Prediction and Evaluation of Bioactive Properties of Cowpea Protein Hydrolysates

Abstract

Cowpea protein hydrolysates were prepared using thermolysin, alcalase, and trypsin and analysed for bioactive properties, and then, the release of bioactive peptides was investigated in silico. It was found that the degree of hydrolysis reached 48% after 24 h hydrolysis with alcalase. The hydrolysate prepared using alcalase showed higher ACE inhibitory (62%) and DPPH scavenging activity (19%). SDS-PAGE analysis revealed that vignin was the major protein in cowpea protein isolate. In silico analysis indicated the presence of potential bioactive peptides with potent bioactivity in the primary structure of proteins. The 3D structure of proteins was built, upon which bioactive peptides were mapped using their location in the primary structure. The secondary structure and solvent accessible surface around each bioactive peptide were then calculated. On this basis, the higher degree of hydrolysis and bioactive properties of cowpea protein hydrolysate prepared by alcalase were explained, and structural factors influencing the release of bioactive peptides were investigated.