scholarly journals ACE Inhibitory Activity and Molecular Docking of Gac Seed Protein Hydrolysate Purified by HILIC and RP-HPLC

Molecules ◽  
2020 ◽  
Vol 25 (20) ◽  
pp. 4635
Author(s):  
Samuchaya Ngamsuk ◽  
Tzou-Chi Huang ◽  
Jue-Liang Hsu
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Seed Proteins ◽  
Inhibition Mechanism ◽  
Ace Inhibitory Activity ◽  
Rp Hplc ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Gac (Momordica cochinchinensis Spreng.) seed proteins (GSPs) hydrolysate was investigated for angiotensin I-converting enzyme (ACE) inhibitory activities. GSPs were hydrolyzed under simulated gastrointestinal digestion using a combination of enzymes, including pepsin, trypsin, and chymotrypsin. The screening of ACE inhibitory peptides from GSPs hydrolysate was performed using two sequential bioassay-guided fractionations, namely hydrophilic interaction liquid chromatography (HILIC) and reversed-phase high-performance liquid chromatography (RP-HPLC). Then, the peptides in the fraction with the highest ACE inhibitory activity were identified by LC-MS/MS. The flow-through (FT) fraction showed the most potent ACE inhibitory activity when HILIC fractionation was performed. This fraction was further separated using RP-HPLC, and the result indicated that fraction 8 (RP-F8) showed the highest ACE inhibitory activity. In the HILIC-FT/RP-F8 fraction, 14 peptides were identified using LC-MS/MS analysis coupled with de novo sequencing. These amino acid chains had not been recorded previously and their ACE inhibitory activities were analyzed in silico using the BIOPEP database. One fragment with the amino acid sequence of ALVY showed a significant ACE inhibitory activity (7.03 ± 0.09 µM). The Lineweaver-Burk plot indicated that ALVY is a competitive inhibitor. The inhibition mechanism of ALVY against ACE was further rationalized through the molecular docking simulation, which revealed that the ACE inhibitory activities of ALVY is due to interaction with the S1 (Ala354, Tyr523) and the S2 (His353, His513) pockets of ACE. Bibliographic survey allowed the identification of similarities between peptides reported as in gac fruit and other proteins. These results suggest that gac seed proteins hydrolysate can be used as a potential nutraceutical with inhibitory activity against ACE.

scholarly journals Identification and Molecular Docking Study of a Novel Angiotensin-I Converting Enzyme Inhibitory Peptide Derived from Enzymatic Hydrolysates of Cyclina sinensis

Marine Drugs ◽  
2018 ◽  
Vol 16 (11) ◽  
pp. 411 ◽  
Author(s):  
Fangmiao Yu ◽  
Zhuangwei Zhang ◽  
Liwang Luo ◽  
Junxiang Zhu ◽  
Fangfang Huang ◽  
...  
Keyword(s):  
Liquid Chromatography ◽  
Molecular Docking ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Cyclina Sinensis ◽  
Ace Inhibitory

Marine-derived angiotensin-I converting enzyme (ACE) inhibitory peptides have shown potent ACE inhibitory activity with no side effects. In this study, we reported the discovery of a novel ACE-inhibitory peptide derived from trypsin hydrolysates of Cyclina sinensis (CSH). CSH was separated into four different molecular weight (MW) fractions by ultrafiltration. Fraction CSH-I showed the strongest ACE inhibitory activity. A peptide was purified by fast protein liquid chromatography (FPLC) and reversed-phase high-performance liquid chromatography (RP-HPLC) and its sequence was determined to be Trp-Pro-Met-Gly-Phe (WPMGF, 636.75 Da). The Lineweaver-Burk plot showed that WPMGF was a competitive inhibitor of ACE. WPMGF showed a significant degree of stability at varying temperatures, pH, and simulated gastrointestinal environment conditions. We investigated the interaction between this pentapeptide and ACE by means of a flexible molecular docking tool. The results revealed that effective interaction between WPMGF and ACE occurred mainly through hydrogen bonding, hydrophobic interactions, and coordination bonds between WPMGF and Zn(II). In conclusion, our study indicates that a purified extract derived from Cyclina sinensis or the WPMGF peptide could potentially be incorporated in antihypertensive functional foods or dietary supplements.

