Abstract
The stability of BTCI has been investigated as function of pH and temperature, following its inhibitory activity against trypsin. The isolated inhibitor of 9,084 Oa is stable over pH 3 to 12 at 25°C. BTCI showed high thermal stability ranging from 25 to 95°C at pH 3 and 7. However, the protein lost about 20% of its inhibitory activity over 75°C at pH 8.2. The results indicated that BTCI is extremely stable to heat and pH as typical of Bowman-Birk inhibitors.