This work evaluates the trypsin inhibitors reactivation, after in vitro proteolysis, of heat-treated soybean. For the inhibitors thermal inactivation, soybeans were soaked in distilled water (1:5 p/v) during 12 hours and heated on reflux plates for 30 minutes. The inhibitors reactivation was evaluated in comparison with the activity of raw and heated samples. The in vitro digestibility of proteins ranged from 47% ( 'OC-13') to 59% ('Parana'), showing an average progress of 32.6% with the heating. The trypsin inhibitors activity ranged from 122 to 206 UTI/mg for the raw sample, and the values correlated negatively with the digestibility percentage (r = - 0.9177). The inhibitors had the activities totally inactivated with the heating of soybeans, which showed an average recovering percentage of 40%. With the heating, the inactivation of inhibitors probably takes place by complexing with the soybean components, which leads to the recovering of activity with the enzymatic digestion process.
trypsin inhibitors; thermal inactivation; in vitro digestibility; reactivation; soybeans
