Effects of bioactive peptides encrypted in whey-, soy- and rice protein on local and systemic angiotensin-converting enzyme activity

Michelke, Lydia; Deußen, Andreas; Dieterich, Peter; Martin, Melanie

doi:10.1016/j.jff.2016.11.026

Cited by 11 publications

(13 citation statements)

References 31 publications

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“…This antihypertensive effect of IW was associated with decreased ACE activity and minimized myocardial remodeling [20]. As shown in previous studies, IW inhibits systemic ACE and also local tissue ACE activity [20,21], which plays a prominent role in vascular remodeling and cardiovascular homeostasis [6,22]. Evidence for ACE inhibition by IW in humans was provided by Kaiser et al [23], who reported a transient rise of IW plasma concentrations after oral intake that was correlated with reduced plasma ACE activity [23].…”

mentioning

confidence: 79%

“…The potential of rIW and cIW to inhibit rabbit lung ACE was analyzed as described in with the following modifications: 15 μL ACE solution (dissolved in PBS corresponding to 0.05 U/mL activity in the assay mixture), 65 μL Hip‐HL solution (5 mM) and either 10 μL PBS (blank) or 10 μL IW solution giving final peptide concentrations from 0.21 to 20.3 μM in the assay mixture were incubated for 1 h at 37°C. The enzymatic reaction was stopped with 95 μL HCl (0.33 M).…”

Section: Methodsmentioning

confidence: 99%

“…Plasma was separated by centrifugation from human whole blood (approved by the Ethics Committee of the Medical Faculty of Technische Universität Dresden, Germany, permission EK 299082014) and ACE activity determined as described in with the following modifications: 30 μL plasma, 50 μL Hip‐HL solution (5 mM) and either 10 μL PBS (blank) or 10 μL IW solution giving final peptide concentrations from 10.1 to 20.3 μM in the assay mixture were incubated for 30 min at 37°C. The enzymatic reaction was stopped with 95 μL HCl (0.33 M).…”

Section: Methodsmentioning

confidence: 99%

“…Permission for use of umbilical cords for isolation of HUVECs had been given by the Ethics Committee of the Medical Faculty of Technische Universität Dresden, Germany (permission EK 203112005). ACE activity was determined as described with modifications as follows: HUVECs were seeded in 48‐well plates (Corning Incorporated) exhibiting a cell growth area of approximately 0.95 cm 2 per well. In each well 200 μl Hip‐HL solution (4 mM, preheated to 37°C) and either 200 μL PBS (blank, preheated to 37°C) or IW solution (preheated to 37°C) giving final peptide concentrations from 2.15 to 125 μM in the assay mixture was added per well.…”

Section: Methodsmentioning

confidence: 99%

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Biotechnological production of the angiotensin‐converting enzyme inhibitory dipeptide isoleucine‐tryptophan

Michelke

Deußen

Kettner

et al. 2018

Engineering in Life Sciences

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Peptides with angiotensin‐converting enzyme (ACE)‐inhibitory and antihypertensive effects are suggested as innovative food additives to prevent or treat hypertension. Currently, these substances are isolated from food proteins following nonselective hydrolysis as a mixture of ACE‐inhibitory peptides and other protein fragments. This study presents an innovative biotechnological method, based on recombinant DNA technology that was established to specifically produce the ACE‐inhibitory dipeptide isoleucine‐tryptophan. In a first step, a repetitive isoleucine‐tryptophan construct fused to the maltose‐binding protein was generated and expressed in Escherichia coli BL21 cells. The chromatographically purified recombinant fusion protein was enzymatically hydrolyzed using α‐chymotrypsin to liberate the dipeptide isoleucine‐tryptophan. The identity of the liberated isoleucine‐tryptophan was confirmed by MS and derivatization of its N‐terminus. The ACE‐inhibitory effect of the recombinant dipeptide on soluble and membrane bound ACE was found to be indistinguishable from the inhibitory potential of the chemically produced commercially available dipeptide. The established experimental strategy represents a promising approach to the biotechnical production of sufficient amounts of recombinant peptide‐based ACE‐inhibitory and antihypertensive substances that are applicable as functional food additives to delay or even prevent hypertension.

