Heated soy flours have been analyzed by the pH stat successfully for tryptic proteolysis and for residual trypsin inhibitor in previous studies. Unheated soy flours give a sudden release of hydrogen ion followed by a constantly decreasing proteolysis rate and consequently are difficult to analyze. We have found that by adjusting the pH of the trypsin preparation to 9 (the pH of the analysis) the pH stat method measured proteolysis and trypsin inhibitor in unheated soy flours. The unheated soy protein was hydrolyzed at 40% of the rate of heated soy protein and contained 68 mg/g of Kunitz trypsin inhibitor equivalents.
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HILL et al. (1982) studied this question.
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