FACTORS AFFECTING THE GELATION PROPERTIES OF HYDROLYZED SUNFLOWER PROTEINS

The effects of temperature and several chemicals on gelation time and strength of gels formed by heating (pH 8) 5% solutions of trypsin hydr olyzed sunflower proteins were studied by dynamic rheological methods. The storage modulus reached a maximum at 80 degrees C. Ca2Cl (and NaC l at > 0.2M) accelerated gelation and weakened the gel. NaCOCH3, Na2SO 4 and NaSCN decreased the storage modulus. Urea decreased gel strength and at high concentrations slowed gelation. Time for gelation diminis hed and gel strength increased with increasing mercaptoethanol concent ration up to 0.1M. Propylene glycol at 5-20% concentrations accelerate d gelation and at 5% also increased gel strength. Trypsin hydrolyzed s unflower proteins could be useful in products requiring strong gels at high temperatures.