ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins

Mario Domínguez Magaña, Maira Segura-Campos, Gloria Dávila-Ortiz, David Betancur-Ancona, Luis Chel-Guerrero

Research output: Contribution to journalArticle

10 Citations (Scopus)

Abstract

© 2015, Sociedade Brasileira de Ciencia e Tecnologia de Alimentos, SBCTA. All rights reserved. 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.
Original languageAmerican English
Pages (from-to)167-174
Number of pages8
JournalFood Science and Technology
DOIs
StatePublished - 1 Jan 2015

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Phaseolus lunatus
pancreatin
Phaseolus
protein concentrates
subtilisin
peptidyl-dipeptidase A
Pancreatin
Peptidyl-Dipeptidase A
pepsin
Subtilisins
hydrolysates
Pepsin A
peptides
Seeds
flour
Flour
seeds
Peptides
Proteins
proteins

Cite this

Magaña, Mario Domínguez ; Segura-Campos, Maira ; Dávila-Ortiz, Gloria ; Betancur-Ancona, David ; Chel-Guerrero, Luis. / ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins. In: Food Science and Technology. 2015 ; pp. 167-174.
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ACE-I inhibitory properties of hydrolysates from germinated and ungerminated Phaseolus lunatus proteins. / Magaña, Mario Domínguez; Segura-Campos, Maira; Dávila-Ortiz, Gloria; Betancur-Ancona, David; Chel-Guerrero, Luis.

In: Food Science and Technology, 01.01.2015, p. 167-174.

Research output: Contribution to journalArticle

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AU - Segura-Campos, Maira

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AB - © 2015, Sociedade Brasileira de Ciencia e Tecnologia de Alimentos, SBCTA. All rights reserved. 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.

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