Assessment of IsPETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain
Wagner-Egea, Paula ; Tosi, Virginia ; Wang, Ping LU ; Grey, Carl LU
; Zhang, Baozhong
LU
and Linares-Pastén, Javier A.
LU
(2021)
In Applied Sciences (Switzerland)
11(18).
- Abstract
- Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from Ideonella sakaiensis 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The IsPETase showed remarkable activity toward PET (39% degradation of the original polyester) that was... (More)
- Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from Ideonella sakaiensis 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The IsPETase showed remarkable activity toward PET (39% degradation of the original polyester) that was higher than that toward Akestra™ (0.13%), PBT (0.25%) and PHT (0.13%) after 72 h. Thus, based on experimental data and computational analysis, we report insights into IsPETase activity on a series of terephthalate-based polyesters. Aside from that, the fusion domain (Trx) effect in the production and activity of a recombinant Trx-IsPETase is reported. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/21ab602c-6a1e-4d5b-ad00-7c6ac91cf6cd
- author
- Wagner-Egea, Paula
; Tosi, Virginia
; Wang, Ping
LU
; Grey, Carl
LU
; Zhang, Baozhong
LU
and Linares-Pastén, Javier A.
LU
- organization
- publishing date
- 2021-09-08
- type
- Contribution to journal
- publication status
- published
- subject
- keywords
- Enzymatic depolymerization, IsPETase, thioredoxin, aromatic polyesters, plastic biodegradation
- in
- Applied Sciences (Switzerland)
- volume
- 11
- issue
- 18
- article number
- 8315
- pages
- 15 pages
- publisher
- MDPI AG
- external identifiers
-
- scopus:85114701347
- ISSN
- 2076-3417
- DOI
- 10.3390/app11188315
- language
- English
- LU publication?
- yes
- id
- 21ab602c-6a1e-4d5b-ad00-7c6ac91cf6cd
- date added to LUP
- 2021-09-08 17:22:38
- date last changed
- 2025-04-04 14:42:34
@article{21ab602c-6a1e-4d5b-ad00-7c6ac91cf6cd,
abstract = {{Terephthalate polyesters such as poly(ethylene terephthalate) (PET) have been massively produced over the last few decades due to their attractive properties in multiple applications. However, due to their limited biodegradability, they have accumulated in landfills and oceans, posing an environmental threat. Enzymatic recycling technologies are predicted to generate long-term socioeconomic benefits. In the present work, we compared the IsPETase (from <i>Ideonella sakaiensis</i> 201-F6) activity on a series of polyesters, including poly(butylene) terephthalate (PBT), poly(hexamethylene) terephthalate (PHT) and Akestra™, with PET. The <i>Is</i>PETase showed remarkable activity toward PET (39% degradation of the original polyester) that was higher than that toward Akestra™ (0.13%), PBT (0.25%) and PHT (0.13%) after 72 h. Thus, based on experimental data and computational analysis, we report insights into <i>Is</i>PETase activity on a series of terephthalate-based polyesters. Aside from that, the fusion domain (Trx) effect in the production and activity of a recombinant Trx-<i>Is</i>PETase is reported.}},
author = {{Wagner-Egea, Paula and Tosi, Virginia and Wang, Ping and Grey, Carl and Zhang, Baozhong and Linares-Pastén, Javier A.}},
issn = {{2076-3417}},
keywords = {{Enzymatic depolymerization; IsPETase; thioredoxin; aromatic polyesters; plastic biodegradation}},
language = {{eng}},
month = {{09}},
number = {{18}},
publisher = {{MDPI AG}},
series = {{Applied Sciences (Switzerland)}},
title = {{Assessment of <i>Is</i>PETase-Assisted Depolymerization of Terephthalate Aromatic Polyesters and the Effect of the Thioredoxin Fusion Domain}},
url = {{http://dx.doi.org/10.3390/app11188315}},
doi = {{10.3390/app11188315}},
volume = {{11}},
year = {{2021}},
}