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Display of PETase on the cell surface of Escherichia coli using the anchor protein PgsA
Summary
This study engineered bacteria to display a PET-degrading enzyme (PETase) on their cell surface, eliminating the costly step of purifying the enzyme for plastic breakdown. The approach could reduce the cost of biological PET plastic recycling, potentially offering a more scalable pathway for breaking down one of the most common plastic types.
<title>Abstract</title> Enzymatic degradation of polyethylene terephthalate (PET) is attracting attention as a new technology because of its mild reaction conditions. However, the cost of purified enzymes is a major challenge for the practical application of this technology. In this study, we attempted to display the surface of the PET-degrading enzyme, PETase, onto<italic> Escherichia coli</italic> using the membrane anchor, PgsA, from <italic>Bacillus subtilis</italic> to omit the need for purification of the enzyme. Immunofluorescence staining confirmed that PETase was successfully displayed on the surface of <italic>E. coli</italic> cells when a fusion of PgsA and PETase was expressed. The surface-displaying <italic>E. coli</italic> was able to degrade 94.6% of 1 mM bis(2-hydroxyethyl) terephthalate in 60 min, and the PET films were also degraded in trace amounts. These results indicate that PgsA can be used to present active PETase on the cell surface of <italic>E. coli</italic>. This technique is expected to be applied for efficient PET degradation.
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