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Isoelectric fractionation of the two major proteins of soy is characterized. Fractions are acid precipitated and centrifugally collected at pH 6.0 (glycinin) and pH 4.8 (B-conglycinin). Two extremes in the speed of acid addition (rapid, with no mixing, and slow, via acid dialysis, with complete mixing) are compared to determine their effects on the properties of the precipitate. Total protein yield, fraction composition, and aggregate microstructure do not depend significantly on the method of acid addition. Particle size distribution and hindered settling behavior do differ and are explained using a model of aggregate strength. The rapid acid addition produces larger primary particles, because of higher supersaturation, and yields larger aggregates, because of higher interparticle potential and stronger aggregates. Further aggregation in lowshear hindered settling is faster for the slowly precipitated aggregate because few of these bonding sites could survive the high-shear precipitator, whereas more can contribute to aggregation during hindered settling.

Protein precipitation with acids and polyelectrolytes: the effects of reactor conditions and models of the particle size distributions