ArticleApplied and environmental microbiology2013
Two novel class II hydrophobins from Trichoderma spp. stimulate enzymatic hydrolysis of poly(ethylene terephthalate) when expressed as fusion proteins.
Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 36 papers.
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Who cites it
36 citing papers in PubMed, 112 citations in OpenAlex.
- Fungal Hydrophobins: Taxonomic Distribution, Functional Roles, Physicochemical Properties, and Biotechnological Applications.Journal of fungi (Basel, Switzerland) · 2026Review
- Aqueous-Based Biomimetic Porphyrin-Catalyzed Surface Oxidation of Polyethylenes for Enhanced 3D-Printability.Journal of the American Chemical Society · 2026Article
- Esterase and Peroxidase Are Involved in the Transformation of Chitosan Films by the FungusJournal of fungi (Basel, Switzerland) · 2025Article
- Biodegradation Efficacy ofPolymers · 2025Article
- Structural elucidation of four fungal hydrophobins belonging to classes I and II: Results from Alphafold and accelerated molecular dynamics simulations.Computational and structural biotechnology journal · 2025Article
- Design of Plastic Binding Lytic Polysaccharide Monooxygenases via Modular Engineering.Chem & bio engineering · 2024Article
- Preparation and Characterization of Hydrophobin 4-Coated Liposomes for Doxorubicin Delivery to Cancer Cells.Pharmaceuticals (Basel, Switzerland) · 2024Article
- Molecular Insights into the Enhanced Activity and/or Thermostability of PET Hydrolase by D186 Mutations.Molecules (Basel, Switzerland) · 2024Article
- Fungal Screening for Potential PET Depolymerization.Polymers · 2023Article
- Current advances in the structural biology and molecular engineering of PETase.Frontiers in bioengineering and biotechnology · 2023Review
- Ethylene glycol metabolism in the poly(ethylene terephthalate)-degrading bacterium Ideonella sakaiensis.Applied microbiology and biotechnology · 2022Article
- Biodegradation of highly crystallized poly(ethylene terephthalate) through cell surface codisplay of bacterial PETase and hydrophobin.Nature communications · 2022Article
- Review
- Mechanism-Based Design of Efficient PET Hydrolases.ACS catalysis · 2022Review
- Catalytic Features and Thermal Adaptation Mechanisms of a Deep Sea Bacterial Cutinase-Type Poly(Ethylene Terephthalate) Hydrolase.Frontiers in bioengineering and biotechnology · 2022Article
- Fungal Enzymes as Catalytic Tools for Polyethylene Terephthalate (PET) Degradation.Journal of fungi (Basel, Switzerland) · 2021Review
- The pleiotropic functions of intracellular hydrophobins in aerial hyphae and fungal spores.PLoS genetics · 2021Article
- Fungal and enzymatic bio-depolymerization of waste post-consumer poly(ethylene terephthalate) (PET) bottles using3 Biotech · 2021Article
- At least three families of hyphosphere small secreted cysteine-rich proteins can optimize surface properties to a moderately hydrophilic state suitable for fungal attachment.Environmental microbiology · 2021Article
- Synergistic biodegradation of poly(ethylene terephthalate) using Microbacterium oleivorans and Thermobifida fusca cutinase.Applied microbiology and biotechnology · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Poly(ethylene terephthalate) (PET) can be functionalized and/or recycled via hydrolysis by microbial cutinases. The rate of hydrolysis is however low. Here, we tested whether hydrophobins (HFBs), small secreted fungal proteins containing eight positionally conserved cysteine residues, are able to enhance the rate of enzymatic hydrolysis of PET. Species of the fungal genus Trichoderma have the most proliferated arsenal of class II hydrophobin-encoding genes among fungi. To this end, we studied two novel class II HFBs (HFB4 and HFB7) of Trichoderma. HFB4 and HFB7, produced in Escherichia coli as fusions to the C terminus of glutathione S-transferase, exhibited subtle structural differences reflected in hydrophobicity plots that correlated with unequal hydrophobicity and hydrophily, respectively, of particular amino acid residues. Both proteins exhibited a dosage-dependent stimulation effect on PET hydrolysis by cutinase from Humicola insolens, with HFB4 displaying an adsorption isotherm-like behavior, whereas HFB7 was active only at very low concentrations and was inhibitory at higher concentrations. We conclude that class II HFBs can stimulate the activity of cutinases on PET, but individual HFBs can display different properties. The present findings suggest that hydrophobins can be used in the enzymatic hydrolysis of aromatic-aliphatic polyesters such as PET.
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