Isolation and identification of trypsin inhibitors from wheat grain, Beta variety

Abstract

The aim of this study was the identification of trypsin inhibitors in wheat grain, Beta variety. These inhibitors in spite of other functional properties belong to the antinutrient substances. According to the elaborated procedure first, the extract showing inhibitory activity was salted out at 30-80 % ammonium sulfate saturation. Subsequently the preparation was purified by afinity chromatography with trypsin bound on Sepharose 4B. As result of this treatment a protein which had inhibitory activity 20-fold stronger than that of the crude extract was obtained. The homogeneity of the preparation was checked by disc electrophoresis.The study showed that the isolated protein was most probably a monomer bound to some carbohydrates.