%0 Journal Article
%T Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis
%A Maira Rubi Segura Campos
%A Fanny Peralta Gonz¨¢lez
%A Luis Chel Guerrero
%A David Betancur Ancona
%J International Journal of Food Science
%D 2013
%I Hindawi Publishing Corporation
%R 10.1155/2013/158482
%X Synthetic angiotensin I-converting enzyme (ACE-I) inhibitors can have undesirable side effects, while natural inhibitors have no side effects and are potential nutraceuticals. A protein-rich fraction from chia (Salvia hispanica L.) seed was hydrolyzed with an Alcalase-Flavourzyme sequential system and the hydrolysate ultrafiltered through four molecular weight cut-off membranes (1£¿kDa, 3£¿kDa, 5£¿kDa, and 10£¿kDa). ACE-I inhibitory activity was quantified in the hydrolysate and ultrafiltered fractions. The hydrolysate was extensive (DH = 51.64%) and had 58.46% ACE-inhibitory activity. Inhibition ranged from 53.84% to 69.31% in the five ultrafiltered fractions and was highest in the <1£¿kDa fraction (69.31%). This fraction¡¯s amino acid composition was identified and then it was purified by gel filtration chromatography and ACE-I inhibition measured in the purified fractions. Amino acid composition suggested that hydrophobic residues contributed substantially to chia peptide ACE-I inhibitory strength, probably by blocking angiotensin II production. Inhibitory activity ranged from 48.41% to 62.58% in the purified fractions, but fraction F1 (1.5¨C2.5£¿kDa) exhibited the highest inhibition (IC50 = 3.97£¿¦Ìg/mL; 427¨C455£¿mL elution volume). The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system. 1. Introduction Cardiovascular disease (CVD) affects the heart and blood vessels and is the principal cause of death worldwide. Considered the primary risk factor for CVD, high blood pressure, or hypertension, consists of a sustained increase in blood pressure levels. In 2000, >25% of the population worldwide (approximately 1 billion) suffered from hypertension, a figure predicted to increase to 1.56 billion by 2025 [1]. Angiotensin I-converting enzyme (peptidyl carboxy peptidase, EC 3.4.15.1, ACE) belongs to the class of zinc proteases that require zinc and chloride for activation. ACE plays an important role in blood pressure regulation via the renin-angiotensin system (RAS) and the kallikrein-kinnin system (KKS). In the KKS, ACE inactivates the vasodilator bradykinin, while in the RAS, ACE acts as an exopeptidase cleaving His-Leu from the C-terminal of decapeptide angiotensin I and producing the potent vasoconstrictor octapeptide angiotensin II [2]. Use of enzyme technologies for protein recovery and modification has led to production of a broad spectrum of food ingredients and industrial products. Hydrolysis selectivity is commonly manipulated by
%U http://www.hindawi.com/journals/ijfs/2013/158482/