Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain (original) (raw)
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Characterization and ACE-Inhibitory Activity of Amaranth Proteins
Journal of Food Science, 2009
Amaranth seeds have been considered as an excellent alternative or complementary source of food protein due to their balanced amino acid composition. However, their potential as a source of bioactive peptides has not been explored. The present study is aimed at characterizing and evaluating the activity of the angiotensin converting enzyme inhibitor of the amaranth protein concentrate and of hydrolysates produced with Alcalase. The protein concentrate, after simulated gastrointestinal digestion, showed lower angiotensin converting enzymeinhibitory activity (IC 50 of 0.439 ± 0.018 mg protein/mL and 0.475 ± 0.021 mg protein/mL, for untreated and heat treated protein concentrate, respectively) than the hydrolysates produced with Alcalase, before and after simulated gastrointestinal digestion (IC 50 0.118 ± 0.009, 0.123 ± 0.007, 0.137 ± 0.002, and 0.176 ± 0.014 mg protein/mL, respectively). The simulated gastrointestinal digestion (pepsin-pancreatin) did not significantly alter the angiotensinconverting enzyme inhibiting activity of the Alcalase hydrolysates, suggesting that the peptides of the hydrolysates were resistant to gastrointestinal hydrolysis. These results highlight the angiotensin converting enzyme-inhibitory potential of amaranth proteins, which is an indication of their health-promoting potential.
Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity
Food Chemistry, 2011
The objective of this work was to study the hydrolytic release of encrypted peptides with antihypertensive activity from storage proteins of Amaranthus mantegazzianus, as determined by in vitro assays, for the first time by in vivo studies in animal models, and by ex vivo assays. Hydrolysates with hydrolysis degree (DH) of 45% and 65% (IC50 0.12 mg/ml, equivalent to 300-600 lM) exhibited an angiotensin-I converting enzyme 1 (ACE) inhibitory activity equal or higher than the potential inhibitory of the average antihypertensive peptides registered in the BIOPEP database and of semi-purified Amaranthus hypochondriacus albumin and globulin protein fractions. Intragastric administration of hydrolysates with DH of 45% was effective in lowering blood pressure of male spontaneously hypertensive rats (SHR). Experiments performed in papillary muscles isolated from hearts and with isolated aortic smooth muscle of SHR suggest that the hypotensive effect could be attributed to a lowering of the peripheral resistance. We assume that the amaranth hydrolysates would be acting at the level of the local or autocrine renin-angiotensin system (RAS).
Journal of Agricultural and Food Chemistry, 2017
Among the factors affecting the development of cardiovascular diseases, hypertension is one of the most important. Research done on amaranth proteins has demonstrated their hypotensive capacity in vivo and in vitro; nevertheless, the mechanism underlying this effect remains unclear. The aim of this study was to analyze in vitro the inhibition of peptides derived from an amaranth hydrolysate (AHH) on other RAS enzymes other than ACE. The chymase and renin activities were studied. AHH was not able to inhibit chymase activity, although a dose−response effect was found on renin activity (IC 50 0.6 mg/mL). To provide an approach to the renin inhibition mechanism, we analyzed AHH renin inhibition kinetics and performed a structural characterization of the peptides involved in the effect in terms of molecular size and hydrophobicity. Results suggest that amaranth peptides exhibit renin competitive inhibition behavior. Renin inhibition potency was directly related to peptide hydrophobicity. RP-HPLC separation of AHH and subsequent analysis of the peptide sequences showed 6 peptides belonging to 11S globulin (that can be grouped into 3 families) that would be responsible for renin inhibition. These results demonstrate that Amaranthus hypochondriacus seeds are an adequate source of peptides with renin inhibitory properties that could be used in functional food formulations.
Amaranth as a Source of Antihypertensive Peptides
Frontiers in Plant Science, 2020
Amaranth is an ancestral crop used by pre-Columbian cultures for 6000 to 8000 years. Its grains have a relevant chemical composition not only from a nutritional point of view but also due to the contribution of components with good techno-functional properties and important potential as bioactive compounds. Numerous studies have shown that amaranth storage proteins possess encrypted sequences that, once released, exhibit different physiological activities. One of the most studied is antihypertensive activity. This review summarizes the progress made over the last years (2008-2020) related to this topic. Studies related to inhibition of different enzymes of the Renin-Angiotensin-Aldosterone system, in particular Angiotensin Converting Enzyme (ACE) and Renin, as well as those referring to potential modulation mechanisms of tissue or local Renin-Angiotensin-Aldosterone system, are analyzed, including in silico, in vitro, in vivo, and ex vivo assays. Furthermore, the potential use of these bioactive peptides or products containing them, in the elaboration of functional food matrices is discussed. Finally, the most relevant conclusions and future requirements in research and development of food products are presented.
