ArticleApplied and environmental microbiology2015
Enhanced cutinase-catalyzed hydrolysis of polyethylene terephthalate by covalent fusion to hydrophobins.
Article in Applied and environmental microbiology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers, 1 of them a synthesis that pooled it.
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Who cites it
53 citing papers in PubMed, 1 synthesis or guideline pooled it, 191 citations in OpenAlex.
- The diversity of PET degrading enzymes: A systematic review of sequence, structure, and function.Protein science : a publication of the Protein Society · 2025Pooled it
- Lipases and Cutinases from Phytopathogenic and Saprobic Fungi in Plastic.Methods in molecular biology (Clifton, N.J.) · 2027Article
- Fungal Hydrophobins: Taxonomic Distribution, Functional Roles, Physicochemical Properties, and Biotechnological Applications.Journal of fungi (Basel, Switzerland) · 2026Review
- Insights into Microbial Enzymatic Biodegradation of Plastics and Microplastics: Technological Updates.ACS environmental Au · 2025Review
- A High-Throughput Investigation of the Binding Specificity of Carbohydrate-Binding Modules for Synthetic and Natural Polymers.ChemSusChem · 2025Article
- Biodegradation Efficacy ofPolymers · 2025Article
- Structural and Electronic Properties of Poly(ethylene terephthalate) (PET) from Polarizable Molecular Dynamics Simulations.Macromolecules · 2025Article
- Design of Plastic Binding Lytic Polysaccharide Monooxygenases via Modular Engineering.Chem & bio engineering · 2024Article
- Review
- Interfacial Reactions in Chemical Recycling and Upcycling of Plastics.ACS applied materials & interfaces · 2024Review
- Soil Microplastic Pollution and Microbial Breeding Techniques for Green Degradation: A Review.Microorganisms · 2024Review
- Surface-associated residues in subtilisins contribute to poly-L-lactic acid depolymerization via enzyme adsorption.Microbial biotechnology · 2024Article
- Recent advances in microbial and enzymatic engineering for the biodegradation of micro- and nanoplastics.RSC advances · 2024Review
- Constructing Escherichia coli co-display systems for biodegradation of polyethylene terephthalate.Bioresources and bioprocessing · 2023Article
- Harnessing extremophilic carboxylesterases for applications in polyester depolymerisation and plastic waste recycling.Essays in biochemistry · 2023Article
- Discovery and mechanism-guided engineering of BHET hydrolases for improved PET recycling and upcycling.Nature communications · 2023Article
- Screening the Degradation of Polymer Microparticles on a Chip.ACS omega · 2023Article
- Current advances in the structural biology and molecular engineering of PETase.Frontiers in bioengineering and biotechnology · 2023Review
- Recent advances in the biodegradation of polyethylene terephthalate with cutinase-like enzymes.Frontiers in microbiology · 2023Review
- Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin.Nature communications · 2022Article
Corrections and comments
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Authors and funding
15 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cutinases have shown potential for hydrolysis of the recalcitrant synthetic polymer polyethylene terephthalate (PET). We have shown previously that the rate of this hydrolysis can be enhanced by the addition of hydrophobins, small fungal proteins that can alter the physicochemical properties of surfaces. Here we have investigated whether the PET-hydrolyzing activity of a bacterial cutinase from Thermobifida cellulosilytica (Thc_Cut1) would be further enhanced by fusion to one of three Trichoderma hydrophobins, i.e., the class II hydrophobins HFB4 and HFB7 and the pseudo-class I hydrophobin HFB9b. The fusion enzymes exhibited decreased kcat values on soluble substrates (p-nitrophenyl acetate and p-nitrophenyl butyrate) and strongly decreased the hydrophilicity of glass but caused only small changes in the hydrophobicity of PET. When the enzyme was fused to HFB4 or HFB7, the hydrolysis of PET was enhanced >16-fold over the level with the free enzyme, while a mixture of the enzyme and the hydrophobins led only to a 4-fold increase at most. Fusion with the non-class II hydrophobin HFB9b did not increase the rate of hydrolysis over that of the enzyme-hydrophobin mixture, but HFB9b performed best when PET was preincubated with the hydrophobins before enzyme treatment. The pattern of hydrolysis by the fusion enzymes differed from that of Thc_Cut1 as the concentration of the product mono(2-hydroxyethyl) terephthalate relative to that of the main product, terephthalic acid, increased. Small-angle X-ray scattering (SAXS) analysis revealed an increased scattering contrast of the fusion proteins over that of the free proteins, suggesting a change in conformation or enhanced protein aggregation. Our data show that the level of hydrolysis of PET by cutinase can be significantly increased by fusion to hydrophobins. The data further suggest that this likely involves binding of the hydrophobins to the cutinase and changes in the conformation of its active center.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.