Soy protein fractions rich in β-conglycinin (7S) or glycinin (11S) were freeze dried or spray dried at temperatures of 120, 150 or 180 °C. The fractions were characterized for their particle size distribution, sorption isotherms and by scanning differential calorimetry. The gelling capacity of the protein fractions was studied at pH values of 3 and 7 using oscillatory measurements, mechanical properties and water holding capacity. The rheological measurements showed that viscous modulus (G″) predominated at low temperatures and the elastic modulus (G′) at high temperatures. At pH 3, the G′-G″ crossover occurred at lower temperatures when compared to pH 7. This behaviour was more accentuated for the 11S fractions due to its capacity to form stronger gels. An increase of drying temperature led to a displacement of the gel point to higher temperatures and decreased the elasticity modulus or gelling capacity of protein fractions. These results were confirmed by the mechanical properties, since at higher temperatures the gels were more fragile and brittle, especially when formed at pH 7. © 2012 The Institution of Chemical Engineers.