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DESIGN AND CHARACTERIZATION OF MHETASE MUTANTS FOR IMPROVED ACTIVITY AND SOLUBILITY IN PET DEGRADATION
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| Polyethylene terephthalate (PET) is a plastic polymer valued for its durability and chemical inertness. However, inefficient recycling and improper disposal pose major environmental challenges. The bacterium Ideonella sakaiensis can biodegrade PET with two en zymes: PETase, which cleaves PET into smaller intermediates like mono-(2-hydroxyethyl) terephthalate(MHET),and MHETase, which hydrolyzes MHET into the monomers terephthalic acid (TPA) and ethylene glycol (EG). While PETase has been widely studied and engineered, MHETase remains comparative ly underexplored. This work addresses this gap by engineering mutants to improve both its catalytical efficiency and solubility. | 54 MB | Adobe PDF |
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Polyethylene terephthalate (PET) is a plastic polymer valued for its durability and chemical inertness. However, inefficient recycling and improper disposal pose major environmental challenges. The bacterium Ideonella sakaiensis can biodegrade PET with two enzymes: PETase, which cleaves PET into smaller intermediates like mono-(2-hydroxyethyl) terephthalate(MHET),and MHETase, which hydrolyzes MHET into the monomers terephthalic acid (TPA) and ethylene glycol (EG). While PETase has been widely studied and engineered, MHETase remains comparative ly underexplored. This work addresses this gap by engineering mutants to improve both its catalytical efficiency and solubility.
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Polyethylene terephthalate Protein engineering Biodegradation Molecular Docking Molecular Dynamics MHETase