Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins

Rudolph, Steffi; Lunow, Diana; Kaiser, Susanne; Henle, Thomas

doi:10.1016/j.foodchem.2016.12.039

Cited by 57 publications

(41 citation statements)

References 32 publications

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“…In recent years, it has been demonstrated that ACE appears to prefer substrates or competitive inhibitors that contain hydrophobic amino acid residues, particularly Val, Leu, and/or aromatic residues (Trp, Tyr, or Phe) in the C-terminal tripeptide [25,29]. Moreover, accumulating studies suggest that the positive charge of Arg (guanidine group) at N-terminus contributes substantially to the inhibitory activity against ACE [32,33]. Regarding the antioxidant activity of peptides, it was more related to size, amino acid constituents and sequence, structure, and hydrophobicity [27].…”

Section: Characterization Of Pooled Peptide Fraction By Mass Spectrommentioning

confidence: 99%

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

et al. 2019

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Albumin is the major fraction of quinoa protein that is characterized as having high nutritional value. However, until now, scant information is available on the bioactivity of quinoa albumin or its hydrolysates. To promote its usage, we extracted albumin in this study from quinoa bran assisted with cellulase and hemicellulose, and hydrolyzed it by alcalase and trypsin to produce bioactive peptides. The hydrolysates (QBAH) were purified by gel filtration and reversed-phase high-performance liquid chromatography (RP-HPLC), followed by identification using liquid chromatography-mass spectrometry (LC-MS/MS). Furthermore, based on in silico analysis, one angiotensin-I converting enzyme (ACE)-inhibitory and antioxidant peptide, RGQVIYVL (946.6 Da), and two antioxidant peptides, ASPKPSSA (743.8 Da), and QFLLAGR (803.5 Da), from QBAH were synthesized. RGQVIYVL showed a high ACE-inhibitory activity (IC 50 = 38.16 µM) with competitive mode of inhibition, and showed significant antihypertensive effect in spontaneously hypertensive rats at a concentration of 100-150 mg/kg body weight (bw). Molecular docking simulation showed that it could interact with the active ACE site via hydrogen bonds with high binding power. Moreover, RGQVIYVL, ASPKPSSA, and QFLLAGR all demonstrated high ·OH scavenging activity (IC 50 = 61.69-117.46 µM), ABTS + scavenging activity (58.29-74.28%) and Fe 2+ chelating ability (32.54-82.48% at 0.5 mg/mL). They could also retain activity after gastrointestinal enzyme digestion. These results indicate that quinoa albumin is a potential source of bioactive peptides possessing antioxidant and ACE-inhibitory activities.

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Section: Characterization Of Pooled Peptide Fraction By Mass Spectrommentioning

confidence: 99%

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

et al. 2019

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“…Now, it has been demonstrated that hydrogen bonds formed between the ACE active sites (S1, S1’, and S2) and peptides’ C ‐terminal tripeptide are crucial to ACE inhibition (Rudolph et al., 2017). Previous studies found that peptides with hydrophobic amino acid residues especially aromatic residues, Pro and/or Lys in C ‐terminal tripeptide were more easily bind to the active sites of ACE (Abdelhedi et al., 2018; Lee & Hur, 2019).…”

Section: Resultsmentioning

confidence: 99%

“…Over the recent years, increasing studies have investigated the isolation, identification, characterization, and in vivo antihypertension and of ACE‐inhibitory peptides derived from various food resources. However, studies focused on structural bioinformatics, bioavailability, and action mechanism of ACE‐inhibitory peptides are limited (Abdelhedi et al., 2018; Ambigaipalan & Shahidi, 2017; Li, Zhao, & Liu, 2017; Rudolph, Lunow, Kaiser, & Henle, 2017).…”

Section: Introductionmentioning

confidence: 99%

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Zheng

Wang

Zhuang

et al. 2020

Journal of Food Science

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Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed-phase high performance liquid chromatography (RP-HPLC). Finally, fraction D7d with the highest ACE-inhibitory was subjected to liquid chromatography-mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE-inhibitory activity (IC 50 : 91.82 µM) with competitive inhibition mode, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE-inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin-1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products.Practical Application: One novel ACE-inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin-1 suppressing capacity, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.Additional supporting information may be found online in the Supporting Information section at the end of the article. Supplementary Table S1. Body weight (g) of the spontaneous hypertensive rats administrated with peptide SSYYPFK a Supplementary Table S2. Heart rate of the spontaneous hypertensive rats administrated with peptide SSYYPFK a

