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Engineering IsPETase and Its Homologues: Advances in Enzyme Discovery and Host Optimisation
Summary
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.