Purification of Mucuna pruriens (L) peptide fractions and evaluation of their ACE inhibitory effect

The ACE inhibitory potential of Mucuna pruriens (L) protein derivatives was evaluated. M. pruriens (L) protein concentrate was sequentially hydrolyzed using pepsin and pancreatin. Biological activity in the hydrolysate and its ultrafiltered fractions was evaluated and that with the highest biological activity was purified by gel filtration chromatography (GFC) and reverse phase high-performance liquid chromatography (RP-HPLC). The ACE inhibition manner and amino acid profile of the purified fractions with the highest biological potential was registered. The IC50 value for hydrolysate was 13.0270 μg/mL and for the ultrafiltered fractions ranged from 0.0009 to 5.7519 μg/mL. The five fractions (F1-F5) obtained by GFC had IC50 values in the range of 0.401-0.969 μg/mL. The two fractions (F1-1 and F1-2) obtained by RP-HPLC from F1 had IC50 values of 16.162 and 14.542 μg/mL, respectively with a competitive inhibition mechanism and a high hydrophobic amino acids distribution.