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; Stamatina Vouyiouka; Evangelos Topakas

doi:10.1016/j.jhazmat.2023.131574

Discovery of a polyesterase from Deinococcus maricopensis and comparison to the benchmark LCC^ICCG suggests high potential for semi-crystalline post-consumer PET degradation

J Hazard Mater. 2023 Aug 5:455:131574. doi: 10.1016/j.jhazmat.2023.131574. Epub 2023 May 4.

Authors

Konstantinos Makryniotis¹, Efstratios Nikolaivits², Christina Gkountela³, Stamatina Vouyiouka³, Evangelos Topakas⁴

Affiliations

¹ Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
² Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece. Electronic address: snikolai@chemeng.ntua.gr.
³ Laboratory of Polymer Technology, School of Chemical Engineering, National Technical University of Athens, Athens, Greece.
⁴ Industrial Biotechnology & Biocatalysis Group, Biotechnology Laboratory, School of Chemical Engineering, National Technical University of Athens, Athens, Greece. Electronic address: vtopakas@chemeng.ntua.gr.

PMID: 37150100
DOI: 10.1016/j.jhazmat.2023.131574

Abstract

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 LCC^ICCG, 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 LCC^ICCG. 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 LCC^ICCG 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.

Keywords: LCC; PET crystallinity; PETase; Plastic biodegradation; Post-consumer PET degradation.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Benchmarking*
Environmental Pollution*
Hydrolases / metabolism
Plastics*
Polyethylene Terephthalates* / chemistry

Substances

Hydrolases
Plastics
Polyethylene Terephthalates

Supplementary concepts

Deinococcus maricopensis