Characterization and engineering of a plastic-degrading aromatic polyesterase

2018 Proceedings of the National Academy of Sciences 974 citations

Abstract

Significance Synthetic polymers are ubiquitous in the modern world but pose a global environmental problem. While plastics such as poly(ethylene terephthalate) (PET) are highly versatile, their resistance to natural degradation presents a serious, growing risk to fauna and flora, particularly in marine environments. Here, we have characterized the 3D structure of a newly discovered enzyme that can digest highly crystalline PET, the primary material used in the manufacture of single-use plastic beverage bottles, in some clothing, and in carpets. We engineer this enzyme for improved PET degradation capacity and further demonstrate that it can also degrade an important PET replacement, polyethylene-2,5-furandicarboxylate, providing new opportunities for biobased plastics recycling.

Keywords

CutinasePolyesterBiodegradationPolyethylene terephthalateHydrolaseProtein engineeringPolymerMaterials scienceChemistryEnzymeBiologyBiochemistryOrganic chemistry

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Publication Info

Year
2018
Type
article
Volume
115
Issue
19
Pages
E4350-E4357
Citations
974
Access
Closed

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Harry P. Austin, Mark D. Allen, Bryon S. Donohoe et al. (2018). Characterization and engineering of a plastic-degrading aromatic polyesterase. Proceedings of the National Academy of Sciences , 115 (19) , E4350-E4357. https://doi.org/10.1073/pnas.1718804115

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DOI
10.1073/pnas.1718804115