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Review
. 2019 Jan 23:13:10.
doi: 10.1186/s13036-018-0136-1. eCollection 2019.

Hydrophobins: multifunctional biosurfactants for interface engineering

Bryan W Berger  1   2 , Nathanael D Sallada  1
Affiliations
Review

Hydrophobins: multifunctional biosurfactants for interface engineering

Bryan W Berger et al. J Biol Eng. .

Abstract

Hydrophobins are highly surface-active proteins that have versatile potential as agents for interface engineering. Due to the large and growing number of unique hydrophobin sequences identified, there is growing potential to engineer variants for particular applications using protein engineering and other approaches. Recent applications and advancements in hydrophobin technologies and production strategies are reviewed. The application space of hydrophobins is large and growing, including hydrophobic drug solubilization and delivery, protein purification tags, tools for protein and cell immobilization, antimicrobial coatings, biosensors, biomineralization templates and emulsifying agents. While there is significant promise for their use in a wide range of applications, developing new production strategies is a key need to improve on low recombinant yields to enable their use in broader applications; further optimization of expression systems and yields remains a challenge in order to use designed hydrophobin in commercial applications.

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Conflict of interest statement

Not applicable.Not applicable.The authors declare that they have no competing interests.Springer Nature remains neutral with regard to jurisdictional claims in published maps and institutional affiliations.

Figures

Fig. 1
Fig. 1
Visual summary of current hydrophobin applications and production systems
See this image and copyright information in PMC

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References

    1. Kershaw MJ, Talbot NJ. Hydrophobins and repellents: proteins with fundamental roles in fungal morphogenesis. Fungal Genet Biol. 1998;23:18–33. doi: 10.1006/fgbi.1997.1022. - DOI - PubMed
    1. Wösten HAB, de Vocht ML. Hydrophobins, the fungal coat unravelled. Biochim Biophys Acta (BBA)-Reviews Biomembr. 2000;1469:79–86. doi: 10.1016/S0304-4157(00)00002-2. - DOI - PubMed
    1. Wösten HAB. Hydrophobins: multipurpose proteins. Annu Rev Microbiol. 2001;55:625–646. doi: 10.1146/annurev.micro.55.1.625. - DOI - PubMed
    1. Kallio, J., Paananen, A., Askolin, S., Nakari-Setälä, T., Parkkinen, T., Penttilä, M., Linder, M., and Rouvinen, J. (2004) Atomic resolution structure of the HFBII Hydrophobin, a self-assembling Amphiphile. - PubMed
    1. Hakanpää J, Szilvay GR, Kaljunen H, Maksimainen M, Linder M, Rouvinen J. Two crystal structures of Trichoderma reesei hydrophobin HFBI—the structure of a protein amphiphile with and without detergent interaction. Protein Sci. 2006;15:2129–2140. doi: 10.1110/ps.062326706. - DOI - PMC - PubMed

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