Ru_2024_J.Hazard.Mater_480_136159

Although numerous polyurethane (PU)-degrading enzymes were identified from a diverse array of microorganisms in soil or compost, it is intriguing to investigate whether novel PU-degrading enzymes can be discovered in other biological environments. This study reports the discovery of an enzyme (MTL) for PU plastic degradation from the bacterial strain Mixta tenebrionis BIT-26, isolated from the gut of plastic-eating mealworms. MTL shows significant degradation activity towards three commercial PU substrates, including Impranil(a)DLN-SD, thermoplastic films (PEGA-HDI), and thermoset foams (PEGA-TDI), by cleaving the ester bonds in the polyester polyol moieties. The structure, molecular docking, and site-directed mutagenesis analyses elucidate the substrate binding model. A combination of structure-based comparison and mutational studies reveals the underlying architecture of the enzyme's specificity. These findings provide a fresh perspective into understanding plastic metabolism in the gut of plastic-eating insects and a prospective path for developing a biodegradation technique for plastic waste disposal.