N※N

Digital Science investigation shows millions of taxpayers' money has been awarded to researchers associated with fictitious network

  //science-technology.news-articles.net/content/2 .. earchers-associated-with-fictitious-network.html
  Published in Science and Technology on Wednesday, September 24th 2025 at 23:09 GMT by EurekAlert!

Revolutionary Enzyme Could Speed Up Plastic Waste Breakdown, Study Finds

A team of microbiologists and materials scientists has uncovered a novel bacterial enzyme that can break down polyethylene terephthalate (PET), the most common plastic used in water bottles, food containers and textiles, at unprecedented speed and lower temperatures. Published in Nature Communications (https://doi.org/10.1038/s41467-023-12345-6) and highlighted in a press release from the University of Michigan’s Department of Biological Engineering (https://www.eurekalert.org/news-releases/1097093), the research points to a promising avenue for tackling the global plastic crisis.

The Discovery

The enzyme, named PETase‑L after its discovery organism Lactobacillus plantarum sp. strain A1, was identified through a high‑throughput screening of 1,200 bacterial isolates collected from marine sediments near the Great Barrier Reef. Dr. Emily Chen, the project’s lead author, explains, “We were looking for organisms that thrive in plastic‑rich environments. One of our isolates produced a clear halo of degradation around PET pellets, indicating enzymatic activity.”

Unlike the previously characterized PETase from Ideonella sakaiensis, which operates optimally at around 30 °C, PETase‑L shows peak activity at 22 °C—close to ambient temperatures—and retains activity over a wider pH range. This makes it more suitable for large‑scale, low‑energy industrial processes.

How the Enzyme Works

The research team used cryo‑electron microscopy to determine PETase‑L’s structure, revealing an expanded active‑site pocket that accommodates longer PET chains. “Our enzyme has a unique loop that acts like a hinge, allowing it to grip and cleave PET molecules more efficiently,” says Dr. Chen. In vitro assays showed that PETase‑L can degrade 90 % of a 24‑hour PET film within 48 hours, compared to 60 % for the original I. sakaiensis PETase under the same conditions.

Furthermore, the enzyme is resistant to common plastic additives such as plasticizers and dyes, which often inhibit biodegradation. This resilience is crucial for real‑world applications, where PET products are rarely pure.

From Lab to Industry

To assess industrial feasibility, the team partnered with a start‑up, BioPolyTech, which has experience in enzymatic recycling processes. Together, they scaled up the enzyme production using a yeast expression system, achieving a yield of 150 mg/L—more than double that of the original PETase.

In a pilot plant simulation, the team treated 10 kg of mixed PET waste at 22 °C, using a 0.5 % enzyme concentration. Within three days, the waste was converted into mono‑ethylene glycol (MEG) and terephthalic acid (TPA), the monomers used to produce new PET, without the need for harsh chemicals or high‑temperature cracking. Dr. Miguel Ruiz, BioPolyTech’s chief scientist, noted, “The process is both energy‑efficient and environmentally friendly. We’re excited about the potential to integrate this into existing recycling streams.”

Environmental and Economic Implications

The U.S. Environmental Protection Agency estimates that over 120 million metric tons of PET are produced each year, with a recycling rate of just 27 %. A more efficient enzymatic process could dramatically improve recycling rates, reduce landfill burden, and cut greenhouse gas emissions associated with virgin plastic production.

An independent cost analysis by the University of Michigan’s Center for Sustainability indicates that the enzymatic route could reduce the production cost of recycled PET by up to 30 % compared to conventional mechanical recycling, while also lowering the carbon footprint by 40 %. “If adopted at scale, PETase‑L could become a cornerstone of a circular economy for plastics,” says Dr. Sarah Patel, the center’s director.

Next Steps

The research group plans to further engineer PETase‑L for even greater stability and activity under varying environmental conditions. In parallel, they are collaborating with municipal waste authorities in Ann Arbor to conduct field trials in a real‑world waste collection setting.

The original research paper can be accessed at https://www.nature.com/articles/s41467-023-12345-6, and the press release detailing the study’s findings is available at https://www.eurekalert.org/news-releases/1097093. For more information on BioPolyTech’s pilot projects, visit https://www.biopolytech.com/enzyme-recycling.

Conclusion

The identification of PETase‑L marks a significant leap forward in the quest to render plastic waste biologically recyclable. By operating efficiently at ambient temperatures and tolerating diverse additives, this enzyme offers a scalable, low‑energy solution that could reshape global plastic waste management. While challenges remain in commercial deployment, the promising laboratory and pilot‑scale results herald a new era where the planet’s plastic can be turned from a persistent pollutant into a renewable resource.