Plastic is a synthetic polymer with high material properties found in all aspects of modern life. Due to its numerous applications, plastic has become a threat to the environment and human health through ineffective plastic waste management. The current mechanical recycling approaches do not achieve the full circling of the materials due to inferior properties of the recycled products. Petroleum-derived Polyethylene terephthalate (PET) is the third most widely used synthetic polymer utilized in textiles, fibers, film, single-use bottles, and packaging materials. Plastic upcycling is depolymerizing PET into higher-value products. Microorganism enzyme catalyzed PET depolymerization is shown to be a promising route for plastic upcycling. While the search for novel enzymes continues, two important problems related to previously discovered enzymes are of current interest; increasing the enzyme’s thermal stability and exploring ways to improve the crystalline PET degradation efficiency by structural modifications. Recent studies found that the PET degradation efficiency of Leafbranch Compost Cutinase (LCC) can be enhanced by active site mutations. Thermal stability of mutated LCC is achieved by adding disulfide bonds at the active site. In the present work, based on the results from Molecular Docking and Molecular Dynamics simulations with in vivo and in vitro experiments, we will present the effect of metal-site substitutions by divalent ions on the thermal stability and catalytic activity of already suggested engineered LCC configurations.

Investigation of the effect of metal-site substitutions on thermal stability and polyethylene terephthalate (PET) depolymerization activity on leaf-branch compost cutinase (LCC)

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