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Angiotensin‐converting enzyme‐inhibitory activity in protein hydrolysates from normal and anthracnose disease‐damaged Phaseolus vulgaris seeds
Author(s) -
HernándezÁlvarez Alan Javier,
CarrascoCastilla Janet,
DávilaOrtiz Gloria,
Alaiz Manuel,
GirónCalle Julio,
VioquePeña Javier,
JacintoHernández Carmen,
JiménezMartínez Cristian
Publication year - 2012
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.5841
Subject(s) - phaseolus , hydrolysate , food science , colletotrichum lindemuthianum , enzyme , angiotensin converting enzyme , biology , chemistry , hydrolysis , biochemistry , botany , horticulture , blood pressure , endocrinology
Abstract BACKGROUND: Bean seeds are an inexpensive source of protein. Anthracnose disease caused by the fungus Colletotrichum lindemuthianum results in serious losses in common bean ( Phaseolus vulgaris L.) crops worldwide, affecting any above‐ground plant part, and protein dysfunction, inducing the synthesis of proteins that allow plants to improve their stress tolerance. The aim of this study was to evaluate the use of beans damaged by anthracnose disease as a source of peptides with angiotensin‐converting enzyme (ACE‐I)‐inhibitory activity. RESULTS: Protein concentrates from beans spoiled by anthracnose disease and from regular beans as controls were prepared by alkaline extraction and precipitation at isolelectric pH and hydrolysed using Alcalase 2.4 L. The hydrolysates from spoiled beans had ACE‐I‐inhibitory activity (IC 50 0.0191 mg protein mL −1 ) and were very similar to those from control beans in terms of ACE‐I inhibition, peptide electrophoretic profile and kinetics of hydrolysis. Thus preparation of hydrolysates using beans affected by anthracnose disease would allow for revalorisation of this otherwise wasted product. CONCLUSION: The present results suggest the use of spoiled bean seeds, e.g. anthracnose‐damaged beans, as an alternative for the isolation of ACE‐I‐inhibitory peptides to be further introduced as active ingredients in functional foods. © 2012 Society of Chemical Industry