Journal of Nutrition & Food Sciences
Open Access

Abstract

Electrophoretic Profiles and Angiotensin I-Converting Enzyme Inhibitory Activities of Nine Varieties of Phaseolus Vulgaris Protein Hydrolysates

Xin Rui, Joyce I. Boye, Chockry Barbana, Benjamin K. Simpson and Shiv O. Prasher

Nine dry bean (Phaseolus vulgaris) varieties largely grown in Canada were subjected to digestion using trypsin and in vitro gastrointestinal simulation (GIS) followed by a study of their in vitro ACE inhibitor properties and digestibility. GIS hydrolysates of all varieties presented significantly higher ACE inhibitory activities and degree of hydrolysis (DH) compared to those of trypsin hydrolysates (P < 0.05). Cranberry and light red kidney bean protein isolates contained ‘T’ type phaseolin and had higher DH values during both digestions, with average ACE inhibitory activities of 281.7–281.8 μg/mL and 141.6–185.1 μg/mL, respectively, for tryptic and GIS hydrolysates. The other seven bean varieties contained ‘S’ type phaseolin, and of these small red bean showed the lowest ACE inhibitory activities for both trypsin (IC₅₀ of 170 μg/mL) and GIS (IC₅₀ of 118 μg/mL) digestion, followed by navy bean, with IC₅₀ of 200 μg/mL (trypsin digestion) and 137 μg/mL (GIS digestion). The results demonstrated that both methods of digestions yielded bioactive peptides, however, differing peptide profiles of the bean protein hydrolysates affected their in vitro ACE inhibitory property.