Identification of post-digestion angiotensin-I converting enzyme (ACE) inhibitory peptides from soybean protein Isolate: Their production conditions and in silico molecular docking with ACE

Xu, Zhifeng; Wu, Changping; Sun‐Waterhouse, Dongxiao; Zhao, Tiantian; Waterhouse, Geoffrey I.N.; Zhao, Ming; Su, Guowan

doi:10.1016/j.foodchem.2020.128855

Cited by 93 publications

(72 citation statements)

References 38 publications

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“…Because the subfraction C4 exhibited the highest ACE-inhibitory activity (59.76% ± 3.70% at 1.0 mg/mL) among these subfractions (C1–C5), it was selected and used for the peptide sequence analysis. In addition, previous studies have also demonstrated that Sephadex G-15 gel chromatography combined with RP-HPLC was an effective way for separation and purification of ACE-inhibitory peptides from protein hydrolysates [ 5 , 16 ].…”

Section: Resultsmentioning

confidence: 99%

“…The result means that APKIEEV can inhibit ACE activity through hindering the touch between ACE and its substrates, such as angiotensin-1 and bradykinin, but cannot bind to active sites of ACE [ 20 ]. Xu et al [ 16 ] and Ling et al [ 20 ] also identified uncompetitive inhibitors of ACE from soybean protein hydrolysates and tilapia skin gelatin hydrolysates, respectively. In addition, it has been found that competitive peptides always show a higher ACE-inhibitory activity than that of uncompetitive peptides [ 1 , 5 ].…”

Section: Resultsmentioning

confidence: 99%

“…This is also the main reason why APKIEEV has relatively high ACE-inhibitory activity (550.41 μmol/L, Figure 4 A). It has been demonstrated that uncompetitive inhibitors usually showed lower ACE-inhibitory activity than that of competitive inhibitors [ 16 ]. Therefore, APKIEEV (an uncompetitive inhibitor) showed a lower ACE inhibition activity than that of peptide NMAINPSKENLCSTFCK (a competitive inhibitor of ACE) [ 18 ].…”

Section: Resultsmentioning

confidence: 99%

“…Plant seed protein can be classified into five fractions: albumin, globulin, prolamine, glutelin-1 and glutelin-2 based on solubility. The globulin is a kind of protein fraction soluble in dilute salt solution and exists widely in cereal and oil crops such as soybean, coconut and oil palm [ 5 , 16 ]. The result of the pre-experiment of this study reveals that globulin is the major fraction of areca nut kernel, according for 49.37 g/100 g areca nut kernel protein.…”

Section: Introductionmentioning

confidence: 99%

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Identification, Characterization and Antihypertensive Effect In Vivo of a Novel ACE-Inhibitory Heptapeptide from Defatted Areca Nut Kernel Globulin Hydrolysates

Liu

Wang

et al. 2021

Molecules

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The areca (Areca catechu L.) nut kernel (ANK) is a good potential protein source for its high protein content of 9.89–14.62 g/100 g and a high yield of around 300,000 tons per year in China. However, utilization of the areca nut kernel is limited. To expand the usage of ANK in pharmaceutical or foods industries, areca nut kernel globulin was extracted and angiotensin-I converting enzyme (ACE) inhibition peptides were prepared and identified using gel chromatography, reversed phase HPLC separation, UPLC-ESI-MS/MS analysis and in silico screening. Finally, a novel ACE-inhibitory heptapeptide (Ala–Pro–Lys–Ile–Glu–Glu–Val) was identified and chemically synthesized. The combination pattern between APKIEEV and ACE, and the inhibition kinetics, antihypertensive effect and endothlein-1 inhibition activity of APKIEEV were studied. The results of the molecular docking demonstrated that APKIEEV could bind to four active sites (not the key active sites) of ACE via short hydrogen bonds and demonstrated high ACE-inhibitory activity (IC50: 550.41 μmol/L). Moreover, APKIEEV exhibited a significantly lowering effect on both the systolic blood pressure and diastolic blood pressure of spontaneously hypertensive rats, and had considerable suppression ability on intracellular endothelin-1. These results highlight the potential usage of APKIEEV as ingredients of antihypertensive drugs or functional foods.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Identification, Characterization and Antihypertensive Effect In Vivo of a Novel ACE-Inhibitory Heptapeptide from Defatted Areca Nut Kernel Globulin Hydrolysates