scholarly journals Whey-Derived Peptides Interactions with ACE by Molecular Docking as a Potential Predictive Tool of Natural ACE Inhibitors

2020 ◽  
Vol 21 (3) ◽  
pp. 864 ◽  
Author(s):  
Yara Chamata ◽  
Kimberly A. Watson ◽  
Paula Jauregi
Keyword(s):  
Molecular Docking ◽  
Amino Acid ◽  
Ace Inhibitors ◽  
Inhibitory Activity ◽  
Antihypertensive Activity ◽  
Ace Inhibitory Activity ◽  
Predictive Tool ◽  
Ace Inhibitory

Several milk/whey derived peptides possess high in vitro angiotensin I-converting enzyme (ACE) inhibitory activity. However, in some cases, poor correlation between the in vitro ACE inhibitory activity and the in vivo antihypertensive activity has been observed. The aim of this study is to gain insight into the structure-activity relationship of peptide sequences present in whey/milk protein hydrolysates with high ACE inhibitory activity, which could lead to a better understanding and prediction of their in vivo antihypertensive activity. The potential interactions between peptides produced from whey proteins, previously reported as high ACE inhibitors such as IPP, LIVTQ, IIAE, LVYPFP, and human ACE were assessed using a molecular docking approach. The results show that peptides IIAE, LIVTQ, and LVYPFP formed strong H bonds with the amino acids Gln 259, His 331, and Thr 358 in the active site of the human ACE. Interestingly, the same residues were found to form strong hydrogen bonds with the ACE inhibitory drug Sampatrilat. Furthermore, peptides IIAE and LVYPFP interacted with the amino acid residues Gln 259 and His 331, respectively, also in common with other ACE-inhibitory drugs such as Captopril, Lisinopril and Elanapril. Additionally, IIAE interacted with the amino acid residue Asp 140 in common with Lisinopril, and LIVTQ interacted with Ala 332 in common with both Lisinopril and Elanapril. The peptides produced naturally from whey by enzymatic hydrolysis interacted with residues of the human ACE in common with potent ACE-inhibitory drugs which suggests that these natural peptides may be potent ACE inhibitors.

scholarly journals Antioxidant and angiotensin I-converting enzyme inhibitory activities of Xuanwei ham before and after cooking and in vitro simulated gastrointestinal digestion

2018 ◽  
Vol 5 (7) ◽  
pp. 180276 ◽  
Author(s):  
Le Wang ◽  
Xiang Li ◽  
Yingnan Li ◽  
Wenying Liu ◽  
Xiaoyun Jia ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Scavenging Activity ◽  
Angiotensin I ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Before And After ◽  
Inhibitory Activities ◽  
Ace Inhibitory ◽  
Significant Increment

Xuanwei ham is especially rich in a large amount of peptides and free amino acids under the action of protein degradation. Some of these peptides can potentially exert bioactivities of interest for human health. Traditionally, Xuanwei ham should undergo Chinese household cooking treatments before eating. However, it has not been known how its bioactivity changes after cooking and gastrointestinal digestion. Herein, Xuanwei ham is analysed before and after cooking, as well as gastrointestinal digestion being simulated so as to evaluate and compare its effect on antioxidant and angiotensin I-converting enzyme (ACE) inhibitory activities. The antioxidant activity is analysed using five different methods, and results demonstrate that cooking has some negative effects on antioxidative capacity when determined using different antioxidant methods except for a significant increment in 1,1'-diphenyl-2-picrylhydrazyl radical-scavenging activity, while ACE inhibitory activity increases significantly after cooking compared with control samples. After gastrointestinal digestion of samples, there is a significant increment of the antioxidant and ACE inhibitory activities in comparison with control and cooked samples. Particularly, after gastrointestinal digestion, free thiols content and 2,2'-azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) radical-cation-scavenging activity of Xuanwei ham, respectively, increase about twice and fourfold, while ACE inhibitory activity increases about twice compared to cooked samples, reaching the value of 83.73%. Therefore, through cooking the antioxidant activity and ACE inhibitory activity of Xuanwei ham are not completely lost and a part of them is still maintained, while gastrointestinal digestion produces a significant enhancement in both bioactivities, highlighting a greater potential for a beneficial physiological effect on human health after eating it.

scholarly journals Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 879
Author(s):  
Ramya Jayaprakash ◽  
Conrad O. Perera
Keyword(s):  
New Zealand ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Partial Purification ◽  
Ace Inhibitory Activity ◽  
Perna Canaliculus ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications.

