Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization
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), initi...
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MDPI AG
2023-08-01
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| author | Paula Wagner-Egea Lucía Aristizábal-Lanza Cecilia Tullberg Ping Wang Katja Bernfur Carl Grey Baozhong Zhang Javier A. Linares-Pastén |
| author_facet | Paula Wagner-Egea Lucía Aristizábal-Lanza Cecilia Tullberg Ping Wang Katja Bernfur Carl Grey Baozhong Zhang Javier A. Linares-Pastén |
| author_sort | Paula Wagner-Egea |
| collection | DOAJ |
| description | 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 <i>Is</i>PETase, an enzyme derived from <i>Ideonella sakaiensis</i>, 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. |
| first_indexed | 2024-03-10T22:56:10Z |
| format | Article |
| id | doaj.art-481b27706e584e8a8b16f8fbf2af5886 |
| institution | Directory Open Access Journal |
| issn | 2073-4344 |
| language | English |
| last_indexed | 2024-03-10T22:56:10Z |
| publishDate | 2023-08-01 |
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| spelling | doaj.art-481b27706e584e8a8b16f8fbf2af58862023-11-19T09:57:35ZengMDPI AGCatalysts2073-43442023-08-01139123410.3390/catal13091234Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester DepolymerizationPaula Wagner-Egea0Lucía Aristizábal-Lanza1Cecilia Tullberg2Ping Wang3Katja Bernfur4Carl Grey5Baozhong Zhang6Javier A. Linares-Pastén7Division of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenDivision of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenDivision of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenCentre for Analysis and Synthesis, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenDivision for Biochemistry and Structural Biology, Department of Chemistry, Lund University, P.O. Box 124, SE-22100 Lund, SwedenDivision of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenCentre for Analysis and Synthesis, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenDivision of Biotechnology, Department of Chemistry, Faculty of Engineering (LTH), Lund University, P.O. Box 124, SE-22100 Lund, SwedenEnzymatic 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 <i>Is</i>PETase, an enzyme derived from <i>Ideonella sakaiensis</i>, 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.https://www.mdpi.com/2073-4344/13/9/1234plastic biodegradationmarine PET hydrolaseenzymatic degradationindole-based polyestersPETasePET |
| spellingShingle | Paula Wagner-Egea Lucía Aristizábal-Lanza Cecilia Tullberg Ping Wang Katja Bernfur Carl Grey Baozhong Zhang Javier A. Linares-Pastén Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization Catalysts plastic biodegradation marine PET hydrolase enzymatic degradation indole-based polyesters PETase PET |
| title | Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization |
| title_full | Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization |
| title_fullStr | Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization |
| title_full_unstemmed | Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization |
| title_short | Marine PET Hydrolase (PET2): Assessment of Terephthalate- and Indole-Based Polyester Depolymerization |
| title_sort | marine pet hydrolase pet2 assessment of terephthalate and indole based polyester depolymerization |
| topic | plastic biodegradation marine PET hydrolase enzymatic degradation indole-based polyesters PETase PET |
| url | https://www.mdpi.com/2073-4344/13/9/1234 |
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