We can't find the internet
Attempting to reconnect
Something went wrong!
Hang in there while we get back on track
Design of Functionalized Silica Immobilization of PETase from Kibdelosporangium aridum : Comparison of Glyoxyl and Glutaraldehyde Strategies for PET Depolymerization
AI summary Read the abstract
Researchers immobilized a PET-degrading enzyme from Kibdelosporangium aridum onto three functionalized silica supports, finding that glutaraldehyde-linked variants achieved up to five-fold greater thermal stability and catalytic efficiency than the free enzyme, with enhanced PET surface modification confirmed by XPS analysis.
Polyethylene terephthalate (PET) is a widely used thermoplastic that poses a major challenge to global resource sustainability because of its extensive consumption and contribution to plastic pollution. This study aimed to enhance the performance of PETase derived from Kibdelosporangium aridum (KaPETase) through immobilization onto aldehyde-functionalized silica supports with varying active groups: (i) 3-aminopropyl silica gel via glutaraldehyde (Si-NH2@KaPETase), (ii) (3-aminopropyl)triethoxysilane (3-APTES) functionalized silica via glutaraldehyde (Si-Glu@KaPETase), and (iii) glyoxyl silica (Si-Ald@KaPETase). The immobilized biocatalysts exhibited 4.6- to 5.1-fold greater thermal stability at 75 °C than that of the free enzyme. Catalytic efficiency was also significantly enhanced, increasing by 2.6- to 5.0-fold. Under optimized conditions, PET depolymerization assays demonstrated improved hydrolytic performance. HPLC analysis confirmed terephthalic acid (TPA) and mono(2-hydroxyethyl) terephthalate (MHET) as the primary degradation products. After 1 h of reaction, degradation product concentrations reached 43.4, 75.6, 93.4, and 61.2 mg mg–1 protein for free KaPETase, Si-NH2@KaPETase, Si-Glu@KaPETase, and Si-Ald@KaPETase, respectively. Surface-sensitive XPS measurements revealed more pronounced PET surface chemical modifications for PET surfaces incubated by aldehyde- and especially glutaraldehyde-functionalized KaPETase systems, indicating enhanced enzyme–surface interactions. Overall, immobilization on functionalized silica supports significantly improved catalytic activity, thermostability, and reusability. These findings demonstrate the strong potential of robust immobilized KaPETase systems for sustainable and industrially relevant PET biodegradation.
More Papers Like This
Directed Immobilization of PETase on Mesoporous Silica Enables Sustained Depolymerase Activity in Synthetic Wastewater Conditions
AI summary Read the abstract
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.
Silica immobilized PETase for microplastic bioremediation: Influence of linker peptides on activity
AI summary Read the abstract
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.
Enhancement of the degradation capacity of IsPETase by acidic amino acids insertion and carbohydrate-binding module fusion
AI summary Read the abstract
Researchers engineered an improved PET-degrading enzyme by inserting a negatively charged glutamate residue at a key structural bend in IsPETase and fusing a carbohydrate-binding module to its C-terminus, achieving a 10-fold activity increase at 45°C and successfully demonstrating degradation of industrial polyester filter cloth.
Site-Directed Immobilization of DuraPETase onto PET-Binding PDA@SiO2 for High-Efficiency PET Degradation
AI summary Read the abstract
Scientists engineered a plastic-eating enzyme and attached it to tiny particles in a precise way, making it work over twice as fast at breaking down PET plastic (the kind used in water bottles) while staying stable at high heat. This matters because better plastic-recycling enzymes could help reduce the mountains of plastic waste that eventually break down into microplastics—tiny particles increasingly found in our food, water, and even our bodies, with still-unclear health effects.
An Overview into Polyethylene Terephthalate (PET) Hydrolases and Efforts in Tailoring Enzymes for Improved Plastic Degradation
AI summary Read the abstract
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.
Research digests by email
When a large batch of papers lands in the Atlas, we read through it and send a short write-up of what stood out.