Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca
Abstract Summary: It is demonstrated that PET, which is usually regarded as ‘non‐biodegradable’, can effectively be depolymerized by a hydrolase from the actinomycete Thermobifida fusca . Erosion rates of 8 to 17 µm per week were obtained upon incubation at 55 °C. Lipases from Pseudomonas sp. and Ca...
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Online Access: | http://dx.doi.org/10.1002/marc.200500410 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmarc.200500410 https://onlinelibrary.wiley.com/doi/pdf/10.1002/marc.200500410 |
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crwiley:10.1002/marc.200500410 2024-10-13T14:02:52+00:00 Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca Müller, Rolf‐Joachim Schrader, Hedwig Profe, Jörn Dresler, Karolin Deckwer, Wolf‐Dieter 2005 http://dx.doi.org/10.1002/marc.200500410 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmarc.200500410 https://onlinelibrary.wiley.com/doi/pdf/10.1002/marc.200500410 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Macromolecular Rapid Communications volume 26, issue 17, page 1400-1405 ISSN 1022-1336 1521-3927 journal-article 2005 crwiley https://doi.org/10.1002/marc.200500410 2024-09-27T04:16:56Z Abstract Summary: It is demonstrated that PET, which is usually regarded as ‘non‐biodegradable’, can effectively be depolymerized by a hydrolase from the actinomycete Thermobifida fusca . Erosion rates of 8 to 17 µm per week were obtained upon incubation at 55 °C. Lipases from Pseudomonas sp. and Candida antarctica did not degrade PET under comparable conditions. The influences of crystallinity, melting point, and glass transition temperature on the enzymatic attack on PET, PBT, and PHB are discussed. Outline of the degradation of PET. image Outline of the degradation of PET. Article in Journal/Newspaper Antarc* Antarctica Wiley Online Library Macromolecular Rapid Communications 26 17 1400 1405 |
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Wiley Online Library |
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crwiley |
language |
English |
description |
Abstract Summary: It is demonstrated that PET, which is usually regarded as ‘non‐biodegradable’, can effectively be depolymerized by a hydrolase from the actinomycete Thermobifida fusca . Erosion rates of 8 to 17 µm per week were obtained upon incubation at 55 °C. Lipases from Pseudomonas sp. and Candida antarctica did not degrade PET under comparable conditions. The influences of crystallinity, melting point, and glass transition temperature on the enzymatic attack on PET, PBT, and PHB are discussed. Outline of the degradation of PET. image Outline of the degradation of PET. |
format |
Article in Journal/Newspaper |
author |
Müller, Rolf‐Joachim Schrader, Hedwig Profe, Jörn Dresler, Karolin Deckwer, Wolf‐Dieter |
spellingShingle |
Müller, Rolf‐Joachim Schrader, Hedwig Profe, Jörn Dresler, Karolin Deckwer, Wolf‐Dieter Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
author_facet |
Müller, Rolf‐Joachim Schrader, Hedwig Profe, Jörn Dresler, Karolin Deckwer, Wolf‐Dieter |
author_sort |
Müller, Rolf‐Joachim |
title |
Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
title_short |
Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
title_full |
Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
title_fullStr |
Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
title_full_unstemmed |
Enzymatic Degradation of Poly(ethylene terephthalate): Rapid Hydrolyse using a Hydrolase from T. fusca |
title_sort |
enzymatic degradation of poly(ethylene terephthalate): rapid hydrolyse using a hydrolase from t. fusca |
publisher |
Wiley |
publishDate |
2005 |
url |
http://dx.doi.org/10.1002/marc.200500410 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fmarc.200500410 https://onlinelibrary.wiley.com/doi/pdf/10.1002/marc.200500410 |
genre |
Antarc* Antarctica |
genre_facet |
Antarc* Antarctica |
op_source |
Macromolecular Rapid Communications volume 26, issue 17, page 1400-1405 ISSN 1022-1336 1521-3927 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/marc.200500410 |
container_title |
Macromolecular Rapid Communications |
container_volume |
26 |
container_issue |
17 |
container_start_page |
1400 |
op_container_end_page |
1405 |
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1812819323430895616 |