Electrophoretic Profiles and Angiotensin I-Converting Enzyme Inhibitory Activities of Nine Varieties of Phaseolus Vulgaris Protein HydrolysatesXin Rui1,2, Joyce I. Boye1*, Chockry Barbana1, Benjamin K. Simpson3 and Shiv O. Prasher2
- *Corresponding Author:
- Joyce Irene Boye
Food Research and Development Centre
Agriculture and Agri-Food Canada
3600 Casavant Blvd. W., St-Hyacinthe, QC, J2S 8E3, Canada
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Received Date: July 05, 2011; Accepted Date: August 10, 2012; Published Date: August 13, 2012
Citation: Rui X, Boye JI, Barbana C, Simpson BK, Prasher SO (2012) Electrophoretic Profiles and Angiotensin I-Converting Enzyme Inhibitory Activities of Nine Varieties of Phaseolus Vulgaris Protein Hydrolysates. J Nutr Food Sci 2:156. doi: 10.4172/2155-9600.1000156
Copyright: © 2012 Rui X, et al. This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.
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.