Scientists are developing a new enzyme to beat plastic waste
Scientists have taken an important step in developing nature-based solutions to overcome the global crisis over plastic waste.
They have characterized an enzyme with a remarkable ability to break down terephthalate (TPA), one of the chemical building blocks of polyethylene terephthalate (PET) used in the manufacture of disposable beverage bottles, clothing and carpets.
The results of the study were published in The Proceedings of the National Academy of Sciences (PNAS).
The research was led jointly by a professor Jen DuBoisMontana State University, and Professor John McGeehan From the University of Portsmouth, who in 2018 led an international team that designed a natural enzyme that could break down PET plastic. This new study describes the next steps, especially in the management of TPA.
Professor DuBois said: “While EG is a chemical with many uses – it’s part of an antifreeze put in a car, for example – TPA doesn’t have many uses outside of PET, and it’s not something that most bacteria can even digest. The Portsmouth team however, revealed that an enzyme from PET-consuming bacteria recognizes TPA like a glove in our hand. Our group at MSU then showed that this enzyme called TPADO degrades TPA and almost only TPA with amazing efficiency. “
With more than 400 million tonnes of plastic waste generated each year, most of which ends up in landfills, it is hoped that this work will open the door to improving bacterial enzymes such as TPADO. This will help meet the challenge of plastic pollution and develop biological systems that can turn plastic waste into valuable products.
Professor McGeehan, director of the University’s Center for Enzyme Innovation, said: “Incredible progress has been made in recent years in designing enzymes that break down PET plastic into its building blocks. make use of these durable chemicals and materials, which are essential for the production of valuable products from plastic waste. “
Professor McGeehan concluded, “Using the powerful X-ray of the diamond light source, we were able to create a detailed 3D structure of the TPADO enzyme that reveals how it performs this crucial reaction. This gives researchers a plan for faster and more efficient design. Versions of this complex enzyme.”
Source: ANI