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Sub-micro- and nano-sized polyethylene terephthalate deconstruction with engineered protein nanopores
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Researchers engineered protein nanopores — tiny molecular tunnels — capable of breaking down nano-sized PET plastic (a common plastic found in bottles and packaging) under mild conditions. While these nanoreactors cannot degrade large plastic pieces, they show promise for filtering and destroying nanoplastics in wastewater treatment, where conventional methods fall short.
Abstract The identification or design of biocatalysts to mitigate the accumulation of plastics, including sub-micro- and nano-sized polyethylene terephthalate (nPET), is becoming a global challenge. Here we computationally incorporated two hydrolytic active sites with geometries similar to that of Idionella sakaiensis PET hydrolase, to fragaceatoxin C (FraC), a membrane pore-forming protein. FraC m1/m2 could be assembled into octameric nanopores (7.0 nm high × 1.6–6.0 nm entry), which deconstructed (40 °C, pH 7.0) nPET from GoodFellow, commodities and plastic bottles. FraC m1 and FraC m2 degrade nPET by endo- and exo-type chain scission. While FraC m1 produces bis(2-hydroxyethyl) terephthalate as the main product, FraC m2 yields a high diversity of oligomers and terephthalic acid. Mechanistic and biochemical differences with benchmark PET hydrolases, along with pore and nPET dynamics, suggest that these pore-forming protein catalytic nanoreactors do not deconstruct macro-PET but are promising in nanotechnology for filtering, capturing and breaking down nPET, for example, in wastewater treatment plants.
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