Purification and Partial Characterization of Trypsin Inhibitor from Watermelon Seeds

Abstract

Several fractions demonstrating trypsin inhibitory activity were isolated from the seeds of watermelon. One of the mrnbnors was punfied to apparent homogeneity and partially characterized emploYing ion-exchange chromatography on DEAESephadex A-50, gel filtration on Sepnadex G100 and affinity chromatography on Trypsrn-Aqarose. The inhibitor has relative molecular mass of 10,000 by gel filtration. The inhibitor was resistant to heat up to iO"C for 30 minutes and acidic condition down to pH 4.0. Possibly the inhibitor belongs to the famlfy of low molecular weight heat resistant protease inhibitors.