Angiotensin I-converting enzyme inhibitory activity in lima bean (Phaseolus Lunatus) protein hydrolysates produced with alcalase or pepsin-pancreatin

L. Chel-Guerrero, M. Domínguez-Magaña, G. Dávila-Ortiz, D. Betancur-Ancona

Producción científica: Capítulo del libro/informe/acta de congresoCapítulorevisión exhaustiva

Resumen

Protein concentrates from ungerminated and germinated lima bean Phaseolus lunatus seed flours were hydrolyzed with alcalase 2.4L or pepsin-pancreatin sequential hydrolysis, and ACE inhibitory activity measured in the different hydrolysis treatments. A 23 factorial design with four replicates of the central trial was used. Evaluated factors were protein concentrate source (ungerminated seeds, PC1; germinated seeds, PC2), enzyme/substrate ratio E/S (1/50 or 1/10) and hydrolysis time (0.5 or 2.0 h for alcalase; 1 or 3 h for pepsin-pancreatin). Degree of hydrolysis (DH) was high for the alcalase hydrolysates (24.12-58.94%), but the pepsin-pancreatin hydrolysates exhibited the highest ACE inhibitory activity (IC50 = 0.250-0.692 mg/mL). Under the tested conditions, the hydrolysates with the highest ACE inhibitory activity were produced with sequential pepsin-pancreatin using either PC1 at 1 h hydrolysis time and a 1/10 E/S ratio or PC2 at 1 h hydrolysis time and a 1/50 E/S ratio. Lima bean protein hydrolysates prepared with alcalase or pepsin-pancreatin are a potential ingredient in the production of physiologically functional foods with antihypertensive activity.

Idioma originalInglés
Título de la publicación alojadaAngiotensin
Subtítulo de la publicación alojadaNew Research
EditorialNova Science Publishers, Inc.
Páginas131-148
Número de páginas18
ISBN (versión impresa)9781621007739
EstadoPublicada - ene. 2012

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