Skip to main content

Lund University Publications

LUND UNIVERSITY LIBRARIES

Marine PET Hydrolase (PET2) : Assessment of Terephthalate- and Indole-Based Polyester Depolymerization

Wagner-Egea, Paula ; Aristizábal-Lanza, Lucía ; Tullberg, Cecilia LU ; Wang, Ping LU ; Bernfur, Katja LU ; Grey, Carl LU ; Zhang, Baozhong LU and Linares-Pastén, Javier A. LU orcid (2023) In Catalysts 13(9).
Abstract
Enzymatic polyethylene terephthalate (PET) recycling processes are gaining interest for their low environmental impact, use of mild conditions, and specificity. Furthermore, PET hydrolase enzymes are continuously being discovered and engineered. In this work, we studied a PET hydrolase (PET2), initially characterized as an alkaline thermostable lipase. PET2 was produced in a fusion form with a 6-histidine tag in the N-terminal. The PET2 activity on aromatic terephthalate and new indole-based polyesters was evaluated using polymers in powder form. Compared with IsPETase, an enzyme derived from Ideonella sakaiensis, PET2 showed a lower PET depolymerization yield. However, interestingly, PET2 produced significantly higher polybutylene... (More)
Enzymatic polyethylene terephthalate (PET) recycling processes are gaining interest for their low environmental impact, use of mild conditions, and specificity. Furthermore, PET hydrolase enzymes are continuously being discovered and engineered. In this work, we studied a PET hydrolase (PET2), initially characterized as an alkaline thermostable lipase. PET2 was produced in a fusion form with a 6-histidine tag in the N-terminal. The PET2 activity on aromatic terephthalate and new indole-based polyesters was evaluated using polymers in powder form. Compared with IsPETase, an enzyme derived from Ideonella sakaiensis, PET2 showed a lower PET depolymerization yield. However, interestingly, PET2 produced significantly higher polybutylene terephthalate (PBT) and polyhexylene terephthalate (PHT) depolymerization yields. A clear preference was found for aromatic indole-derived polyesters over non-aromatic ones. No activity was detected on Akestra™, an amorphous copolyester with spiroacetal structures. Docking studies suggest that a narrower and more hydrophobic active site reduces its activity on PET but favors its interaction with PBT and PHT. Understanding the enzyme preferences of polymers will contribute to their effective use to depolymerize different types of polyesters. (Less)
Please use this url to cite or link to this publication:
author
; ; ; ; ; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Catalysts
volume
13
issue
9
article number
1234
publisher
MDPI AG
external identifiers
  • scopus:85172776172
ISSN
2073-4344
DOI
10.3390/catal13091234
language
English
LU publication?
yes
id
d1ee1f71-be3c-45d9-a9e6-fd9c63b396b5
date added to LUP
2023-08-24 20:30:45
date last changed
2023-11-15 04:02:06
@article{d1ee1f71-be3c-45d9-a9e6-fd9c63b396b5,
  abstract     = {{Enzymatic polyethylene terephthalate (PET) recycling processes are gaining interest for their low environmental impact, use of mild conditions, and specificity. Furthermore, PET hydrolase enzymes are continuously being discovered and engineered. In this work, we studied a PET hydrolase (PET2), initially characterized as an alkaline thermostable lipase. PET2 was produced in a fusion form with a 6-histidine tag in the N-terminal. The PET2 activity on aromatic terephthalate and new indole-based polyesters was evaluated using polymers in powder form. Compared with IsPETase, an enzyme derived from Ideonella sakaiensis, PET2 showed a lower PET depolymerization yield. However, interestingly, PET2 produced significantly higher polybutylene terephthalate (PBT) and polyhexylene terephthalate (PHT) depolymerization yields. A clear preference was found for aromatic indole-derived polyesters over non-aromatic ones. No activity was detected on Akestra™, an amorphous copolyester with spiroacetal structures. Docking studies suggest that a narrower and more hydrophobic active site reduces its activity on PET but favors its interaction with PBT and PHT. Understanding the enzyme preferences of polymers will contribute to their effective use to depolymerize different types of polyesters.}},
  author       = {{Wagner-Egea, Paula and Aristizábal-Lanza, Lucía and Tullberg, Cecilia and Wang, Ping and Bernfur, Katja and Grey, Carl and Zhang, Baozhong and Linares-Pastén, Javier A.}},
  issn         = {{2073-4344}},
  language     = {{eng}},
  month        = {{08}},
  number       = {{9}},
  publisher    = {{MDPI AG}},
  series       = {{Catalysts}},
  title        = {{Marine PET Hydrolase (PET2) : Assessment of Terephthalate- and Indole-Based Polyester Depolymerization}},
  url          = {{http://dx.doi.org/10.3390/catal13091234}},
  doi          = {{10.3390/catal13091234}},
  volume       = {{13}},
  year         = {{2023}},
}