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Engineering IsPETase and Its Homologues: Advances in Enzyme Discovery and Host Optimisation
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This review summarizes recent advances in engineering IsPETase and related enzymes to improve their ability to break down PET plastic more efficiently and under a wider range of conditions. Researchers discuss strategies including directed evolution and rational design that have enhanced enzyme stability, activity, and substrate binding. These developments move plastic-degrading enzymes closer to practical deployment in industrial-scale recycling systems.
Polyethylene terephthalate (PET) pollution represents a significant environmental challenge due to its widespread use and recalcitrant nature. PET-degrading enzymes, particularly Ideonella sakaiensis PETases (IsPETase), have emerged as promising biocatalysts for mitigating this problem. This review provides a comprehensive overview of recent advancements in the discovery and heterologous expression of IsPETase and closely related enzymes. We highlight innovative approaches, such as in silico and AI-based enzyme screening and advanced screening assays. Strategies to enhance enzyme secretion and solubility, such as using signal peptides, fusion tags, chaperone co-expression, cell surface display systems, and membrane permeability modulation, are critically evaluated. Despite considerable progress, challenges remain in achieving industrial-scale production and application. Future research must focus on integrating cutting-edge molecular biology techniques with host-specific optimisation to achieve sustainable and cost-effective solutions for PET biodegradation and recycling. This review aims to provide a foundation for further exploration and innovation in the field of enzymatic plastic degradation.
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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.
Engineering, Expression, and Purification Fast-petase with Pelb Signal Peptide
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This study describes the design, expression, and purification of FAST-PETase, an engineered plastic-degrading enzyme derived from PETase produced by Ideonella sakaiensis, with a novel signal peptide for improved production. FAST-PETase showed significantly enhanced PET hydrolysis efficiency and stability, offering promise for industrial-scale plastic recycling.
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.
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.
A high‐throughput expression and screening platform for applications‐driven PETase engineering
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Researchers developed a high-throughput platform for engineering PETase enzymes — which break down plastic polyester — by using secretory expression to eliminate purification steps, enabling faster screening of enzyme variants for industrial plastic biodegradation applications.
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When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.