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mentioning

confidence: 79%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Biotechnological production of the angiotensin‐converting enzyme inhibitory dipeptide isoleucine‐tryptophan

Michelke

Deußen

Kettner

et al. 2018

Engineering in Life Sciences

Self Cite

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“…They concluded that the animal proteins are more difficult to hydrolyze with specific plant proteases, and therefore it is necessary to continue studying more plant proteases such as the proteases in this study and enzyme complexes. On the other hand, Michelke et al (2017) reported that the soy, milk and egg proteins are an excellent source of BP although they have been hydrolyzed with microbial enzymes. Therefore, the use of plant proteases such as B. pinguin and B. karatas proteases can be a good alternative because they can resist a wide range of pH and temperatures that microbiological enzyme can no resist (Moreno-Hernández et al, 2017).…”

Section: Total Soluble Biopeptide Content (Tsp)mentioning

confidence: 99%

Antioxidant capacity of egg, milk and soy protein hydrolysates and biopeptides produced by Bromelia pinguin and Bromelia karatas-derived proteases

et al. 2018

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Given the lack of knowledge in the generation and biological activity of biopeptides (BP) produced by Bromelia pinguin and Bromelia karatas-derived proteases, the objective of this work was to evaluate the antioxidant capacity (AOX) of protein hydrolysates and peptide fractions from hydrolysis of egg, milk and soy proteins with enzymes extracted from Bromelia pinguin and Bromelia karatas fruits. The degree of hydrolysis (DH) of the mentioned proteins was measured. The hydrolysates were sequentially fractionated by ultrafiltration using different membrane pore sizes (≤30, ≤10, ≤5 and ≤1 kDa) to obtain biopeptide fractions (BPF). The antioxidant capacity (AOX) of protein hydrolysates and BPF were evaluated. AOX was performed using 2,2´-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS•+), ferric reducing antioxidant power (FRAP) and oxygen radical absorbance capacity (ORAC) assays. after the enzymatic action of B. pinguin and B. karatas proteases, the highest DH values for egg, milk and soy protein hydrolysates ranged from 50-61%, 55-68% and 73-81%, respectively. The AOX was higher for soy hydrolysates than for egg and milk hydrolysates. Additionally, the highest AOX from ABTS and FRAP assays was observed for BPF ≤30 kDa, PF ≤5 kDa and ≤1 kDa, respectively. These results highlight the potential of B. pinguin and B. karatas proteases to hydrolyze food proteins and release bioactive peptides. Moreover, it has been shown that the hydrolysis products are a mixture of BP of different molecular weights, which could present AOX through different mechanisms.

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Comparison of alcalase- and pepsin-treated oilseed protein hydrolysates – Experimental validation of predicted antioxidant, antihypertensive and antidiabetic properties

Han

Hernández-Álvarez

Maycock

et al. 2021

Current Research in Food Science

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There is emerging evidence on the importance of food-derived bioactive peptides to promote human health. Compared with animal derived proteins, plant proteins, in particular oilseed proteins, are considered as affordable and sustainable sources of bioactive peptides. Based on our previous bioinformatic analysis, five oilseed proteins (flaxseed, rapeseed, sunflower, sesame and soybean) were enzymatically hydrolysed using alcalase and pepsin (pH 1.3 and pH 2.1). Further, low molecular weight (M w < 3 kDa) fractions were generated using ultrafiltration. The protein hydrolysates and their low M w fractions were evaluated for their in vitro antioxidant, antihypertensive and antidiabetic capabilities, in comparison with samples obtained from two dairy proteins (whey and casein). Apart from dipeptidyl-peptidase IV inhibition, significantly stronger bioactivities were detected for the low M w fractions. In partial agreement with in silico predictions, most oilseed hydrolysates exerted comparable angiotensin-converting enzyme inhibitory capability to dairy proteins, whilst whey protein was the most promising source of dipeptidyl-peptidase IV inhibitors. Apart from alcalase-treated soybean, dairy proteins were more efficient in releasing antioxidant peptides as compared to oilseed proteins. On the other hand, soybean protein hydrolysates showed the highest α-glucosidase inhibitory activity amongst all protein sources. Overall, there was limited correlation between in silico predictions and in vitro experimental results. Nevertheless, our results indicate that oilseed proteins have potential as bioactive peptide sources, and they might therefore be suitable replacers for dairy proteins as well as good sources for development of functional foods.

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Effects of bioactive peptides encrypted in whey-, soy- and rice protein on local and systemic angiotensin-converting enzyme activity

Cited by 11 publications

References 31 publications

Biotechnological production of the angiotensin‐converting enzyme inhibitory dipeptide isoleucine‐tryptophan

Biotechnological production of the angiotensin‐converting enzyme inhibitory dipeptide isoleucine‐tryptophan

Antioxidant capacity of egg, milk and soy protein hydrolysates and biopeptides produced by Bromelia pinguin and Bromelia karatas-derived proteases

Comparison of alcalase- and pepsin-treated oilseed protein hydrolysates – Experimental validation of predicted antioxidant, antihypertensive and antidiabetic properties

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