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Comparison of the enzymatic depolymerization of polyethylene terephthalate and AkestraTM using Humicola insolens cutinase

Aristizábal-Lanza, Lucía ; Mankar, Smita V. LU ; Tullberg, Cecilia LU ; Zhang, Baozhong LU and Linares-Pastén, Javier A. LU orcid (2022) In Frontiers in Chemical Engineering 4.
Abstract
The enzymatic depolymerization of synthetic polyesters has become of great interest in recycling plastics. Most of the research in this area focuses on the depolymerization of polyethylene terephthalate (PET) due to its widespread use in various applications. However, the enzymatic activity on other commercial polyesters is less frequently investigated. Therefore, AkestraTM attracted our attention, which is a copolymer derived from PET with a partially biobased spirocyclic acetal structure. In this study, the activity of Humicola insolens cutinase (HiCut) on PET and AkestraTM films and powder was investigated. HiCut showed higher depolymerization activity on amorphous PET films than on Akestra™ films.... (More)
The enzymatic depolymerization of synthetic polyesters has become of great interest in recycling plastics. Most of the research in this area focuses on the depolymerization of polyethylene terephthalate (PET) due to its widespread use in various applications. However, the enzymatic activity on other commercial polyesters is less frequently investigated. Therefore, AkestraTM attracted our attention, which is a copolymer derived from PET with a partially biobased spirocyclic acetal structure. In this study, the activity of Humicola insolens cutinase (HiCut) on PET and AkestraTM films and powder was investigated. HiCut showed higher depolymerization activity on amorphous PET films than on Akestra™ films. However, an outstanding performance was achieved on AkestraTM powder, reaching 38% depolymerization in 235h, while only 12% for PET powder. These results are consistent with the dependence of the enzymes on the crystallinity of the polymer since Akestra™ is amorphous while the PET powder has 14% crystallinity. On the other hand, HiCut docking studies and molecular dynamic simulations (MD) suggested that the PET-derived mono (hydroxyethyl)terephthalate dimer (MHET)2 is a hydrolyzable ligand, producing terephthalic acid (TPA), while the Akestra™-derived TPA-spiroglycol ester is not, which is consistent with the depolymerization products determined experimentally. MD studies also suggest ligand-induced local conformational changes in the active site. (Less)
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author
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type
Contribution to journal
publication status
published
subject
in
Frontiers in Chemical Engineering
volume
4
article number
1048744
pages
13 pages
publisher
Frontiers Media S. A.
external identifiers
  • scopus:85151511411
ISSN
2673-2718
DOI
10.3389/fceng.2022.1048744
language
English
LU publication?
yes
id
d3f830c3-ecb4-47d3-b704-24c13eff7c8f
date added to LUP
2022-12-15 13:56:27
date last changed
2024-01-07 04:01:43
@article{d3f830c3-ecb4-47d3-b704-24c13eff7c8f,
  abstract     = {{The enzymatic depolymerization of synthetic polyesters has become of great interest in recycling plastics. Most of the research in this area focuses on the depolymerization of polyethylene terephthalate (PET) due to its widespread use in various applications. However, the enzymatic activity on other commercial polyesters is less frequently investigated. Therefore, Akestra<sup>TM</sup> attracted our attention, which is a copolymer derived from PET with a partially biobased spirocyclic acetal structure. In this study, the activity of <em>Humicola insolens</em> cutinase (HiCut) on PET and Akestra<sup>TM</sup> films and powder was investigated. HiCut showed higher depolymerization activity on amorphous PET films than on Akestra™ films. However, an outstanding performance was achieved on Akestra<sup>TM</sup> powder, reaching 38% depolymerization in 235h, while only 12% for PET powder. These results are consistent with the dependence of the enzymes on the crystallinity of the polymer since Akestra™ is amorphous while the PET powder has 14% crystallinity. On the other hand, HiCut docking studies and molecular dynamic simulations (MD) suggested that the PET-derived mono (hydroxyethyl)terephthalate dimer (MHET)<sub>2</sub> is a hydrolyzable ligand, producing terephthalic acid (TPA), while the Akestra™-derived TPA-spiroglycol ester is not, which is consistent with the depolymerization products determined experimentally. MD studies also suggest ligand-induced local conformational changes in the active site.}},
  author       = {{Aristizábal-Lanza, Lucía and Mankar, Smita V. and Tullberg, Cecilia and Zhang, Baozhong and Linares-Pastén, Javier A.}},
  issn         = {{2673-2718}},
  language     = {{eng}},
  month        = {{12}},
  publisher    = {{Frontiers Media S. A.}},
  series       = {{Frontiers in Chemical Engineering}},
  title        = {{Comparison of the enzymatic depolymerization of polyethylene terephthalate and Akestra<sup>TM</sup> using <i>Humicola insolens</i> cutinase}},
  url          = {{http://dx.doi.org/10.3389/fceng.2022.1048744}},
  doi          = {{10.3389/fceng.2022.1048744}},
  volume       = {{4}},
  year         = {{2022}},
}