Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.

Cheung, H.S.; Wang, F L; Ondetti, Miguel A.; Sabo, Emily F.; Cushman, David

doi:10.1016/s0021-9258(19)86187-2

Cited by 686 publications

(161 citation statements)

References 38 publications

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“…This finding was probably because microbial metabolic interactions resulting in the C-terminal residue of peptides produced by co-cultures of 3 strains involved more proline. Proline as the C-terminal residue could be primarily responsible for the high activity (Cheung et al, 1980;Quirós et al, 2005). Interestingly, the ACE inhibition of the St-Lp fermented milk was lower than that of the St fermented milk after pepsin digestion, implying that some of the active sequences of peptides from St-Lp samples were totally hydrolyzed after digestion (Vercruysse et al, 2005).…”

Section: Ace-inhibitory Activitymentioning

confidence: 99%

In vitro antioxidant and angiotensin-converting enzyme inhibitory activity of fermented milk with different culture combinations

Tang

et al. 2020

Journal of Dairy Science

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This study investigated the effects of Lactobacillus plantarum (Lp) and Bifidobacterium animalis ssp. lactis (Ba) in co-cultures with Streptococcus thermophilus (St) on changes in the acidification profile, proteolytic activity, peptide production, in vitro antioxidant activity, and angiotensin-converting enzyme (ACE) inhibitory properties of fermented milks during 21 d of storage at 4°C. The pH values and proteolysis in all batches showed a gradual decrease and increase during storage, respectively. The ACE-inhibitory activity and total antioxidant capacity of all co-fermented milk samples followed a similar pattern, with maximum values on d 6 of storage. The St starter, in conjunction with Ba or Lp or both, enhanced proteolysis, peptide generation, and ACE-inhibitory and antioxidant activity, but decreased pH values compared with St alone. The St-Ba-Lp samples showed higher DPPH • (1,1-diphenyl-2-picrylhydrazyl) radical scavenging activity, hydroxyl radical scavenging activity, and total antioxidant capacity, but similar superoxide anion scavenging activity compared to St-Ba or St-Lp samples. The St-Ba samples showed higher DPPH • radical scavenging activity but lower hydroxyl radical scavenging activity than St-Lp samples. In the ACE-inhibitory assays, the St-Lp samples exhibited relatively low activity among the co-fermented milks, digested or not. The presence of Ba and Lp in fermentation together did not affect ACE-inhibitory activity in undigested fermented milks compared with the presence of Ba alone, and St-Ba-Lp fermented milks demonstrated an increase in ACEinhibitory activity after simulated gastrointestinal digestion in storage. Pepsin digestion largely improved ACE-inhibitory activity, except in St-Lp samples, in which the activity was reduced. Further hydrolysis by trypsin reduced final activity in digestion. This study suggests that co-cultured fermentation with probiotics improves in vitro antioxidant and ACE inhibition activity in fermented milks, and this effect is partly due to the higher proteolytic activity of probiotics.

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Section: Ace-inhibitory Activitymentioning

confidence: 99%

In vitro antioxidant and angiotensin-converting enzyme inhibitory activity of fermented milk with different culture combinations

Tang

et al. 2020

Journal of Dairy Science

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“…The search revealed that the same peptide sequence was found in squid small albumin (Iwaniak and Dziuba, 2011), pork sarcoplasmic protein (Castellano et al, 2013), raw chicken muscle protein (Iwaniak and Dziuba, 2009), grain storage protein (Cavazos and Mejia, 2013), and milk protein (Iwaniak and Dziuba, 2009). Cheung et al (1980) investigated the binding of peptide substrates and ACE inhibitors and found that the IC 50 of synthetic GA was 2 mM. In this study, the GA dipeptide was isolated and purified to determine its properties.…”

Section: Identification Of Acei Peptidesmentioning

confidence: 99%

Purification and characterization of angiotensin-I-converting enzyme inhibitory peptides isolated from whey proteins of milk fermented with Lactobacillus plantarum QS670