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“…Tyrosine was proposed as the main contributing factor of inhibitory properties since the IC50 values increased as the tyrosine increased. Wheat showed the highest inhibitory activity, with an IC50 of 39 mg/L, followed closely by soy, pea and rice protein hydrolysates 95 . Legumes, such as chickpeas, lentils, lupins, and beans are another source of highly potent ACE-inhibitory protein hydrolysates, however, the extraction and hydrolysis methods may have an effect on the overall inhibitory activities 96 .…”

Section: Biological Activities Of Protein Hydrolysatesmentioning

confidence: 96%

“…Most commonly studied sources for ACE inhibitory hydrolysates are milk and fish 61 . In a recent study by Rudolph et al, it was discovered that enzymatically hydrolyzed proteins from wheat, pea, soy, and rice produced hydrolysates with ACE-inhibitory properties 95 . It was hypothesized that the presence of aromatic amino acids was the contributing factor to the inhibitory properties.…”

Section: Biological Activities Of Protein Hydrolysatesmentioning

confidence: 99%

Effects of Ultrasonication on the Antioxidant and Anti-diabetic Properties of Hydrolyzed Oat Proteins

Walters¹

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The method of protein extraction from foods can affect yields, compositions, and functionalities of the isolated proteins. The first objective of this work was to determine the effects of ultrasonic treatments on protein yields and polypeptide compositions. Proteins were consequently extracted from oat brans under normal (CTL) conditions and after pre-treatments of brans with ultrasonic bath (UB), and high power (HP) sonication. There was no significant difference in extraction yields (2.06 -3.79%), meanwhile gel electrophoresis and tandem mass spectrometry (LC-MS/MS) analysis showed differences in polypeptide compositions. Specifically, globulin and avenin proteins were present in all samples, however, ultrasonic treatments (UB and HP) released vromindoline, a starch-bound protein, while tryptophanin, a lipid-bound protein, was released after high power ultrasonic (HP) treatment. The second objective of this work was to determine the physical, chemical, and biological properties of the proteins after hydrolysis with proteases of various specificities. Proteins from CTL, UB, HP samples were hydrolyzed by three proteases (Flavourzyme, Papain, and Alcalase) and then characterized based on their sulfhydryl (SH) content, hydrophobicity and zeta potential. Data showed that HP ultrasonic treatments decreased SH concentrations in Papain and Alcalase hydrolysates but increased it in the Flavourzyme hydrolysate. The surface charge (i.e. zeta potential) was dependent on both the protein extraction and the protease. Papain had a much weaker surface charge (-0.78 to -1.32 mV) than the other proteases (-3.67 to -9.17 mV). UB treatments increased hydrophobicity for Flavourzyme and Papain hydrolysates, while HP treatments decreased the hydrophobicity. To further evaluate the hydrolyzed proteins (i.e. hydrolysates), their biological activities were determined. It was found that in general, ultrasonic treatments reduced the antioxidant activity of the protein hydrolysates. For example, peroxyl radical scavenging activity was reduced by UB and HP sonication; however, HO• scavenging activity was reduced by HP and not UB sonication. In the antidiabetic tests, hydrolysates were evaluated for their ability to modulate the activity of dipeptidyl peptidase-4 (DPP-4) and alpha-amylase, as well as the secretion of GLP-1, a hormone that stimulates insulin response in NCI-H716 cells. Ultrasonication did not affect DPP-4 inhibition; however, concerning proteases, Papain hydrolysates had substantially greater (49.7 -53.6%) DPP-4 inhibitory activity for all conditions. HP sonication slightly decreased the alpha-amylase inhibitory activity by 4.8 -7.2% compared to UB and control. A two-fold increase in hydrolysate concentration resulted in a 13.7 -76% increase in GLP-1 secretion, indicating a dose-dependent

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Identification and quantification of ACE-inhibiting peptides in enzymatic hydrolysates of plant proteins

Cited by 57 publications

References 32 publications

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

Isolation of Novel ACE-Inhibitory and Antioxidant Peptides from Quinoa Bran Albumin Assisted with an In Silico Approach: Characterization, In Vivo Antihypertension, and Molecular Docking

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Effects of Ultrasonication on the Antioxidant and Anti-diabetic Properties of Hydrolyzed Oat Proteins

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