A. Rouhana et al., HEAT INACTIVATION KINETICS OF TRYPSIN-INHIBITORS DURING HIGH-TEMPERATURE SHORT-TIME PROCESSING OF SOYMILK, Journal of food science, 61(2), 1996, pp. 265-269
Heat treatment of soymilk was studied in the conventional batch boilin
g process and under High Temperature-Short Time (HTST) conditions. Red
uction in total trypsin inhibitor was assayed enzymatically, and indiv
idual inhibitors, the Kunitz and the Bowman-Birk inhibitor, were assay
ed by ELISA technique. Standard first-order reaction kinetics and ther
modynamics were applicable for inactivation, and results indicated tha
t the mechanism was not protein unfolding, because entropy changes wer
e zero or negative. The two inhibitors were inactivated at the same ra
te around 137 degrees C. Therefore, a simple first-order kinetic model
which gave a good, slightly conservative estimate of residual anti-tr
ypsin activity under HTST conditions could be established.