Angiotensin Converting Enzyme Inhibitory Activity of Soy Protein Subjected to Selective Hydrolysis and Thermal Processing

Soy protein isolate (SPI) and beta-conglycinin- and glycinin-rich fractions were hydrolyzed using papain and pepsin. Protein denaturation, profiling, and peptide identification were carried out following DSC, SDS-PAGE, and liquid chromatography-tandem mass spectrometry (LC-MS/MS) analysis. The in vitro antihypertensive activity of the hydrolysates was compared by determining the angiotensin converting enzyme (ACE) inhibitory activity. SDS-PAGE and LC-MS/MS analysis confirmed pepsin selectivity to glycinin and papain partial selectivity to beta-conglycinin when the protein is least denatured. Both the papain-hydrolyzed SPI and the papain-hydrolyzed beta-conglycinin-rich fraction had more than double the ACE inhibitory activity of that of pepsin-hydrolyzed SPI and pepsin-hydrolyzed glycinin-rich fraction. This observation indicated that beta-conglycinin is a better precursor for antihypertensive peptides than glycinin. Additionally, the inhibitory activity of the papain-hydrolyzed SPI was thermally stable. This work demonstrated, for the first time, that selective hydrolysis to release peptides with ACE inhibitory activity can be accomplished without inducing extensive hydrolysis and performing unnecessary fractionation.