Journal article Embargoed Access
Discovery of a polyesterase from Deinococcus maricopensis and comparison to the benchmark LCCICCG suggests high potential for semi- crystalline post-consumer PET degradation
Konstantinos Makryniotis;
Efstratios Nikolaivits;
Christina Gkountela;
Stamina Vouyiouka;
Evangelos Topakas
Plastic pollution remains a significant environmental challenge, with conventional waste management strategies proving insufficient in addressing the problem. Enzymatic degradation has emerged as a promising alternative, with LCCICCG, an engineered metagenome-derived cutinase, being the most effective in degrading polyethylene terephthalate (PET), the most commonly produced and discarded polyester. However, more efficient PET-hydrolases are needed for the upscaling of a PET-waste biorefinery. In this regard, the study reports the characterization of a novel, phylogenetically distinct, thermophilic polyesterase from Deinococcus maricopensis (DmPETase) and its comparison to LCCICCG. DmPETase is capable of degrading various synthetic polymers, including PET, polyurethane, as well as four semi- crystalline aliphatic polyesters. DmPETase was found to be comparable to LCCICCG at 50 °C in degrading semi-crystalline sections of post-consumer PET bottles, but it appeared to be less sensitive to crystallinity degree increase. This property makes DmPETase a new template for protein engineering endeavors to create an efficient biocatalyst to be integrated into the bio-recycling process of PET waste, without the need for amorphization of the materials.
Embargoed Access
Files are currently under embargo but will be publicly accessible after November 3, 2023.
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- Publication date:
- May 2, 2023
- DOI:
-
- Keyword(s):
- PETase; LCC; post-consumer PET degradation; plastic biodegradation; PET crystallinity
- Grants:
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European Commission:
- BioICEP - Bio Innovation of a Circular Economy for Plastics (870292)
- License (for files):
- Creative Commons Attribution 4.0 International