Resumo

MARRUFO ESTRADA, Duly Marianely; CHEL GUERRERO, Luis; BETANCUR ANCONA, David  e  HERNANDEZ ESCALANTE, Víctor. Angiotensin I-Converting Enzyme inhibition with protein hydrolysates from Jatropha curcas. Acta bioquím. clín. latinoam. [online]. 2012, vol.46, n.3, pp.385-392. ISSN 0325-2957.

In vitro angiotensin I-converting enzyme (ACE) inhibitory activity was evaluated in protein hydrolysates from defatted meal and protein isolate from Jatropha curcas L. Seed, in order to determine their potential inclusion in functional food formulation. Hydrolysates were produced using Alcalase® or a sequential pepsin-pancreatin enzymatic system. Mean inhibitory concentration (IC50) was used to measure the degree of ACE enzymatic activity inhibition. Bioactivity was evaluated in the hydrolysates with the lowest hydrolysis time (60 min) given that no differences in degree of hydrolysis in terms of reaction time in each system were observed (60, 90 and 120 min) in the enzymatic hydrolysis kinetics for the defatted meal and protein isolate. The protein isolate exhibited the highest inhibitory effect, as seen in the IC50 values: 2.8 µg/mL in the alcalase system and 7.0 µg/mL in the pepsin-pancreatin system. Hydrolysates from J. curcas seed exhibit ACE inhibition and could be incorporated into functional foods or treatments for those suffering hypertension.

Palavras-chave : Angiotensin I-converting enzyme inhibitors; Jatropha curcas; Protein hydrolysates; Antihypertensive agents; Bioactive peptides.

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