Abstract
Hydrophobins are low-molecular surface-active proteins of fungi with high surface activity and the ability to self-assemble at the interface. The unusual properties of hydrophobins open up possibilities for their application in various fields, including medicine and the food industry. The wide range of possible applications of hydrophobins makes it important to develop and improve technology for their isolation and purification. The aim of the study was to select methods for the extraction of hydrophobin-type proteins and to study the ability of the obtained extracts to modify the solid surface. The source of hydrophobins in this study was the biomass of the fungus Funalia trogii. Methods for the isolation of hydrophobin-type proteins were developed, including purification of the extract from ballast proteins, followed by the destruction of agglomerates of hydrophobin-type proteins using acids in high concentrations. The surface activity and the ability to modify the surface of the obtained proteins were evaluated. As a result, we obtained extracts containing hydrophobin-type proteins with high surface activity. Funalia trogii extracts are capable of changing the hydrophobicity of the surface and can be used in various industries.
Highlights
Mushrooms are a source of a large number of useful substances: antibiotics, organic acids, carotenoids, enzymes, etc [1]
An interesting example of such compounds are structural proteins of fungi - hydrophobins. These proteins were discovered in 1986 while searching for genes expressed during the formation of aerial mycelium in the Schizophyllum commune [2]
Hydrophobins are a class of low molecular weight structural proteins consisting of about 100 amino acid residues and found exclusively in filamentous fungi
Summary
Mushrooms are a source of a large number of useful substances: antibiotics, organic acids, carotenoids, enzymes, etc [1]. The compounds contained in mushrooms can have high biological, and surface activity. An interesting example of such compounds are structural proteins of fungi - hydrophobins. These proteins were discovered in 1986 while searching for genes expressed during the formation of aerial mycelium in the Schizophyllum commune [2]. Hydrophobins are a class of low molecular weight structural proteins consisting of about 100 amino acid residues and found exclusively in filamentous fungi. Hydrophobins with high surface activity are capable of self-assembly into hydrophilic or hydrophobic amphipathic monolayers at the interface between the hydrophobic and hydrophilic phases, as well as on various surfaces [4]. As a result of the formation of such structures, the surface character changes from hydrophilic to hydrophobic (and vice versa)
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