Lima Bean (Phaseolus lunatus) Protein Hydrolysates with ACE-I Inhibitory Activity

Luis Chel-Guerrero, Mario Domínguez-Magaña, Alma Martínez-Ayala, Gloria Dávila-Ortiz, David Betancur-Ancona

Centro de Investigación en Biotecnología Aplicada, Instituto Politécnico Nacional, Tlaxcala, México..
Escuela Nacional de Ciencias Biológicas, Instituto Politécnico Nacional, Miguel Hidalgo, México.
Facultad de Ingeniería Química, Universidad Autónoma de Yucatán, Mérida, México.

DOI: 10.4236/fns.2012.34072                

Abstract

Several protein sources can be used to produce bioactive peptides with angiotensin I-converting enzyme (ACE) inhibittory activity. Protein concentrates from ungerminated and germinated lima bean Phaseolus lunatus seed flours were hydrolyzed with Alcalase 2.4 L or pepsin-pancreatin sequential hydrolysis, and ACE inhibitory activity measured in the different hydrolysis treatments. Protein hydrolysate production was analyzed with a 2³ factorial design with four replicates of the central treatment. 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.

Keywords

Lima Bean; Degree of Hydrolysis; ACE Inhibition; Protein Hydrolysates; IC50

Conflicts of Interest

The authors declare no conflicts of interest.

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