Two types of soy protein hydrolysates were produced by hydrolysis of isolated soy protein (ISP) with a combination of Alcalase and Flavourzyme in a continuous membrane system with 3000 and 30,000 daltons molecular-weight-cut-off (MWCO) membranes, respectively. Both hydrolysates were completely soluble over a pH range of 2-9. Their water-binding capacity increased 1.8-3.4 times at a water activity of 0.6-0.95 sts compared to intact ISP. The antioxidant activity of ISP was remarkably enhanced by enzyme hydrolysis. The hydrolysate from the 30,000 daltons MWCO membrane had a much higher antioxidant activity than that from the 3000 daltons MWCO membrane. The results suggested that both selected enzymes and MWCO membrane governed the functional properties of protein hydrolysates. Long-term operation study showed that the membrane reactor system could maintain a steady production of ISP hydrolysate over 16 h. (C) 1999 Elsevier Science Ltd. All rights reserved.