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

Food Science and Technology (Campinas)

Mario Domínguez Magaña¹  Maira Segura-campos¹  Gloria Dávila-ortiz¹  David Betancur-ancona¹  Luis Chel-guerrero¹ 

关键词: P. lunatus;    hydrolysates;    peptides;    ACE inhibitory activity;   

DOI  :  10.1590/1678-457X.6551

来源: SciELO

【 摘 要 】

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.

【 授权许可】

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