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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.
Poly(ethylene terephthalate) (PET) is a highly useful synthetic polyester plastic that is widely used in daily life. However, the increase in postconsumer PET as plastic waste that is recalcitrant to biodegradation in landfills and the natural environment has raised worldwide concern. Currently, traditional PET recycling processes with thermomechanical or chemical methods also result in the deterioration of the mechanical properties of PET. Therefore, it is urgent to develop more efficient and green strategies to address this problem. Recently, a novel mesophilic PET-degrading enzyme (IsPETase) from Ideonella sakaiensis was found to streamline PET biodegradation at 30°C, albeit with a lower PET-degrading activity than chitinase or chitinase-like PET-degrading enzymes. Consequently, the molecular engineering of more efficient PETases is still required for further industrial applications. This review details current knowledge on IsPETase, MHETase, and IsPETase-like hydrolases, including the structures, ligand‒protein interactions, and rational protein engineering for improved PET-degrading performance. In particular, applications of the engineered catalysts are highlighted, including metabolic engineering of the cell factories, enzyme immobilization or cell surface display. The information is expected to provide novel insights for the biodegradation of complex polymers.
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Explorations of Polyethylene Terephthalate (PET) Hydrolase for addressing PET Plastic Pollution
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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.
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.
Characterization and engineering of a two-enzyme system for plastics depolymerization
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A 1.6 Å resolution crystal structure of MHETase — the second enzyme in Ideonella sakaiensis's PET-degrading two-enzyme system — revealed a PETase-like core capped by a lid domain, and computational and biochemical analysis confirmed a canonical serine hydrolase mechanism, enabling rational engineering of the PET recycling pathway.
An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
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This review examines the discovery and engineering of PET-degrading enzymes including PETase and cutinase variants, discussing protein engineering strategies to improve catalytic efficiency and thermostability for practical biodegradation of polyethylene terephthalate plastic waste.
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.
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