Xia

et al. 2020

Journal of Dairy Science

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An angiotensin-converting enzyme inhibitory (ACEI) peptide with a median inhibitory concentration (IC 50 ) of 1.26 mg/mL was purified from whey proteins resulting from a fermentation using Lactobacillus plantarum QS670. The peptide was subsequently derived from an α S1 -casein, κ-casein, β-lactoglobulin, or serum albumin fraction. Analysis via liquid chromatography tandem mass spectrometry indicated that it had an amino acid sequence of Gly-Ala (GA). The GA dipeptide was also synthesized using an Fmoc solid-phase method. The GA dipeptide exhibited an IC 50 of 1.22 mg/mL and was shown to be stable across both temperature (20 to 60°C) and pH (2 to 12). Digestive enzymes including pepsin, trypsin, and chymotrypsin had negligible effects on activity. The whey exerted hypotensive effects when fed to spontaneously hypertensive rats (SHR), which exhibited a blood pressure drop of 2.33 kPa. A 4-wk gavage treatment resulted in greater decreases of 7.46 kPa. Results of this study indicate that milk fermented using Lb. plantarum QS306 has potential to be used as a functional food to help prevent or reduce hypertension-associated diseases.

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“…Eventually, mixtures were centrifuged at 1750× g for 10 min, 1 mL of supernatant was transferred into a test tube, and ethyl acetate was eliminated by heat evaporation at 95 • C. The precipitate was re-dissolved in 2 mL of deionized water and measured spectrophotometrically at 228 nm, using a UV-1800 spectrophotometer (Shimadzu, Kyoto, Japan). For the analysis of samples fractionated by reversed-phase chromatography, the synthetic peptides were assayed using the modified method reported by Cheung, et al [26]. Briefly, 50 µL of sample solution, 100 µL of the ACE 0.01 U/mL, and 20 µL of 25 mM HHL were mixed in a 96-well plate and incubated at 37 • C for 40 min.…”

Section: Assay Of Ace Inhibitory Activity Of the Products Of In Vitro Meat Digestionmentioning

confidence: 99%

Isolation, Evaluation, and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Game Meat

Takeda

Kaneko

Sogawa

et al. 2020

Foods

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Game meat has been underutilized, while it offers the potential to diversify not only the human diet but also increase food production and the nutritional value of meat products. This study aimed to determine the angiotensin I-converting enzyme (ACE) inhibitory activities of the digested game meats (venison and boar meat) compared with those of livestock meats (beef and pork). Through the sodium dodecyl sulfate polyacrylamide gel electrophoresis and size chromatography results, we found that the digested products from each meat had different molecular weights. The ACE inhibitory ratio in all tested samples had gradually increased following by the enzyme treatments. ACE inhibitory ratios and the half maximal inhibitory concentration values indicated that digested venison was the most potent inhibitor of ACE activity, followed by the digested boar meat. The level of anserine in digested venison was higher than that in the other meats, but the carnosine level was lower. Through fractionations and liquid chromatography–tandem mass spectrometry analysis, five ACE inhibitory peptides were identified from the digested venison. Of these peptides, Isoleucine-Lysine- Glutamic Acid-Valine-Threonine-Glutamic Acid-Arginine (IKEVTER) demonstrated the highest ACE inhibitory activity. Therefore, the game meat is food that is believed potentially to offer high bioactivities, particularly antihypertensive forces.

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Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence.

Cited by 686 publications

References 38 publications

In vitro antioxidant and angiotensin-converting enzyme inhibitory activity of fermented milk with different culture combinations

In vitro antioxidant and angiotensin-converting enzyme inhibitory activity of fermented milk with different culture combinations

Purification and characterization of angiotensin-I-converting enzyme inhibitory peptides isolated from whey proteins of milk fermented with Lactobacillus plantarum QS670

Isolation, Evaluation, and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Game Meat

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