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Bioactive peptides produced from enhanced common bean cultivars inhibit angiotensin converting enzyme activity (647.14)
Author(s) -
MojicaContreras Luis,
Mejia Elvira
Publication year - 2014
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.28.1_supplement.647.14
Subject(s) - phaseolus , chemistry , cultivar , enzyme , food science , peptide , angiotensin converting enzyme , biochemistry , botany , biology , endocrinology , blood pressure
Common bean ( Phaseolus vulgaris L .) is a good source of proteins (16‐33%), vitamins, minerals and complex carbohydrates. The objective was to produce, characterize and evaluate the angiotensin converting enzyme (ACE) inhibition and antioxidant capacity (AC) of bioactive peptides from proteins of common bean cultivars from Mexico and Brazil. Bean protein isolates were hydrolyzed by pepsin‐pancreatin and the molecular mass of the produced peptides determined by mass spectrometry. Phaseolin and lectin were the major proteins identified in the studied common beans. Forty seven abundant peptides were identified ranging from 347 to 3067 Da in beans BRS‐Horizonte, BRS‐ Pontal, Perola and Black‐Otomi; the black bean presented the highest amount of identified peptides (689.3, 713.4, 959.6, 981.6 and 1275.7 Da). Common bean Pontal showed the highest AC value (274 mmol ± 0.8 TE/g protein) and BRS‐Horionte the lowest (240 ± 3.8 mmol TE/g protein). ACE inhibition by peptides from Black‐Otomi (YG, RP, GT, GG, DG, NY, CF) was the highest (IC 50 = 0.29 ± 0.08 mg /mL) and Pontal the lowest (IC 50 = 0.45 ± 0.06 mg/mL), p < 0.05. Mexico and Brazil cultivars showed similar peptide pattern. Peptides from common bean showed high ACE inhibitor activity, high AC, and potential to enhance health and wellness if used as functional ingredients. Grant Funding Source : Supported by CONACYT, Research Council for Science and Technology