Journal of the Science of Food and Agriculture, 2011
BACKGROUND: Amaranth 7S globulin is a minor globulin component and its impact on the properties of an amaranth protein ingredient depends on its proportion in the variety of amaranth being considered. Some physicochemical, functional and angiotesin I-converting enzyme (ACE) inhibitory properties of amaranth vicilin were studied in this work and compared with the 11S globulin. RESULTS: Fluorescence spectroscopy results indicated that 7S globulin tryptophans were more exposed to the solvent and, by calorimetry, the 7S globulin denaturation temperature (T d) was found lower than the 11S globulin T d , suggesting a more flexible structure. The 7S globulin surface hydrophobicity was higher than that of the 11S globulin, which is in agreement with the better emulsifying properties of the 7S globulin. The solubility in neutral buffer of the 7S globulin (851 ± 25 g kg −1) was also higher than that of the 11S globulin (195 ± 6 g kg −1). Bioinformatic analyses showed the presence of ACE inhibitory peptides encrypted in 7S tryptic sequences and peptides released after in vitro gastrointestinal digestion showed a high ACE-inhibitory capacity (IC 50 = 0.17 g L −1), similar to that of 11S globulin peptides. CONCLUSION: Compared with the 11S globulin, the 7S globulin presents similar ACE inhibitory activity and some functional advantages, better solubility and emulsifying activity, which suits some food requirements. The functional behavior has been related with the structural properties.
Current Pharmaceutical Design, 2009
The existence of endogenous bioactive protein or peptide with angiotensin-converting enzyme (ACE) inhibitory activity in snakehead fish fillet is promising to be investigated. The purposes of this research were to extract ACE inhibitory endogenous protein or peptide from snakehead fish fillet and to fractionate the active compounds using ultrafiltration. The extraction employed two solvents, i.e. aquadest and 50% ethanol. Fractionation was conducted using ultrafiltration membranes of 10,000; 5,000 and 3,000 Molecular W eight Cut Off (MW CO) to separate the protein or peptide into the sizes of >10 kDa, 5-10 kDa, 3-5 kDa and <3 kDa. The parameters observed were protein and peptide content, ACE inhibitory activity (in vitro) and also protein and peptide profiles. The result revealed that the snakehead fish fillet contained ACE inhibitory endogenous bioactive protein or peptide. The 50% ethanol was more effective in extracting peptide of <10 kDa than the aquadest. Yet, the aquadest was better in extracting higher molecular weight protein of >10 kDa than the 50% ethanol. The fraction of <3 kDa by aquadest had the highest ACE inhibitor activity per g protein (7.85% inhibition of ACE per g protein). Thus, the fraction of <3 kDa aquadest is the most promising option for further research and development of natural anti-hypertension compound. From the result, snakehead fish fillet was potential to be utilized as a functional food as well as functional ingredient to fight hypertension.
Chickpea seeds are the preferred source of proteins possessing health care functions in countries across the world. In the present investigation, the chickpea seed protein subjected to enzymatic hydrolysis produced bioactive peptides that were able to inhibit the angiotensin converting enzyme (ACE) and cytotoxic effect. Experimental screening was to test the efficacy of hydrolytic enzymes in chickpea seed for production of bioactive peptides was therefore carried out. The optimum hydrolysis times for each protein hydrolysate prepared by alcalase which inhibited ACE-I with IC50 value of 52.22 µg/ml. The protein hydrolysate was further subjected to antiproliferative evaluation for breast cancer cell lines MCF-7 and MDA-MB-231 and the IC50 was observed 0.71 mg/ml and 0.78 mg/ml respectively. Study indicated the potential of chickpea proteins as a source of ACE-inhibitory and antiproliferative potential to foresee the application of chickpea proteins into functional foods.
