Class I and class II hydrophobins are small secreted fungal proteins that s
elf-assemble at hydrophilic-hydrophobic interfaces into amphipathic films.
Apart from eight conserved cysteine residues, the amino acid sequences betw
een and within both classes have diverged considerably, and this is reflect
ed in the biophysical properties of these proteins. For instance, assemblag
es of class I hydrophobins are highly insoluble, while those of class II hy
drophobins readily dissolve in a variety of solvents. The properties of hyd
rophobins make them interesting candidates for use in a wide range of medic
al and technical applications. Each application has its own requirements, w
hich may be met by using specific natural variants of hydrophobins or by mo
difying hydrophobins chemically or genetically. Applications also require h
igh production systems for hydrophobins. In this respect, filamentous fungi
that naturally secrete hydrophobins into the medium seem to be the hosts o
f choice.