Hydrophobins fulfill a
wide spectrum of functions in fungal gro
wth and development. These proteins self-assembleat hydrophilic-hydrophobic interfaces into amphipathic membranes. Hydrophobins are divided into t
wo classesbased on their hydropathy patterns and solubility. We sho
w here that the properties of the class II hydrophobinsHFBI and HFBII of
Trichoderma reesei differ from those of the class I hydrophobin SC3 of
Schizophyllumcommune. In contrast to SC3, self-assembly of HFBI and HFBII at the
water-air interface
was neither accompaniedby a change in secondary structure nor by a change in ultrastructure. Moreover, maximal lo
wering of the
watersurface tension
was obtained instantly or took several minutes in the case of HFBII and HFBI, respectively. Incontrast, it took several hours in the case of SC3. Oil emulsions prepared
with HFBI and SC3
were more stablethan those of HFBII, and HFBI and SC3 also interacted more strongly
with the hydrophobic Teflon surfacemaking it
wettable. Yet, the HFBI coating did not resist treatment
with hot detergent,
while that of SC3 remainedunaffected. Interaction of all the hydrophobins
with Teflon
was accompanied
with a change in the circular dichroismspectra, indicating the formation of an
-helical structure. HFBI and HFBII did not affect self-assembly of theclass I hydrophobin SC3 of
S. commune and vice versa. Ho
wever, precipitation of SC3
was reduced by the classII hydrophobins, indicating interaction bet
ween the assemblies of both classes of hydrophobins.