The DOI matches its Crossref record; 169 of the 169 references it cites were found in a registry or an index.
Mechanism-Based Design of Efficient PET Hydrolases
Open accessAbstract
Polyethylene terephthalate (PET) is the most widespread synthetic polyester, having been utilized in textile fibers and packaging materials for beverages and food, contributing considerably to the global solid waste stream and environmental plastic pollution. While enzymatic PET recycling and upcycling have recently emerged as viable disposal methods for a circular plastic economy, only a handful of benchmark enzymes have been thoroughly described and subjected to protein engineering for improved properties over the last 16 years. By analyzing the specific material properties of PET and the reaction mechanisms in the context of interfacial biocatalysis, this Perspective identifies several limitations in current enzymatic PET degradation approaches. Unbalanced enzyme-substrate interactions, limited thermostability, and low catalytic efficiency at elevated reaction temperatures, and inhibition caused by oligomeric degradation intermediates still hamper industrial applications that require high catalytic efficiency. To overcome these limitations, successful protein engineering studies using innovative experimental and computational approaches have been published extensively in recent years in this thriving research field and are summarized and discussed in detail here. The acquired knowledge and experience will be applied in the near future to address plastic waste contributed by other mass-produced polymer types (e.g., polyamides and polyurethanes) that should also be properly disposed by biotechnological approaches.
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Cited by
An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
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Metadata
- Authors
- Wei, R., von Haugwitz, G., Pfaff, L., Mican, J., Badenhorst, C. P. S., Liu, W., Weber, G., Austin, H. P., Bednar, D., Damborsky, J., & Bornscheuer, U. T.
- Venue
- ACS Catalysis
- Publisher
- American Chemical Society (ACS)
- Published
- 2022-02-28
- Volume
- 12
- Issue
- 6
- Pages
- 3382-3396
- ISSN
- 2155-5435 (ISSN-L)
- OpenAlex
- W4214674682
- Cited by
- 284
- References
- 169
- FWCI
- 15.40
- Type
- journal article
- Language
- en
- Open access
- hybrid
- Funders
- Ministerstvo ?kolstv?, Ml?de?e a Telov?chovy (CZ.02.1.01/0.0/0.0/16_026/0008451)
- H2020 Industrial Leadership (870294, 953214)
- Horizon 2020 Framework Programme (857560)
- Alexander von Humboldt-Stiftung
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- Wei, R., von Haugwitz, G., Pfaff, L., Mican, J., Badenhorst, C. P. S., Liu, W., Weber, G., Austin, H. P., Bednar, D., Damborsky, J., & Bornscheuer, U. T. (2022). Mechanism-Based Design of Efficient PET Hydrolases. ACS Catalysis. https://doi.org/10.1021/acscatal.1c05856
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