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Bacteroidetal cold-active and promiscuous esterases play a significant role in global polyethylene terephthalate (PET) degradation
Summary
Researchers identified new bacterial enzymes from gut-associated Bacteroidetes bacteria capable of breaking down PET plastic at cold temperatures. These cold-active plastic-degrading enzymes could be useful for developing biological solutions to plastic pollution in cold aquatic environments where microplastics accumulate.
Abstract Polyethylene terephthalate (PET) is an important synthetic polymer accumulating in nature and recent studies have identified microorganisms capable of degrading PET. While the majority of known PET hydrolases originate from the Actinobacteria and Proteobacteria, here we describe the first functional PET-active enzymes from the Bacteroidetes phylum. Using a PETase-specific Hidden-Markov-Model (HMM)-based search algorithm we identified two promiscuous and cold-active esterases derived from Aequorivita sp. (PET27) and Chryseobacterium jeonii (PET30) acting on PET foil and powder. Notably, one of the enzymes (PET30) was able to hydrolyze PET at temperatures between 4° - 30°C with a similar turnover rate compared to the well-known Ideonella sakaiensis enzyme (IsPETase). PET27 and PET30 homologues were detected in metagenomes encompassing a wide range of different global climate zones. Additional transcript abundance mapping of marine samples imply that these enzymes and source organisms play a significant role in the long-term degradation of microplastic particles and fibers.