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A mini-review on the role of PETase in polyethylene terephthalate degradation
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This mini-review summarized the structure, performance enhancement approaches, and potential applications of PETase, the enzyme from Ideonella sakaiensis discovered in 2016 that uses PET plastic as a carbon source, alongside MHETase for complete degradation into terephthalic acid and ethylene glycol. The review highlighted progress in enzyme engineering for improved PETase activity and discussed applications in bioremediation and recycling, identifying it as a key candidate for addressing the global plastic waste problem through biological degradation.
Abstract Polyethylene terephthalate (PET) is one of the most widely used thermoplastic materials in the world, commonly found in packaging, textiles, and bottles. However, its persistence in the environment has become a significant global concern due to the growing accumulation of plastic waste. While various strategies for PET degradation have been proposed, none have yet been successfully adopted at an industrial scale. Nonetheless, the discovery of microorganisms that have naturally evolved the ability to break down plastics offers a promising path forward. A major breakthrough came in 2016 with the identification of Ideonella sakaiensis , a bacterium capable of using PET as a carbon source. This microbe relies on two key enzymes- PETase and MHETase- to degrade PET into simpler, non-toxic compounds such as mono(2-hydroxyethyl) terephthalate (MHET), bis(2-hydroxyethyl) terephthalate (BHET), terephthalic acid (TPA), and ethylene glycol (EG). This discovery has opened new possibilities for sustainable and biologically based solutions to the long-standing problem of plastic pollution. This mini-review summarize PETase’s structure, how to enhance its performance, and how it could be used in broader areas such as bioremediation and recycling. By laying out both the progress made and the challenges ahead, this review aims to inspire further work toward making PETase a key player in reducing plastic waste for good.
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This review explores the biology of PETase enzymes and their potential for addressing PET plastic pollution, covering the discovery of Ideonella sakaiensis and subsequent enzyme engineering efforts. Developing efficient PET-degrading enzymes is a promising biotechnological strategy for reducing plastic pollution at scale.
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This review focuses on the role of PETase enzymes in plastic biodegradation, examining how conventional and biological methods compare for PET plastic management and discussing specific enzyme mutants and microbial strains with enhanced PET degradation capacity. The authors highlight that genetically engineered organisms combined with plastic-degrading enzymes represent the most promising pathway for practical industrial-scale PET bioremediation.
Biodegradation of PET: Current Status and Application Aspects
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This review covered the current status of PET biodegradation, focusing on the discovery and mechanism of PET hydrolytic enzymes from Ideonella sakaiensis and the pathway from enzyme identification to potential bioremediation application. The authors assess progress toward commercializing enzymatic PET degradation and identify remaining technical barriers for large-scale plastic waste management.
Insight on recently discovered PET polyester-degrading enzymes, thermostability and activity analyses
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Researchers reviewed the enzymatic machinery of Ideonella sakaiensis and related microorganisms for PET degradation, detailing how PETase and MHETase cooperatively hydrolyze the polymer to terephthalic acid and ethylene glycol at moderate temperatures — and assessing the thermostability and pH tolerances that determine these enzymes' industrial potential.
Current advances in the structural biology and molecular engineering of PETase
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The study reviews advances in the structural biology and molecular engineering of PETase, an enzyme from the bacterium Ideonella sakaiensis that can break down PET plastic at moderate temperatures. Researchers discuss efforts to enhance the enzyme's activity and thermal stability through protein engineering, which could lead to more efficient and environmentally friendly PET recycling strategies.
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