Angiotensin I Converting Enzyme–Inhibitory Activity of Bovine, Ovine, and Caprine κ-Casein Macropeptides and Their Tryptic Hydrolysates

2003 ◽  
Vol 66 (9) ◽  
pp. 1686-1692 ◽  
Author(s):  
M. A. MANSO ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Tryptic Hydrolysate ◽  
Inhibitory Activities ◽  
Ace Inhibitory

This work evaluated the angiotensin-converting enzyme (ACE)–inhibitory activities of bovine, ovine, and caprine κ-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.

Angiotensin I–Converting Enzyme Inhibitory Activity of Peptides Derived from Egg White Proteins by Enzymatic Hydrolysis

2004 ◽  
Vol 67 (9) ◽  
pp. 1914-1920 ◽  
Author(s):  
M. MIGUEL ◽  
I. RECIO ◽  
J. A. GÓMEZ-RUIZ ◽  
M. RAMOS ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
High Performance Liquid Chromatography ◽  
Liquid Chromatography ◽  
Molecular Mass ◽  
Inhibitory Activity ◽  
High Performance ◽  
Egg White ◽  
Reversed Phase ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

The hydrolysis of crude egg white with pepsin, trypsin, and chymotrypsin produced peptides with angiotensin-converting enzyme (ACE) inhibitory properties. These peptides were mainly derived from the proteolysis of ovalbumin. The most active hydrolysates were obtained after treatment with pepsin (50% inhibitory concentration [IC50], 55.3 μg/ml), with the fraction having a molecular mass lower than 3,000 Da giving the highest ACE inhibitory activity (IC50, 34.5 μg/ml). Nine subfractions were collected from the fraction with a molecular mass lower than 3,000 Da using semipreparative reversed-phase high-performance liquid chromatography. Considerable ACE inhibitory activity (IC50 < 40 μg/ml) was found in three of them. These subfractions were analyzed by reversed-phase high-performance liquid chromatography–tandem mass spectrometry, and 14 peptides were identified. These sequences were synthesized, and their ACE inhibitory activities were measured. Among the identified peptides, two novel sequences with potent ACE inhibitory activity were found. The amino acid sequences of these inhibitors were identified as Arg-Ala-Asp-His-Pro-Phe-Leu and Tyr-Ala-Glu-Glu-Arg-Tyr-Pro-Ile-Leu and showed IC50 values of 6.2 and 4.7 μM, respectively.

THE PHYSICOCHEMICAL CHARACTERISTICS AND ANGIOTENSIN CONVERTING ENZYME (ACE) INHIBITORY ACTIVITY OF SKIPJACK TUNA (Katsuwonus pelamis) “BAKASANG”

2016 ◽  
Vol 78 (4-2) ◽  
Author(s):  
Max Robinson Wenno ◽  
Eddy Suprayitno ◽  
Aulanni’am Aulanni’am ◽  
Hardoko Hardoko
Keyword(s):  
Amino Acid ◽  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Enzyme Inhibitor ◽  
Physicochemical Characteristics ◽  
Chemical Characteristics ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Physical And Chemical ◽  
Ace Inhibitory

Bakasang is a traditional fermented fish product which is often used as condiments. This study aimed to determine the physical and chemical characteristics and potential ACE (Angiotensin Converting Enzyme) inhibitor of bakasang. Color and viscosity were physical characteristics measured in which color was presented in value of L* (36.05), a* (18.76), b* (15.65), while viscosity value was 6 950 cP. The result of chemical characteristics including salinity, acidity, pH, TVB-N and LAB were 72 %, 2.56 %, 4.66, 36.88 mg N per 100 g and 3.32 log CFU g–1 respectively. Proximate and amino acid compositions analysis were also identified, resulting in 14.77 % protein, 1.11 % fat, 57.15 % moisture, 25.97 % ash and 1.00 % carbohydrate while the predominant amino acid found was histidine. The ACE inhibitory activity of the isolated bioactive peptides of bakasang was 68.80 %.

