Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity

Fritz, Mariana; Vecchi, Bruno; Rinaldi, Gustavo; Añón, Marı́a Cristina

doi:10.1016/j.foodchem.2010.11.065

Cited by 110 publications

(101 citation statements)

References 30 publications

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“…Another chronic disease is cardiovascular disease which is associated with hypertension (arterial blood pressure sustained elevation) and is of great incidence in developed countries [27]. The dipeptidyl carboxypeptidase ACE (angiotensin I-converting enzyme) regulates arterial pressure by the renin-angiotensin system for which ACE inhibition reduces arterial pressure by reducing the levels of angiotensin II (vasoconstrictor) and increasing bradykinin (vasodilator) [27].…”

Section: Introductionmentioning

confidence: 99%

“…The dipeptidyl carboxypeptidase ACE (angiotensin I-converting enzyme) regulates arterial pressure by the renin-angiotensin system for which ACE inhibition reduces arterial pressure by reducing the levels of angiotensin II (vasoconstrictor) and increasing bradykinin (vasodilator) [27]. Captopril and enalapril are reference drugs to treat hypertension but they have secondary effects for which foods could avoid [28].…”

Section: Introductionmentioning

confidence: 99%

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Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Fernández‑Fernández¹,

López-Pedemonte²,

Medrano-Fernández³

2017

FNS

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Whey proteins are known for their high nutritional value and bioactivity, notably great potential is found on α-lactalbumin. The objective of this study was to evaluate antioxidant, antiglycant and ACE (angiotensin converting enzyme)-inhibitory activity of α-lactalbumin peptides obtained from enzymatic hydrolysis with Alcalase through different hydrolysis conditions. The optimization of enzymatic hydrolysis was studied by response surface methodology variating enzyme:substrate ratio (0.0050%, 0.0525% and 0.1000% w/w) and time (0, 30 and 60 minutes) measuring antioxidant activity by ABTS and ORAC-FL (response variables), founding an augment of this activity with time. Characterization of seven samples showed increasing hydrolysis with time. Hydrolysate obtained with 0.1000% w/w and 60 minutes demonstrated higher antioxidant activity related to greater hydrolysis. This hydrolysate did not show antiglycant activity but promoted advanced glycation end products formation with methylglyoxal and glucose. In contrast, this sample showed 30% of ACE inhibition when compared to Captopril, having great potential by enhancing hydrolysis.

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Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Fernández‑Fernández¹,

López-Pedemonte²,

Medrano-Fernández³

2017

FNS

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“…These studies involve the use of commercial enzymes (alcalase, flavourzyme, pepsin, pancreatin, tripsin, chymotrypsin, neutrase, etc.) at different hydrolysis time, enzyme/substrate ratios, and enzyme's specific pH and temperatures (Alashi et al, 2014;Dnuh et al, 2014;Ahn et al, 2012;Zhao et al, 2012;Fritz et al, 2011). The hydrolysis conditions and the specificity of the enzyme are key factors for protein hydrolysis, because these factors influence the sites and the peptide linkages that will be hydrolyzed.…”

Section: Introductionmentioning

confidence: 99%

Antioxidant activity of black bean (Phaseolus vulgaris L.) protein hydrolysates

et al. 2016

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The objective of this work was to study the effect of enzymatic hydrolysis of black bean protein concentrate using different enzymes. Bean proteins were extracted and hydrolyzed over a period of 120 min using the enzymes pepsin or alcalase. The protein hydrolysates' molecular weight was assayed by electrophoresis and the antioxidant activity was evaluated by the capturing methods of free radicals ABTS•+ and DPPH. Electrophoretic results showed that the bands above 50 kDa disappeared, when the beans protein was subjected to hydrolysis with pepsin. The bean protein hydrolysate obtained by hydrolysis with alcalase enzyme, showed higher antioxidant activity for inhibition of the radical ABTS•+ . However, the hydrolysates obtained by hydrolysis with pepsin had higher antioxidant activity for inhibition of the radical DPPH. The use of pepsin and alcalase enzymes, under the same reaction time, produced black bean protein hydrolysates with different molecular weight profiles and superior antioxidant activity than the native bean protein.

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“…However, the same milk product, after an in vitro partial digestion, lost most of its bioactivity and thus its effectiveness as FF (Domínguez-González et al 2014). On the other hand, amaranth protein hydrolysates with angiotensin I-converting-enzyme-inhibitory activity (ACEIA) and dipeptidyl peptidase IV inhibitory activity (DPPIVIA) remained constant after in vitro or in vivo digestion (Fritz et al 2011;. As a result, the stability of bioactive compounds in foods and foodstuffs must be evaluated throughout the different steps of production and consumption.…”

Section: Introductionmentioning

confidence: 99%

“…(Dexter and Middelberg 2008). Particularly, storage proteins of amaranth grain, in their primary structure, contain peptides with ACEIA (Fritz et al 2011;, DPPIVIA (Montoya-Rodriguez et al 2015;Velarde-Salcedo et al 2013) and antithrombotic activity (Sabione et al 2015), among others. These bioactivities would be highly relevant in the making of N and FF.…”

Section: Introductionmentioning

confidence: 99%

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

et al. 2016

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The aim of this work was to assess the effects of temperature (T), time (t) and pH treatments and an in vitro digestion on the stability of the angiotensin I-convertingenzyme-inhibitory activity (ACEIA) and antithrombotic activity (ATA; assessed as inhibition of platelet aggregation) of selected protein hydrolysates of amaranth named Alb1H103 and GloH88 and GluH24 with dipeptidyl peptidase IV inhibitory activity (DPPIVIA). Heat treatment (40-100°C) for 1 h showed no significant differences among ACEIA, DPPIVIA and ATA of the heated hydrolysates at pH 4 and 7. There was no statistically significant loss of any bioactivity under heat treatment for 3 h at pH 4.0. Alb1H103 and GluH24 maintained the inhibitory activity of ACE and ATA at pH 7.0 for 3 h, whereas GloH88 maintained ACEIA and ATA for 2.0 h at pH 7.0. The pH effect on hydrolysates bioactivity was assessed in the range of 2.0-12.0. This was negligible on ACEIA, ATA and DPPIVIA. The in vitro digestion was performed using pepsin, trypsin (T) and a-chymotrypsin (C). A previous treatment of hydrolysates with pepsin improved the proteolytic activities of T and C. The hydrolysates kept at 100°C for 1 h at pH 4.0, showed a significant increase in bioactivity. Conversely, a treatment at pH 7.0 showed no significant difference (p \ 0.05) in the hydrolysates bioactivities after their digestion. Thus, biological activity of hydrolysates may be preserved or enhanced, depending on their processing conditions.

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Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity

Cited by 110 publications

References 30 publications

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Antioxidant activity of black bean (Phaseolus vulgaris L.) protein hydrolysates

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

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Amaranth seed protein hydrolysates have in vivo and in vitro antihypertensive activity

Cited by 110 publications

References 30 publications

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of &lt;i&gt;α&lt;/i&gt;-Lactalbumin

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of &lt;i&gt;α&lt;/i&gt;-Lactalbumin

Antioxidant activity of black bean (Phaseolus vulgaris L.) protein hydrolysates

Effects of heat and pH treatments and in vitro digestion on the biological activity of protein hydrolysates of Amaranthus hypochondriacus L. grain

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Product

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Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin

Evaluation of Antioxidant, Antiglycant and ACE-Inhibitory Activity in Enzymatic Hydrolysates of <i>α</i>-Lactalbumin