T HE effect of heat on trypsin inhibitor (TI) activity during steam-infusion cooking of soymilk was studied. At 154°C only 40 s process time reduced TI to the same level as conventional cooking at 99°C for 60 min. Between 99 and 154°C the kinetics of TI inactivation followed behavior exemplified by the summation of two first-order reactions. Spline fitting functions effectively modeled the data with r 2 ranging from 0.984 to 0.999. The heat-labile reaction was attributed to Kunitz inhibitor and the heat-stable reaction, to Bowman-Birk inhibitor. The former accounted for approximately 85 percent of the iriginal TI activity. Arrhenius equation kinetic constants for each reaction were calculated.

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due to an increase in the free energy of reaction by forming a relatively unstable cobalt(III) complex and/or a relatively stable MX"+ product. Other functions of bridging ligands (e.g., changing the path of reaction, altering selection rules, varying the lifetimes of bridged intermediates, etc.) are much less obvious and will be considered elsewhere.

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