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Magnetic silica-coated cutinase immobilized via ELPs biomimetic mineralization for efficient nano-PET degradation
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Researchers developed magnetically recoverable cutinase enzymes immobilized on silica-coated nanoparticles via a biomimetic mineralization approach, achieving 86% retained enzyme activity after 11 recycling cycles and degrading nano-sized PET plastic particles nearly as efficiently as free enzymes — offering a reusable, environmentally friendly approach to nanoplastic biodegradation.
The proliferation of nano-plastic particles (NPs) poses severe environmental hazards, urgently requiring effective biodegradation methods. Herein, a novel method was developed for degrading nano-PET (polyethylene terephthalate) using immobilized cutinases. Nano-PET particles were prepared using a straightforward method, and biocompatible elastin-like polypeptide-magnetic nanoparticles (ELPs-MNPs) were obtained as magnetic cores via biomimetic mineralization. Using one-pot synthesis with the cost-effective precursor tetraethoxysilane (TEOS), silica-coated magnetically immobilized ELPs-tagged cutinase (ET-C@SiO@MNPs) were produced. ET-C@SiO@MNPs showed rapid magnetic separation within 30 s, simplifying recovery and reuse. ET-C@SiO@MNPs retained 86 % of their initial activity after 11 cycles and exhibited superior hydrolytic capabilities for nano-PET, producing 0.515 mM TPA after 2 h of hydrolysis, which was 96.6 % that of free enzymes. Leveraging ELPs biomimetic mineralization, this approach offers a sustainable and eco-friendly solution for PET-nanoplastic degradation, highlighting the potential of ET-C@SiO@MNPs in effective nanoplastic waste management and contributing to environmental protection and sustainable development.
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Immobilization of PETase enzymes on magnetic iron oxide nanoparticles for the decomposition of microplastic PET
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PETase enzymes capable of degrading polyethylene terephthalate (PET) were immobilized on superparamagnetic iron oxide nanoparticles via a His-tag to improve stability and enable magnetic recovery. The immobilized enzyme system showed enhanced efficiency and reusability for breaking down PET microplastics in water.
Silica immobilized PETase for microplastic bioremediation: Influence of linker peptides on activity
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Researchers immobilized a modified PETase enzyme onto silica using different linker peptides and tested its ability to break down PET microplastics, finding that linker peptide design significantly influenced enzyme activity and reusability — key parameters for practical application in wastewater treatment.
Recycling the recyclers: strategies for the immobilisation of a PET-degrading cutinase
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Researchers compared immobilization strategies for a PET-degrading cutinase enzyme to enable reuse across multiple recycling cycles, finding that attachment to the pH-responsive polymer Kollicoat yielded 80% recovered activity and over 97% terephthalic acid yield across three consecutive reaction cycles, offering a cost-effective path toward industrial enzymatic PET recycling.
Directed Immobilization of PETase on Mesoporous Silica Enables Sustained Depolymerase Activity in Synthetic Wastewater Conditions
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Researchers developed a PETase enzyme immobilized on mesoporous silica nanoparticles that showed up to 6.2-fold increased activity and 2.5-fold enhanced stability for degrading PET microfibers under simulated wastewater conditions.
Magnetic Peroxidase Nanozyme Gears Up for Microplastic Removal and Deconstruction
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Researchers developed a magnetic peroxidase nanozyme capable of removing and deconstructing microplastics, offering a novel enzymatic approach that overcomes limitations of conventional plastic waste handling methods like landfilling and incineration.
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