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Targeting microplastic particles in the void of diluted suspensions
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Researchers engineered a plastic-degrading enzyme by fusing a polymer-binding peptide to a bacterial cutinase, accelerating the breakdown of polyester-polyurethane nanoparticles by 6.7-fold and cutting the degradation half-life from 42 hours to just 6 hours. This approach of using 'anchor peptides' to direct enzymes to plastic surfaces could be a powerful strategy for breaking down microplastic and nanoplastic pollution.
Accumulation of microplastic in the environment and food chain will be a grand challenge for our society. Polyurethanes are widely used synthetic polymers in medical (e.g. catheters) and industrial products (especially as foams). Polyurethane is not abundant in nature and only a few microbial strains (fungi and bacteria) and enzymes (polyurethaneases and cutinases) have been reported to efficiently degrade polyurethane. Notably, in nature a long period of time (from 50 to >100 years depending on the literature) is required for degradation of plastics. Material binding peptides (e.g. anchor peptides) bind strongly to polymers such as polypropylene, polyethylene terephthalate, and polyurethane and can target specifically polymers. In this study we report the fusion of the anchor peptide Tachystatin A2 to the bacterial cutinase Tcur1278 which accelerated the degradation of polyester-polyurethane nanoparticles by a factor of 6.6 in comparison to wild-type Tcur1278. Additionally, degradation half-lives of polyester-polyurethane nanoparticles were reduced from 41.8 h to 6.2 h (6.7-fold) in a diluted polyester-polyurethane suspension (0.04% w/v).
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Maßgeschneiderte Adhäsionspeptide für die Funktionalisierung von natürlichen Oberflächen, Polymeren und Metalllegierungen
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Anchor peptides were developed to target enzymatic degradation of microplastic particles, with the peptide Tachystatin A2 directing the polyester-polyurethane-degrading cutinase Tcur1278 to plastic nanoparticles. This approach enhanced degradation kinetics up to six-fold and significantly reduced polymer half-life, enabling targeted microplastic breakdown in applications like wastewater treatment.
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Researchers reviewed the growing problem of microplastics and nanoplastics in the environment, then assessed enzyme-based strategies for breaking them down, finding that enzymes specifically targeting plastic polymer structures offer a promising, sustainable approach to degradation, especially when stabilized on nanomaterials to extend their activity.
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Researchers used a rapid lab technique called cell-free expression to screen enzymes that might break down polyester polyurethane plastics, sourcing the enzymes from bacteria found growing on aircraft and vehicle surfaces. They identified 10 enzymes with measurable plastic-degrading activity, though none performed as well as an established plastic-eating enzyme. This work advances the search for biological tools that could help break down microplastic pollution in the environment.
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