A. 2022-01-11 http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8752145/ http://www.ncbi.nlm.nih.gov/pubmed/34705547 https://doi.org/10.1128/AEM.01842-21 en eng American Society for Microbiology http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8752145/ http://www.ncbi.nlm.nih.gov/pubmed/34705547 http://dx.doi.org/10.1128/AEM.01842-21 Copyright © 2022 American Society for Microbiology. https://doi.org/10.1128/ASMCopyrightv2All Rights Reserved (https://doi.org/10.1128/ASMCopyrightv2) . Appl Environ Microbiol Enzymology and Protein Engineering Text 2022 ftpubmed https://doi.org/10.1128/AEM.01842-21 2022-07-31T00:31:47Z Polyethylene terephthalate (PET) is one of the most widely used synthetic plastics in the packaging industry, and consequently has become one of the main components of plastic waste found in the environment. However, several microorganisms have been described to encode enzymes that catalyze the depolymerization of PET. While most known PET hydrolases are thermophilic and require reaction temperatures between 60°C and 70°C for an efficient hydrolysis of PET, a partial hydrolysis of amorphous PET at lower temperatures by the polyester hydrolase IsPETase from the mesophilic bacterium Ideonella sakaiensis has also been reported. We show that polyester hydrolases from the Antarctic bacteria Moraxella sp. strain TA144 (Mors1) and Oleispira antarctica RB-8 (OaCut) were able to hydrolyze the aliphatic polyester polycaprolactone as well as the aromatic polyester PET at a reaction temperature of 25°C. Mors1 caused a weight loss of amorphous PET films and thus constitutes a PET-degrading psychrophilic enzyme. Comparative modeling of Mors1 showed that the amino acid composition of its active site resembled both thermophilic and mesophilic PET hydrolases. Lastly, bioinformatic analysis of Antarctic metagenomic samples demonstrated that members of the Moraxellaceae family carry candidate genes coding for further potential psychrophilic PET hydrolases. IMPORTANCE A myriad of consumer products contains polyethylene terephthalate (PET), a plastic that has accumulated as waste in the environment due to its long-term stability and poor waste management. One promising solution is the enzymatic biodegradation of PET, with most known enzymes only catalyzing this process at high temperatures. Here, we bioinformatically identified and biochemically characterized an enzyme from an Antarctic organism that degrades PET at 25°C with similar efficiency to the few PET-degrading enzymes active at moderate temperatures. Reasoning that Antarctica harbors other PET-degrading enzymes, we analyzed available data from Antarctic metagenomic samples ... Text Antarc* Antarctic Antarctica PubMed Central (PMC) Antarctic The Antarctic Applied and Environmental Microbiology 88 1 |
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English |
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Enzymology and Protein Engineering |
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Enzymology and Protein Engineering Blázquez-Sánchez, Paula Engelberger, Felipe Cifuentes-Anticevic, Jerónimo Sonnendecker, Christian Griñén, Aransa Reyes, Javiera Díez, Beatriz Guixé, Victoria Richter, P. Konstantin Zimmermann, Wolfgang Ramírez-Sarmiento, César A. Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
topic_facet |
Enzymology and Protein Engineering |
description |
Polyethylene terephthalate (PET) is one of the most widely used synthetic plastics in the packaging industry, and consequently has become one of the main components of plastic waste found in the environment. However, several microorganisms have been described to encode enzymes that catalyze the depolymerization of PET. While most known PET hydrolases are thermophilic and require reaction temperatures between 60°C and 70°C for an efficient hydrolysis of PET, a partial hydrolysis of amorphous PET at lower temperatures by the polyester hydrolase IsPETase from the mesophilic bacterium Ideonella sakaiensis has also been reported. We show that polyester hydrolases from the Antarctic bacteria Moraxella sp. strain TA144 (Mors1) and Oleispira antarctica RB-8 (OaCut) were able to hydrolyze the aliphatic polyester polycaprolactone as well as the aromatic polyester PET at a reaction temperature of 25°C. Mors1 caused a weight loss of amorphous PET films and thus constitutes a PET-degrading psychrophilic enzyme. Comparative modeling of Mors1 showed that the amino acid composition of its active site resembled both thermophilic and mesophilic PET hydrolases. Lastly, bioinformatic analysis of Antarctic metagenomic samples demonstrated that members of the Moraxellaceae family carry candidate genes coding for further potential psychrophilic PET hydrolases. IMPORTANCE A myriad of consumer products contains polyethylene terephthalate (PET), a plastic that has accumulated as waste in the environment due to its long-term stability and poor waste management. One promising solution is the enzymatic biodegradation of PET, with most known enzymes only catalyzing this process at high temperatures. Here, we bioinformatically identified and biochemically characterized an enzyme from an Antarctic organism that degrades PET at 25°C with similar efficiency to the few PET-degrading enzymes active at moderate temperatures. Reasoning that Antarctica harbors other PET-degrading enzymes, we analyzed available data from Antarctic metagenomic samples ... |
format |
Text |
author |
Blázquez-Sánchez, Paula Engelberger, Felipe Cifuentes-Anticevic, Jerónimo Sonnendecker, Christian Griñén, Aransa Reyes, Javiera Díez, Beatriz Guixé, Victoria Richter, P. Konstantin Zimmermann, Wolfgang Ramírez-Sarmiento, César A. |
author_facet |
Blázquez-Sánchez, Paula Engelberger, Felipe Cifuentes-Anticevic, Jerónimo Sonnendecker, Christian Griñén, Aransa Reyes, Javiera Díez, Beatriz Guixé, Victoria Richter, P. Konstantin Zimmermann, Wolfgang Ramírez-Sarmiento, César A. |
author_sort |
Blázquez-Sánchez, Paula |
title |
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
title_short |
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
title_full |
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
title_fullStr |
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
title_full_unstemmed |
Antarctic Polyester Hydrolases Degrade Aliphatic and Aromatic Polyesters at Moderate Temperatures |
title_sort |
antarctic polyester hydrolases degrade aliphatic and aromatic polyesters at moderate temperatures |
publisher |
American Society for Microbiology |
publishDate |
2022 |
url |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8752145/ http://www.ncbi.nlm.nih.gov/pubmed/34705547 https://doi.org/10.1128/AEM.01842-21 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic Antarctica |
genre_facet |
Antarc* Antarctic Antarctica |
op_source |
Appl Environ Microbiol |
op_relation |
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC8752145/ http://www.ncbi.nlm.nih.gov/pubmed/34705547 http://dx.doi.org/10.1128/AEM.01842-21 |
op_rights |
Copyright © 2022 American Society for Microbiology. https://doi.org/10.1128/ASMCopyrightv2All Rights Reserved (https://doi.org/10.1128/ASMCopyrightv2) . |
op_doi |
https://doi.org/10.1128/AEM.01842-21 |
container_title |
Applied and Environmental Microbiology |
container_volume |
88 |
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1 |
_version_ |
1766107842501148672 |