Abstract
Fungal hydrophobins are small amphiphilic proteins that self-assemble into monolayers on hydrophobic:hydrophilic interfaces and can be used for surface coatings. Because e.g. Aspergillus nidulans contains six different hydrophobins, it is likely that they have different properties and are used for different “applications” in the fungus. We established a method for recombinant production of different class hydrophobins in Escherichia coli. We produced DewA, DewC, DewD, DewE from A. nidulans and HFBI from Trichoderma reesei and compared surface coating properties of these hydrophobins. All tested proteins formed coatings on glass, strongly increasing the hydrophobicity of the surface, and showed emulsion-stabilizing properties. But whereas the typical class I hydrophobin DewA formed the most stable coating on glass, the intermediate class hydrophobins DewE and DewD were more effective in stabilization of oil:water emulsions. This work gives insights into correlations between structural characteristics of hydrophobins and their behaviour as surface binding agents. It could help with the clarification of their biological functions and lead to novel biotechnological applications.
Highlights
Hydrophobins are small amphiphilic proteins that self-assemble into monolayers on hydrophilic and hydrophobic surfaces and change their properties[1,2,3]
Hydrophobins RodA and DewB both possess a glycosylphosphatidylinositol (GPI) anchor for immobilization on the spore surface and both contribute to the hydrophobicity of the conidiospore surface of A. nidulans[4]
It has been shown previously that the fusion of pectate lyase B (pelB) to the HIV-1 protein Vpu is a suitable method for the expression of membrane-targeted proteins in E. coli, and Class II hydrophobins[24,30]
Summary
Hydrophobins are small amphiphilic proteins that self-assemble into monolayers on hydrophilic and hydrophobic surfaces and change their properties[1,2,3]. Class I hydrophobins form highly stable layers that can withstand detergents and high temperatures Their formation involves conformational changes of the protein molecules upon interaction with one another and formation of amyloid fibrillar structures[9,10]. The function and surface binding properties of other hydrophobins from A. nidulans are less studied They are all present on the spore surface, with DewD and DewE expressed in hyphae[4]. In for example Schizophyllum commune the Sc3 hydrophobin is expressed in aerial hyphae and the Sc1 and Sc4 hydrophobins are expressed in hyphae of fruiting bodies, suggesting different cellular functions and interesting specific properties of each hydrophobin[28]
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