Plastics are one of the versatile materials used worldwide in different applications including packaging and biomedical industries. It is estimated that only 9% of the plastic produced globally are recycled, leaving the rest to accumulate in landfill or ocean. There is a need for a potent next-generation technology to address this challenge. Recently, enzyme-based biocatalysts have emerged as a promising alternative to conventional recycling methods, as they are clean, safe and environmentally friendly. However, breaking down plastics, mainly the polyethylene terephthalate (PET), with the known enzymes has been challenging due to its high crystallinity and glass transition temperature of &gt; 80<sup>o </sup>C. Therefore, developing enzyme catalysts with improved thermostability is important to facilitate effective PET-biodegradation. In this work, we will discuss the structure-function properties of PETase and cutinase, the enzymes that catalyze PET hydrolysis using a combination of computational methods, including molecular phylogenetics, structural modelling and classical molecular dynamics simulations. Our analyses will provide novel mechanistic insights about the enzymes at molecular level and highlight important hotspots for targeted protein engineering to improve their thermal stability suitable for processing PET.

Understanding the structure-property relationships of PET-hydrolyzing enzymes for novel biocatalyst design

ACS Fall 2021

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