Abstract
Bowman-Birk inhibitor, a major trypsin and chymotrypsin inhibitor from soybean, has 71 amino acids with 7 disulfide bonds. Conformation of Bowman-Birk inhibitor in native state, after heating, and after disulfide bonds were broken by sodium metabisulfite was determined by circular dichroism. The native Bowman-Birk inhibitor has 61% β-sheet, 38% unordered form, 1% β-turn, and no a-helical structure. There was no significant change in conformation after Bowman-Birk inhibitor was heated at 80 o C for 1 h in phosphate buffer. There was a decrease in β-sheet and an increase in β-turn structure after Bowman-Birk inhibitor was heated at 80 o C for 1 h in sodium metabisulfite-phosphate buffer
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