Harry P. Austin

TL;DR: 3D structure of a newly discovered enzyme that can digest highly crystalline PET, the primary material used in the manufacture of single-use plastic beverage bottles, in some clothing, and in carpets is characterized and it is shown that PETase degrades another semiaromatic polyester, polyethylene-2,5-furandicarboxylate (PEF), which is an emerging, bioderived PET replacement with improved barrier properties.

TL;DR: The characterization of the MHETase enzyme and synergy of the two-enzyme PET depolymerization system may inform enzyme cocktail-based strategies for plastics upcycling and will inform future efforts in the biological deconstruction andUpcycling of mixed plastics.

TL;DR: Analysis of the specific material properties of PET and the reaction mechanisms in the context of interfacial biocatalysis identifies several limitations in current enzymatic PET degradation approaches that should be addressed in the near future.

TL;DR: In this paper , the authors report that concentration-dependent inhibition of IsPETase is dependent on incubation time, the solution conditions and PET surface area, and this inhibition is evident in other mesophilic PET-degrading enzymes to varying degrees.

TL;DR: In this paper, the engineered enzymes capable of degrading polymers such as polyethylene terephthalate (PET) are described and nucleic acids encoding the enzymes and cells that express the enzymes.