Journal of the Science of Food and Agriculture, 2002
Utilización de aislados proteicos de colza para la producción de péptidos con actividad inhibidora de la enzima convertidora de la angiotensina (ECA). La actividad de ECA está relacionada con una presión arterial alta y enfermedades cardíacas. Un aislado proteico de colza se hidrolizó con alcalasa para estudiar la posible presencia de péptidos inhibidores de ECA en el hidrolizado. La hidrólisis durante 30 min produjo el hidrolizado con la mayor actividad inhibidora de ECA. Dos fracciones de este hidrolizado, obtenidas por cromatografía de filtración en gel Biogel P2, se usaron para la purificación de péptidos inhibidores de ECA. Tres fracciones con actividad inhibidora de ECA se purificaron mediante HPLC en fase reversa de las fracciones obtenidas mediante Biogel P2. Esto demuestra que los hidrolizados proteicos de colza representan una buena fuente de péptidos inhibidores de ECA. PALABRAS-CLAVE: Aislado proteico-Colza-Enzima convertidora de angiotensina-Hidrolizado proteico-Péptidos inhibidores SUMMARY Utilisation of rapeseed protein isolates for production of peptides with angiotensin I-converting enzyme (ACE)inhibitory activity. ACE activity is related to increased arterial pressure and coronary diseases. A rapeseed protein isolate was hydrolyzed with the protease Alcalase in order to investigate the possible presence of ACE inhibitory peptides in the resulting hydrolysates. Hydrolysis for 30 min yielded a hydrolysate with the highest ACE inhibitory activity. Two fractions of this hydrolysate obtained by Biogel P2 gel filtration chromatography were used for further purification of ACE inhibitory peptides. Three fractions with ACE inhibitory activity were purified by reverse-phase HPLC of Biogel P2 fractions. This demonstrates that rapeseed protein hydrolysates represent a good source of ACE inhibitory peptides.
Food chemistry, 2015
An alkaline extracted brewers' spent grain protein-enriched isolate (BSG-PI) was hydrolysed using Alcalase, Corolase PP, Flavourzyme and Promod 144MG, yielding Alc hydrolysate (H), CorH, FlavH and ProH, respectively. The degree of hydrolysis (DH) of the protein hydrolysates varied from 4.45% for ProH to 16.4% for CorH. The in vitro ACE inhibitory activity of the BSG-PI increased significantly following 15min incubations with Alcalase, Corolase PP and Flavourzyme. The 5kDa ultrafiltration permeates of FlavH and CorH resulted in lower ACE IC50 values than their respective hydrolysates. The bioactivity of the BSG-PI hydrolysates was retained after simulated gastrointestinal digestion (SGID) while SGID also resulted in the release of ACE inhibitory peptides from the BSG-PI and ProH. UPLC-MS/MS analysis resulted in the identification of 34 peptides. Of 12 synthesised peptides, IVY and ILDL were the most potent, having ACE IC50 values at 80.4±11.9 and 96.4±8.36μM, respectively.
Winged bean [Psophocarpus tetragonolobus (L.) DC.] seed is a potential underexploited source of vegetable protein due to its high protein content. In the present work, undefatted and defatted winged bean seed hydrolysates, designated as UWBSH and DWBSH, respectively were produced separately by four proteolytic enzymes namely Flavourzyme, Alcalase, Bromelain, and Papain using pH-stat method in a batch reactor. Enzymatic hydrolysis was carried out over a period of 0.5 to 5 h. UWBSH and DWBSH produced were tested for their ACE inhibitory activity in relation to the hydrolysis time and degree of hydrolysis (DH). Maximum ACE inhibitory activity, both for UWBSH and DWBSH, were observed during 3 to 5 h of hydrolysis. Both, UWBSH (DH 91.84 %), and DWSBH (DH 18.72 %), produced by Papain at 5 h hydrolysis, exhibited exceptionally high ACE inhibitory activity with IC 50 value 0.064 and 0.249 mgmL −1 , respectively. Besides, papain-produced UWBSH and DWBSH were further frac-tionated into three fractions based on molecular weight (UWBSH-I, <10 kDa; UWBSH-II, <5 kDa; UWBSH-III, <2 kDa) and (DWBSH-I, <10 kDa; DWBSH-II, <5 kDa; DWBSH-III, <2 kDa). UWBSH-III revealed the highest ACE inhibitory activity (IC 50 0.003 mgmL −1) compared with DWBSH-III (IC 50 0.130 mgmL −1). The results of the present investigation revealed that winged bean seed hydro-lysates can be explored as a potential source of ACE inhibitory peptides suggesting their uses for physiological benefits as well as for other functional food applications. Keywords Undefatted and defatted winged bean seed. Proximate analysis. ACE inhibitory activity. IC 50 value. Degree of hydrolysis. pH-stat titration