Using CD-measurements the influence of nonionic surfactants (dodecyl polyoxyethylene, ethoxylated para tert. octyl phenol, commercial nonionic WON 100 and octyl diethyl phosphinoxid) on the secondary structure of gelatin in aqueous solutions was investigated. At surfactant concentrations smaller than the c.m.c, the triple helical content of the gelatin is increased. At concentrations exceeding the c.m.c, the triple helical content decreases. Chain reversals of the peptide chains after the destruction of the triple helical structure were shown to appear in acidic environment at 298 K. This destruction is reversible by rechilling the solution.

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