• sunflower proteins;
  • gelation;
  • physicochemical interactions


The effects of temperature and several chemicals on gelation time and strength of gels formed by heating (pH 8) 5% solutions of trypsin hydrolyzed sunflower proteins were studied by dynamic rheological methods. The storage modulus reached a maximum at 80°C. Ca2Cl (and NaCl at > 0.2M) accelerated gelation and weakened the gel. NaCOCH3Na2SO4 and NaSCN decreased the storage modulus. Urea decreased gelstrength and at high concentrations slowed gelation. Time for gelation diminished and gel strength increased with increasing mercaptoethanol concentration up to 0.1M. Propylene glycol at 5–20% concentrations accelerated gelation and at 5% also increased gel strength. Trypsin hydrolyzed sunflower proteins could be useful in products requiring strong gels at high temperatures.