School of Life Science, Beijing Institute of Technology, Beijing 100081, PR China.
School of Life Science, Beijing Institute of Technology, Beijing 100081, PR China.
J Hazard Mater. 2024 Dec 5;480:136159. doi: 10.1016/j.jhazmat.2024.136159. Epub 2024 Oct 17.
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®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.
虽然已经从土壤或堆肥中的各种微生物中鉴定出了许多聚氨酯(PU)降解酶,但研究是否可以在其他生物环境中发现新型的 PU 降解酶仍然很有趣。本研究报告了一种来自于嗜塑菌(Mixta tenebrionis)BIT-26 的酶(MTL)的发现,这种酶可以降解 PU 塑料,该菌分离自食用塑料的黄粉虫的肠道。MTL 对三种商业 PU 基质(Impranil®DLN-SD、热塑性薄膜(PEGA-HDI)和热固性泡沫(PEGA-TDI))表现出显著的降解活性,通过切断聚酯多元醇部分的酯键来实现。结构、分子对接和定点突变分析阐明了底物结合模型。基于结构的比较和突变研究的组合揭示了酶特异性的基础结构。这些发现为理解塑料食性昆虫肠道中的塑料代谢提供了新的视角,并为开发塑料废物处理的生物降解技术提供了一个有前景的途径。