TY - JOUR
T1 - ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins
AU - Magaña, Mario Domínguez
AU - Segura-Campos, Maira
AU - Dávila-Ortiz, Gloria
AU - Betancur-Ancona, David
AU - Chel-Guerrero, Luis
N1 - Publisher Copyright:
© 2015, Sociedade Brasileira de Ciencia e Tecnologia de Alimentos, SBCTA. All rights reserved.
PY - 2015
Y1 - 2015
N2 - Phaseolus lunatus protein concentrates and the proteases Alcalase(R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase(R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. On the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high- performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides’ inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase(R) and Pepsin-Pancreatin.
AB - Phaseolus lunatus protein concentrates and the proteases Alcalase(R) and Pepsin-Pancreatin were used for the production of protein hydrolysates that inhibit angiotensin-I converting enzyme (ACE). Protein concentrate obtained from germinated and ungerminated seeds flour was hydrolyzed with Alcalase(R) at enzyme/substrate ratio (E/S) 1/10 and during 0.5 and 2.0 h, respectively. On the other hand, protein concentrate obtained from ungerminated (E/S: 1/10) and germinated (E/S: 1/50) seeds flour was sequentially hydrolyzed with Pepsin-Pancreatin during 1.0 and 3.0 h, respectively. Peptide fractions with ACE inhibitory activity in a range of 0.9 to 3.8 µg/mL were obtained by G-50 gel filtration chromatography and high- performance liquid chromatography C18 reverse phase chromatography. The observed amino acid composition suggests a substantial contribution of hydrophobic residues to the peptides’ inhibitory potency, which potentially acts via blocking of angiotensin II production. These results show that P. lunatus seed proteins are a potential source of ACE inhibitory peptides when hydrolyzed with Alcalase(R) and Pepsin-Pancreatin.
KW - ACE inhibitory activity
KW - Hydrolysates
KW - P. lunatus
KW - Peptides
UR - http://www.scopus.com/inward/record.url?scp=84929259903&partnerID=8YFLogxK
U2 - 10.1590/1678-457X.6551
DO - 10.1590/1678-457X.6551
M3 - Artículo
SN - 0101-2061
VL - 35
SP - 167
EP - 174
JO - Food Science and Technology
JF - Food Science and Technology
IS - 1
ER -