ArticleEuropean biophysics journal : EBJ2010
Recombinantly produced hydrophobins from fungal analogues as highly surface-active performance proteins.
Article in European biophysics journal : EBJ, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed.
- Emerging role of hydrophobins as a novel bio-surfactant and its multifaceted applications for sustainable practices: a mini-revsiew.Archives of microbiology · 2026Review
- Mushroom-Derived Hydrophobins for Antifouling and Interface Preservation in Chemosensors.Sensors (Basel, Switzerland) · 2026Review
- Soluble Expression and Efficient Purification of Recombinant Class I Hydrophobin DewA.International journal of molecular sciences · 2021Article
- Hydrophobins: multifunctional biosurfactants for interface engineering.Journal of biological engineering · 2019Review
- Comparative analysis of surface coating properties of five hydrophobins from Aspergillus nidulans and Trichoderma reseei.Scientific reports · 2018Article
- Pichia pastoris is a Suitable Host for the Heterologous Expression of Predicted Class I and Class II Hydrophobins for Discovery, Study, and Application in Biotechnology.Microorganisms · 2018Article
- Applications of Functional Amyloids from Fungi: Surface Modification by Class I Hydrophobins.Biomolecules · 2017Review
- Characterization of a Basidiomycota hydrophobin reveals the structural basis for a high-similarity Class I subdivision.Scientific reports · 2017Article
- Immobilization of LccC Laccase from Aspergillus nidulans on Hard Surfaces via Fungal Hydrophobins.Applied and environmental microbiology · 2016Article
- Hydrophobin-Based Surface Engineering for Sensitive and Robust Quantification of Yeast Pheromones.Sensors (Basel, Switzerland) · 2016Article
- Fusion to Hydrophobin HFBI Improves the Catalytic Performance of a Cytochrome P450 System.Frontiers in bioengineering and biotechnology · 2016Article
- Recent Advances in Fungal Hydrophobin Towards Using in Industry.The protein journal · 2015Review
- Article
- Hydrophobin can prevent secondary protein adsorption on hydrophobic substrates without exchange.Analytical and bioanalytical chemistry · 2011Article
- Creating Surface Properties Using a Palette of Hydrophobins.Materials (Basel, Switzerland) · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hydrophobins are available from natural resources only in milligram amounts. BASF succeeded in a recombinant production process, up-scaled to pilot plant production in kilogram scale. Strain and protein optimization by modulation of gene expression and generation of fusion proteins finally leads to two class I hydrophobins called H*Protein A and H*Protein B. By analytical ultracentrifugation, we confirm that the self-association of H*Proteins in solution is governed by their sequence, because oligomerization is induced by the same mechanisms (pH > 6, temperature >> 5 degrees C, concentration > 0.2 mg/ml) as for the well-known native hydrophobins SC3 and HFB II. Additionally, we established the triggering of structure formation by bridging with divalent ions and the stabilization of dimers and tetramers by monovalent ions or surfactants. This interplay with surfactants can be exploited synergistically: The capacity for emulsification of a 300 ppm standard surfactant solution is boosted from 0 to 100% by the addition of a mere 1 ppm of our new hydrophobins, with H*Protein A and H*Protein B having specific application profiles. This astonishing performance is rationalized by the finding that the same minute admixtures enhance significantly the interfacial elastic modulus, thus stabilizing interfaces against coalescence and phase separation.
Indexed as
Identifiers
19290518What OpenQuestion holds
Registered trials
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.