Aspects of surface chemical and application properties of acylated pol
ypeptides, resulting from the hydrolysis of proteins from different so
urces and with different molar weight distribution are studied separat
ely and in surfactant systems. This kind of substances is known as pro
tein fatty acid condensates. The activities were observed in connectio
n with the former described enzymically degraded proteins, at which eq
ual samples are used. Acylated polypeptides with chain lengths from C-
6 to C-18, derived from the protein hydrolyzes are powerful amphiphile
s and their surface activity (surface tension, sigma/log c-lsotherms,
c.m.c., contact angle) is affected by the molar weight of the polypept
ides as well as by the acyl chain length. The addition of acylated pol
ypeptides to aqueous surfactant solutions modifies the surface activit
y of the system, mostly in the sense of intensification of the surfact
ant properties (lowering of the surface and the interfacial tension en
hancing of wetting and foaming ability, the skin compatibility, and of
the effect on the viscosity).