Partial purification of trypsin/papain inhibitors from Hymenaea courbaril L. seeds and antibacterial effect of protein fractions

Abstract

ABSTRACT The crude extract and protein fractions of Hymenaea courbaril L. seeds were investigated for the presence of trypsin and papain inhibitors and antimicrobial activity against Vibrio parahaemolyticus, Staphylococcus aureus, and Escherichia coli. Protein fractions were obtained from the crude extract after precipitation with ammonium sulfate into three saturation ranges (0-30%, 30-60%, and 60-90%), called Hc030, Hc3060, and Hc6090, respectively. The crude extract and protein fractions inhibited trypsin and papain activity, but to different degrees. Antimicrobial activity was observed in Hc030 and Hc3060 fractions, but only against V. parahaemolyticus.The inhibitor isolated from the Hc3060 fraction was more effective in inhibiting trypsin (100% inhibition) than papain (54% inhibition), and showed an apparent molecular mass of 20 kDa. This study shows that H. courbaril seeds contain proteins with protease-inhibiting and antibacterial activity, indicating that this species is a source of bioactive compounds.