ABSTRACT

Trypsin Inhibitor was isolated, purified by gel filtration and ion exchange chromatography and partially characterized. The trypsin inhibitor from Luffa aegyptiaca seed had an optimum pH of 8.0 while heating the inhibitor at varying temperature did not  inactivate it completely but the trypsin inhibitor activity was almost lost at 95°C. After which inhibition remained constant. The specific activity of the crude inhibitor extract was 4.44mg pure trypsin inhibited/gm  sample/mg protein. The crude inhibitor extract on Sephadex G-100 gave two peaks, with the prominent peak having an activity of 48.33mg pure trypsin inhibited/gm  sample/mg protein. Pooled fractions from this peak on SP-Sephadex C-50 gave three peaks with first peak having the most activity (95.51mg pure trypsin inhibited/gm sample/mg protein).