Liu

Wang

et al. 2021

Molecules

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“…Since the last century, soybean cultivation has become widespread in western countries, too [ 4 ]. Soy proteins contain all the essential amino acids, and therefore they represent a valid alternative to food of animal origin; furthermore, several biological functions and bioactivities have been attributed to their derived peptides [ 13 ], such as cancer and cardiovascular disease prevention, antihypertensive activity [ 14 ], hypocholesterolemic effect, and antioxidant properties [ 1 , 4 , 7 , 15 , 16 ]. In particular, the antioxidant activity, i.e., the defense against the free radical damage [ 17 ], could be useful in contrasting several pathologies, as well as in nutraceutical and cosmetics applications.…”

Section: Introductionmentioning

confidence: 99%

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

et al. 2021

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Soybeans (Glycine max) are an excellent source of dietary proteins and peptides with potential biological activities, such as antihypertensive, anti-cholesterol, and antioxidant activity; moreover, they could prevent cancer. Also, soy contains all the essential amino acids for nutrition; therefore, it represents an alternative to animal proteins. The goal of this paper was the comprehensive characterization of medium-sized and short peptides (two to four amino acids) obtained from simulated gastrointestinal digestion. Two different analytical approaches were employed for peptide characterization, namely a common peptidomic analysis for medium-sized peptides and a suspect screening analysis for short peptides, employing an inclusion list of exact m/z values of all possible amino acid combinations. Moreover, fractionation by preparative reversed-phase liquid chromatography was employed to simplify the starting protein hydrolysate. Six fractions were collected and tested for antioxidative activity by an innovative antioxidant assay on human gastric adenocarcinoma AGS cell lines. The two most active fractions (2 and 3) were then characterized by a peptidomic approach and database search, as well as by a suspect screening approach, in order to identify potential antioxidant amino acid sequences. Some of the peptides identified in these two fractions have been already reported in the literature for their antioxidant activity.

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Preparation of antihypertensive peptides from quinoa via fermentation with Lactobacillus paracasei

Shi

et al. 2022

eFood

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Quinoa is a pseudo‐cereal that is rich in protein and an ideal source of antihypertensive peptides. In this study, quinoa flour was fermented with Lactobacillus paracasei CICC 20241 via solid fermentation to produce antihypertensive peptides. The peptides were isolated and purified by ultrafiltration and gel chromatography, and then identified by liquid chromatography−tandem mass spectrometry. A total of 91 peptides were identified. In addition, five potential angiotensin‐converting enzyme (ACE) inhibitory peptides were synthesized with reference to in silico analysis. Among them, NIFRPFAPEL and AALEAPRILNL had the greatest inhibitory effect, with an IC50 of 49.02 and 79.72 µM, respectively. Inhibition dynamics and molecular docking indicated that NIFRPFAPEL formed eight hydrogen bonds with ACE residues Tyr523, Arg522, Glu384, Glu143, Glu123, Thr92, Tyr62, and Trp59. NIFRPFAPEL exerted a competitive inhibitory effect by interacting with residues Tyr523 and Glu384 of pocket S1. AALEAPRILNL exerted a noncompetitive inhibitory effect by forming eight hydrogen bonds with the inactive ACE site residues Ser516, Glu403, Ser355, Glu143, ARG124, and Asn70. These results confirmed that quinoa is a potential material for antihypertensive functional foods, while NIFRPFAPEL and AALEAPRILNL could be used for the development of antihypertensive functional foods or drugs.

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Identification of post-digestion angiotensin-I converting enzyme (ACE) inhibitory peptides from soybean protein Isolate: Their production conditions and in silico molecular docking with ACE

Cited by 93 publications

References 38 publications

Identification, Characterization and Antihypertensive Effect In Vivo of a Novel ACE-Inhibitory Heptapeptide from Defatted Areca Nut Kernel Globulin Hydrolysates

Identification, Characterization and Antihypertensive Effect In Vivo of a Novel ACE-Inhibitory Heptapeptide from Defatted Areca Nut Kernel Globulin Hydrolysates

Production and Characterization of Medium-Sized and Short Antioxidant Peptides from Soy Flour-Simulated Gastrointestinal Hydrolysate

Preparation of antihypertensive peptides from quinoa via fermentation with Lactobacillus paracasei

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