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

• Autor(a) principal: Magaña,Mario Domínguez
• Data de Publicação: 2015
• Outros Autores: Segura-Campos,Maira, Dávila-Ortiz,Gloria, Betancur-Ancona,David, Chel-Guerrero,Luis
• Tipo de documento: Artigo
• Idioma: eng
• Título da fonte: Food Science and Technology (Campinas)
• Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0101-20612015000100167
• topic: P. lunatus; hydrolysates; peptides; ACE inhibitory activity

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.