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Discovering Novel PETase Enzymes for Enhanced PET Plastic Degradation Using in Silico Approaches
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This comprehensive review found that freshwater biodiversity faces extinction rates 100 times above background levels, driven by habitat fragmentation, chemical pollution, invasive species, and hydrological alteration, with molluscs, fishes, and crustaceans among the most threatened groups. Microplastic pollution is among the chemical stressors contributing to this crisis, making freshwater biodiversity monitoring frameworks directly relevant to assessing microplastic ecological impacts.
Abstract Accounting for 12% of global solid waste, Poly (ethylene terephthalate) (PET) is one of the most abundantly produced synthetic polymers. While PET offers substantial commercial benefits, its widespread use has led to disproportionate environmental hazards due to its resistance to degradation. To address this problem, several solutions have been proposed, including enzymatic degradation via PETase, MHETase, and Cutinase. Among these, PETase exhibited significant PET-degrading activity. However, the application of PETase has been hampered by its lack of robustness to pH, temperature ranges, and slow reaction rates. Hence, it has become novel enzymes that can overcome these limitations and function efficiently. In this study, we utilised an integrated in silico bioinformatics pipeline to identify and characterise novel PETase candidates from the Thermophilic actinobacteria Thermobifida cellulosilytica and Thermobifida halotolerans species. The PlasticDB database contains 228 plastic-degrading enzyme sequences. In which PETase (00188) is significantly homologous with two putative proteins, Hydrolase (ALF00495.1) and hypothetical protein (WOZ56011.1). The discrete optimized protein energy (DOPE) scores, stereochemical assessments, and homology modeling results closely mirrored our findings for both proteins, supporting their structural stability. The molecular dynamics simulations revealed that the putative ALF00495 variant exhibited more extensive and robust hydrogen-bonding networks, enhanced conformational stability, and increased structural compactness compared to the reference enzyme. The present in silico investigation underscores the potential of putative ALF00495 as a highly effective PETase biocatalyst for polyethylene terephthalate (PET) degradation. Collectively, these findings illustrate the utility of computational approaches of novel PET-degrading enzymes, thereby facilitating the development of sustainable biotechnological strategies to mitigate global plastic pollution.
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In silico structural analysis and biochemical characterization of a novel PETase from Antarctic Streptomyces sp .
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Researchers characterized a novel PET-degrading enzyme (SsPETase) from Antarctic Streptomyces bacteria, using AlphaFold structural prediction and molecular dynamics simulations to reveal key catalytic residues and a substrate-dependent conformational shift that activates the enzyme, providing a foundation for engineering more efficient plastic-degrading enzymes.
In Silico Analysis and Biochemical Characterization of Streptomyces PET Hydrolase with Bis(2-Hydroxyethyl) Terephthalate Biodegradation Activity
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Researchers used computational modeling and biochemical assays to characterize a PET-degrading enzyme from Streptomyces bacteria, finding it can break down bis(2-hydroxyethyl) terephthalate, a key PET degradation product, suggesting potential for enzymatic plastic recycling.
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Researchers used computational methods to screen prokaryotic protein sequences for PET-degrading enzyme candidates, identifying 27 potential PETases across diverse bacterial species and shortlisting three from Halopseudomonas pertucinogena, Halopseudomonas bauzanensis, and Ketobacter sp. as the most structurally and functionally similar to the well-characterized PETase from Ideonella sakaiensis.
MPNN-guided redesign of PET hydrolases with enhanced catalytic activity below the PET glass transition temperature
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A structured PFAS risk matrix for EU food packaging compliance shows that fibre-based materials with grease- or water-resistant coatings carry the highest PFAS relevance, while glass and untreated PET present lower risk, with total fluorine serving as a material-specific rather than standalone compliance indicator. Because PFAS from food packaging leach into food and waterways, systematic risk-based screening frameworks directly support efforts to reduce the chemical contamination load associated with plastic and coated-paper packaging waste.
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.
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