As cool as this is, the word “microplastics” is a little misleading. There are dozens of types of plastic in common use, each made from a different monomer with a different chemical linkage, of which PET is only one. The engineered protein in TFA will only work on PET and we’ll need to design new proteins for the other types of plastic. (I can help with that.)<p>The problem with enzymes eating plastic is that enzymes are small Pacman-shaped protein blobs that are maybe 10 nanometers in diameter, whereas things made of plastic like bottles or even microplastics are huge in comparison. How do you get the little Pacman jaws around the bottle to start breaking it down?<p>The research paper [1] describes the authors’ effective innovation. They make a protein where one end is a pore-forming shape, and the other end is a PET cutting (called a PETase in the jargon of the field). This way, their protein can access nooks and crannies in the macroplastic shapes, allowing tons of copies of this small enzyme to fully degrade a bottle.<p>Without this, a great deal of physical agitation is required to break down the plastics into small enough chunks that earlier Pacman enzymes could work on, increasing the time and the cost.<p>I hope we’ll see the idea of linking the enzymatic “scissors” to a protein pore be used to engineer enzymes to degrade other types of plastics in the future, as the general idea of getting the catalytic machinery into physical contact with every bit of the bottle is broadly applicable to all plastics, not just PET (which is great news)<p>1. <a href="https://phys.org/news/2023-10-scientists-artificial-protein-capable-degrading.html" rel="nofollow noreferrer">https://phys.org/news/2023-10-scientists-artificial-protein-...</a>