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Evaluating cutinase from Fusarium oxysporum as a biocatalyst for the degradation of nine synthetic polymer
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Researchers used computer modeling to test whether a fungal enzyme called cutinase could break down nine types of synthetic plastics, finding strong binding affinity for PET, PCL, and several biodegradable plastics — pointing toward biological tools that could help degrade plastic waste in the environment.
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(ε-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.
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Scientists used computer modeling to show that certain fungal enzymes have a similar shape and chemical "toolkit" as bacteria already known to break down plastic bottles (PET plastic). This matters because plastic waste breaks down into microplastics that are showing up in our food, water, and even our bodies—so finding more natural ways to break down this plastic could eventually help reduce our exposure to it. Note that this is an early-stage computer analysis, not a lab test, so real-world proof that these fungal enzymes actually degrade plastic still needs to be confirmed through experiments.
Fungal Cutinase-Like Hydrolases As Prospective PET-Degrading Enzymes: An In Silico Analysis
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Scientists used computer modeling to show that certain fungal enzymes have a similar shape and chemical "cutting tools" as a bacterial enzyme already known to break down plastic bottles (PET). This matters because plastic pollution and the microplastics it creates are showing up in our food, water, and even bodies — and finding new enzymes that can break down this waste could lead to better tools for cleaning up plastic before it becomes the tiny particles linked to health concerns. This is still early-stage, computer-based research, so real-world lab testing is needed to confirm these fungal enzymes actually work in practice.
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Researchers isolated cutinase and lipase enzymes from Aspergillus tamarii and Penicillium crustosum fungi and demonstrated their ability to catalyze hydrolytic degradation of PET plastic, offering a potential biological route for plastic waste breakdown.
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A review on cutinases enzyme in degradation of microplastics
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This review examines the role of cutinase enzymes produced by bacteria and fungi in degrading various types of microplastics and plastic films. The study suggests that while enzymatic biodegradation shows promise as a remediation strategy, the diversity of microplastic types and their associated contaminants present significant challenges for effective environmental cleanup.
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