scholarly journals Impact of Power Ultrasound on Antihypertensive Activity, Functional Properties, and Thermal Stability of Rapeseed Protein Hydrolysates

2017 ◽  
Vol 2017 ◽  
pp. 1-11 ◽  
Author(s):  
Asif Wali ◽  
Haile Ma ◽  
Muhammad Shahnawaz ◽  
Khizar Hayat ◽  
Jian Xiaong ◽  
...  
Keyword(s):  
Thermal Stability ◽  
Inhibitory Activity ◽  
Surface Hydrophobicity ◽  
Protein Hydrolysates ◽  
Ace Inhibitory Activity ◽  
Power Ultrasound ◽  
Inhibitory Activities ◽  
Rapeseed Protein Hydrolysates ◽  
Thermal Stability Of ◽  
Ace Inhibitory

The effects of power ultrasound pretreatments on the degree of hydrolysis (DH), angiotensin-I-converting enzyme (ACE) inhibitory activity, amino acid composition, surface hydrophobicity, protein solubility, and thermal stability of ACE inhibition of rapeseed protein hydrolysates were evaluated. Ultrasonic pretreatments before enzymolysis in terms of power and exposure time increased the DH and ACE inhibitory activities over the control (without sonication). In this study, maximum DH 22.07% and ACE inhibitory activity 72.13% were achieved at 600 W and 12 min pretreatment. Compared to the hydrolysates obtained without sonication, the amino acid profile of ultrasound pretreated hydrolysates showed significant changes particularly in the proline content and hydrophobic amino acids with an increased rate of 2.47% and 6.31%, respectively. Ultrasound pretreatment (600 watts, 12 min) improved functional properties of protein hydrolysates over control by enhancing surface hydrophobicity and solubility index with an increased rate of 130.76% and 34.22%. Moreover, the stability test showed that the ACE inhibitory activity remains stable against heat treatments. However, extensive heat, prolonged heating time, and alkaline conditions were not in the favor of stability test, while under mild heat and acidic conditions their ACE inhibitory activities were not significantly different from unheated samples.

scholarly journals Chemical Characteristics and Activity of ACE Inhibitors on Fractionation of Tempeh Koro kratok (Phaseolus lunatus) Peptides

2020 ◽  
Vol 16 (2) ◽  
pp. 42
Author(s):  
Marta Tika Handayani ◽  
Retno Indrati ◽  
Muhammad Nur Cahyanto
Keyword(s):  
Molecular Weight ◽  
Amino Acid ◽  
Inhibitory Activity ◽  
Chemical Properties ◽  
Ace Inhibition ◽  
Fermented Food ◽  
Phaseolus Lunatus ◽  
Ace Inhibitory Activity ◽  
Hydrophobic Amino Acid ◽  
Ace Inhibitory

Tempeh is a fermented food that is good for health and has high nutritional value. Koro kratok tempeh is one of tempeh which is made from non-soybean legumes. The fermentation process will convert macromolecular compounds to micromolecules thereby increasing bioavailability and providing functional properties. This study aimed to find out the chemical properties of koro kratok tempeh and the effect of peptide molecular weight of koro kratok tempeh on ACE inhibition activity. The results show that koro kratok seeds contained 20.66% protein which total hydrophobic amino acid was 3.32% (w/w protein). This hydrophobic amino acid was higher than that soybean, indicated that koro kratok (Phaseolus lunatus) has a potential producing ACE peptide inhibitors. The koro kratok seeds had ACE inhibitory activity  19.72%. This activity increased to 84.97% when the seeds were fermented for 48h to become tempeh. Peptide fractionation showed that the smaller the molecular weight of the peptide, the higher the ACE inhibitory activity.

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