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Functional genomics in a microbe that degrades and metabolizes PET plastic
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This study applies functional genomics tools to characterize the molecular mechanisms by which a plastic-degrading microbe breaks down and assimilates synthetic polymers. By mapping the genes and metabolic pathways involved, the research provides a foundation for engineering microorganisms with enhanced plastic biodegradation capabilities.
Abstract Piscinibacter sakaiensis (formerly Ideonella sakaiensis ) was the first bacterial species known to both completely degrade and assimilate polyethylene terephthalate (PET). However, the absence of efficient genetic tools has limited direct engineering of this organism, forcing most efforts to rely on heterologous expression of PET-degrading enzymes in model hosts. Here, we establish foundational genetic tools to engineer P. sakaiensis . We identify a functional plasmid origin of replication, multiple new selectable markers, and a transposon system for the strain. We use these tools to construct a genome-wide, barcoded transposon mutant library for pooled high-throughput functional screens. We apply this mutant library to growth on PET and identify metabolic and physiological genes that impact PET biodegradation. We also use this library to reveal mutants with improved DNA uptake for genome engineering. Together, these advances provide a platform for functional genomics in P. sakaiensis and positions this naturally evolved plastic-degrading bacterium as an engineerable chassis for synthetic biology and sustainable materials research.
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Eco-Microbiology: Discovering Biochemical Enhancers of PET Biodegradation by Piscinibacter sakaiensis
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This paper reviews biochemical strategies for enhancing PET biodegradation by microorganisms, focusing on the discovery and engineering of plastic-degrading enzymes. The review highlights recent advances and remaining challenges in scaling up enzymatic plastic degradation for industrial applications.
Eco-microbiology: discovering biochemical enhancers of PET biodegradation by Piscinibacter sakaiensis
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Researchers are working to accelerate the biodegradation of PET plastic by Piscinibacter sakaiensis, a bacterium that naturally evolved to consume this common type of plastic. Using bioactivity screens and degradation tests, they identified a small number of biochemical conditions that more than doubled the PET biodegradation rate. The work provides a foundation for developing a fermentation process that could help address PET plastic pollution at scale.
Towards Synthetic PETtrophy: Engineering Pseudomonas putida for concurrent polyethylene terephthalate (PET) monomer metabolism and PET hydrolase expression
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Researchers engineered the bacterium Pseudomonas putida to simultaneously break down PET plastic monomers and express a PET hydrolase enzyme, enabling one-step PET degradation and growth. The engineered strain successfully metabolized both TPA and EG monomers released during PET hydrolysis. This work advances the development of microbial biocatalysts for plastic recycling and upcycling.
A mini-review on the role of PETase in polyethylene terephthalate degradation
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This mini-review summarized the structure, performance enhancement approaches, and potential applications of PETase, the enzyme from Ideonella sakaiensis discovered in 2016 that uses PET plastic as a carbon source, alongside MHETase for complete degradation into terephthalic acid and ethylene glycol. The review highlighted progress in enzyme engineering for improved PETase activity and discussed applications in bioremediation and recycling, identifying it as a key candidate for addressing the global plastic waste problem through biological degradation.
Identification of Prospective PETases Across Prokaryotes Using an in silico Approach
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Researchers used computational methods to screen prokaryotic protein sequences for PET-degrading enzyme candidates, identifying 27 potential PETases across diverse bacterial species and shortlisting three from Halopseudomonas pertucinogena, Halopseudomonas bauzanensis, and Ketobacter sp. as the most structurally and functionally similar to the well-characterized PETase from Ideonella sakaiensis.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.