Surface film was formed from an aqueous extract of blanched full-fat peanut cotyledons by heating the dilute solution (2–5% protein, w/v) to 95°C in a stainless steel pan. The effect of three processing parameters (pH, temperature and protein concentration) on film forming properties was investigated. Regression analysis showed process temperature to be the most influential parameter on both the rate of film formation and film yield. Evidence for major structural reorganization of peanut globulins was obtained by gel electrophoresis, ultracentrifugation and differential scanning calorim-etry. During film formation peanut proteins underwent a sequential breakdown of higher molecular weight globulins (S20's of 13.4 and 8.1) into lower molecular weight fractions followed by reaggrega-tion into an insoluble complex at the surface. The process was enhanced by alkaline pH conditions and higher protein concentration (up to 5% w/v). Scanning electron microscopy revealed the structural basis (extensive vacuolation with thinner air cell walls) for an observed loss in tensile strength of films produced at elevated pH levels.