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Degradation of PET microplastic particles to monomers in human serum by PETase
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An engineered enzyme, PETase, broke down PET microplastic-like particles into terephthalic acid and a related compound in human serum at 37 °C. The enzyme did not affect cell viability in lab tests. The work was done in serum samples and cell cultures, not in living subjects.
More than 8 billion tons of plastic waste has been generated, posing severe environmental consequences and health risks. Due to prolonged exposure, microplastic particles are found in human blood and other bodily fluids. Despite a lack of toxicity studies regarding microplastics, harmful effects for humans seem plausible and cannot be excluded. As small plastic particles readily translocate from the gut to body fluids, enzyme-based treatment of serum could constitute a promising future avenue to clear synthetic polymers and their corresponding oligomers via their degradation into monomers of lower toxicity than the material they originate from. Still, whereas it is known that the enzymatic depolymerization rate of synthetic polymers varies by orders of magnitude depending on the buffer and media composition, the activity of plastic-degrading enzymes in serum was unknown. Here, we report how an engineered PETase, which we show to be generally trans-selective via induced fit docking, can depolymerize two different microplastic-like substrates of the commodity polymer polyethylene terephthalate (PET) into its non-toxic monomer terephthalic acid (TPA) alongside mono(2-hydroxyethyl)terephthalate (MHET) in human serum at 37 °C. We show that the application of PETase does not influence cell viability in vitro. Our work highlights the potential of applying biocatalysis in biomedicine and represents a first step towards finding a future solution to the problem that microplastics in the bloodstream may pose.
More Papers Like This
Degradation of PET microplastic particles to monomers in human serum by PETase
AI summary Read the abstract
An engineered PETase enzyme broke crystalline PET microplastic-like particles down into their monomers in human serum at 37 °C. Enzyme activity in serum had not been measured before. The experiments were done in vitro.
Degradation of PET microplastic particles to monomers in human serum by designer enzymes
AI summary Read the abstract
Engineered PETase enzymes broke down PET microplastic-like particles into the monomer terephthalic acid in human serum at 37 °C. The experiments were done in vitro. The authors describe the result as a step toward future work on microplastics in blood.
WITHDRAWN: Degradation of PET microplastic particles to monomers in human serum by PETase
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This paper has been withdrawn from publication. The study described testing PETase enzyme degradation of PET microplastics in human serum; however, as a retracted paper its findings should not be relied upon. (Note: a separate non-withdrawn version appears elsewhere in this database as ID 40206.)
WITHDRAWN: Degradation of PET microplastic particles to monomers in human serum by PETase
AI summary Read the abstract
This record is marked as withdrawn from publication, indicating the study on degradation of PET microplastic particles to monomers in human serum has been retracted; no TLDR is generated for withdrawn publications.
Impact of Enzymatic Degradation on the Material Properties of Poly(Ethylene Terephthalate)
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This study tested whether a plastic-degrading enzyme (PETase) could break down recycled PET plastic and whether the degradation changed its material properties in ways that could affect fragmentation into microplastics. Enzyme treatment caused visible surface degradation and reduced the plastic's strength. Understanding how biological degradation alters plastic properties helps predict how PET breaks down into microplastics in the environment.
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