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The first archaeal PET-degrading enzyme belongs to the feruloyl-esterase family
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Researchers discovered the first archaeal enzyme capable of degrading polyethylene terephthalate (PET) plastic, belonging to the feruloyl-esterase family. Previously, all known plastic-degrading enzymes came from bacteria or fungi. This finding opens new possibilities for using microorganisms from extreme environments in plastic biodegradation and recycling.
ABSTRACT Polyethylene terephthalate (PET) is a commodity polymer known to globally contaminate marine and terrestrial environments. Today, around 40 bacterial and fungal PET-active enzymes (PETases) are known, originating from four bacterial and two fungal phyla. In contrast, no archaeal enzyme has been identified to degrade PET. Here we report on the structural and biochemical characterization of PET46, an archaeal promiscuous feruloyl esterase exhibiting degradation activitiy on PET, bis-, and mono-(2-hydroxyethyl) terephthalate (BHET and MHET). The enzyme, found by a sequence-based metagenome search, was derived from a non-cultivated, deep-sea Candidatus Bathyarchaeota archaeon. Biochemical characterization demonstrated that PET46 is a promiscuous, heat-adapted hydrolase. Its crystal structure was solved at a resolution of 1.71 Å. It shares the core alpha/beta-hydrolase fold with bacterial PETases, but contains a unique lid common in feruloyl esterases, which is involved in substrate binding. Thus, our study significantly widens the currently known diversity of PET-hydrolyzing enzymes, by demonstrating PET depolymerization by a lignin-degrading esterase.
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An archaeal lid-containing feruloyl-esterase degrades polyethylene terephthalate (PET)
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This study identified the first archaeal enzyme capable of degrading PET plastic, characterizing its structure and biochemical properties. Expanding the diversity of organisms with PET-degrading enzymes could accelerate the development of biological strategies for breaking down the microplastics contaminating marine and terrestrial environments.
An archaeal lid-containing feruloyl esterase degrades polyethylene terephthalate
AI summary Read the abstract
Researchers identified the first known archaeal enzyme capable of degrading polyethylene terephthalate (PET), a major plastic pollutant found worldwide. The enzyme, called PET46, comes from a deep-sea archaeon and showed degradation activity on PET comparable to previously known bacterial enzymes. The study expands the known diversity of plastic-degrading enzymes and suggests that organisms from extreme environments may harbor useful tools for addressing plastic pollution.
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Scientists have found that ancient microbes called archaea, which thrive in extreme places like deep-sea trenches, produce enzymes that can break down tough plastics like PET (used in bottles) — sometimes as well as or better than bacteria currently being studied for plastic cleanup. This matters because plastic pollution, including microplastics now found in oceans, soil, and even our bodies, is notoriously hard to break down, and these newly discovered microbes could offer fresh tools for tackling plastic waste in places previously thought too harsh for biological cleanup. This paper reviews existing research on the topic rather than presenting new
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