Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer

Plastic poses a significant environmental impact due to its chemical resilience, leading to prolonged and degradation times and resulting in widespread adverse effects on global flora and fauna. Cutinases are essential enzymes in the biodegradation process of synthetic polymers like polyethylene terephthalate (PET), which recognized organisms can break down. Here, we used molecular dynamics and binding free energy calculations to explore the interaction of nine synthetic polymers, including PET, with Cutinase from Fusarium oxysporum (FoCut). According to our findings, the polymers poly(ethylene terephthalate) (PET), poly(3-hydroxybutyrate-co-3-hydroxyhexanoate) (PHBH), poly(butylene succinate) (PBS), poly(butylene adipate-co-terephthalate) (PBAT) and poly(epsilon-caprolactone) (PCL) can bind to the Cutinase enzyme from F. oxysporum, indicating potential biodegradation activity for these polymers. PET exhibited the highest binding affinity (- 34.26 kcal/mol). Besides PET, the polymers PHBH, PBS, PBAT, and PCL also demonstrated significant affinities for the FoCut enzyme, with binding values of - 18.44, - 29.71, - 22.78, and - 22.26 kcal/mol, respectively. Additionally, analysis of the phylogenetic tree of cutinases produced by different organisms demonstrated that even though the organisms belong to different kingdoms, the cutinase from F. oxysporum (FoCut) showed biological similarity in its activity in degrading polymers with the cutinase enzyme from the bacterium Kineococcus radiotolerans and the fungus Moniliophthora roreri. Furthermore, the phylogenetic analysis demonstrated that the PETase enzyme has a very high similarity with the bacterial cutinase enzyme than with the fungal cutinase, therefore demonstrating that the PETase enzyme from Ideonella sakaiensis can easily be a modified bacterial cutinase enzyme that created a unique feature in biodegrading only the pet polymer through an evolutionary process due to its environment and its biochemical need for carbon. Our data demonstrate that bacterial cutinase enzymes have the same common ancestor as the PETase enzyme. Therefore, cutinases and PETase are interconnected through their biological similarity in biodegrading polymers. We demonstrated that important conserved regions, such as the Ser-Asp-His catalytic triad, exist in the enzyme's catalytic site and that all Cut enzymes from different organisms have the same region to couple with the polymer structures.