Peptide identification in a porcine gelatin prolyl endoproteinase hydrolysate with angiotensin converting enzyme (ACE) inhibitory and hypotensive activity

O’Keeffe, Martina B.; Norris, Roseanne; Alashi, Monisola A.; Aluko, Rotimi E.; Fitzgerald, Richard J.

doi:10.1016/j.jff.2017.04.018

Cited by 65 publications

(40 citation statements)

References 39 publications

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“…Details of the surgical implantation of sensors have been previously described by O'Keeffe et al . (). The SHRs were allowed a 2‐week recovery from the surgery before proceeding to oral administration of test agents.…”

Section: Methodsmentioning

confidence: 99%

Antihypertensive properties of aqueous extracts of vegetable leaf‐fortified bread after oral administration to spontaneously hypertensive rats

Alashi

Taiwo

Oyedele

et al. 2018

Int J of Food Sci Tech

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Summary This study investigated the potential cardiovascular health benefits of leavened bread produced from wheat flour that contained 1%, 2% and 3% additions of leafy vegetable powders obtained from Amaranthus viridis (AO), Solanum macrocarpon (SM) or Telfairia occidentalis (TO). Dried breads were extracted with water at 60 °C followed by analysis for total polyphenolic content (TPC), as well as in vitro inhibitions of angiotensin‐converting enzyme and renin activities. HPLC analysis of the bread extracts indicated the presence of mainly rutin, gallic acid, myricetin and caffeic acid. TPC of the vegetable‐fortified breads was significantly (P < 0.05) higher (5.8–7.6 mg gallic acid equivalent, GAE/g) than that of control bread (5.5 mg GAE/g). Oral administration of 100 mg dried extract/kg body weight to spontaneously hypertensive rats led to reductions (up to 42 mmHg) in systolic, diastolic and mean arterial blood pressure in comparison with 20 mmHg for the control bread.

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Section: Methodsmentioning

confidence: 99%

Antihypertensive properties of aqueous extracts of vegetable leaf‐fortified bread after oral administration to spontaneously hypertensive rats

Alashi

Taiwo

Oyedele

et al. 2018

Int J of Food Sci Tech

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“…Since the important role ACE was found to play in the cause of hypertension, more attention has been focused on discovering ACE inhibitors, especially safer and milder food and/or food by‐product‐derived ACE inhibitory peptides. Some peptides have already been found in Pacific cod, bovine, milk, soybean, egg white, wine and porcine samples, for example. Some ACE inhibitory peptides from Salmo salar have also been reported .…”

Section: Introductionmentioning

confidence: 99%

Identification and molecular docking study of novel angiotensin‐converting enzyme inhibitory peptides from Salmo salar using in silico methods

Chen

Zhao

et al. 2018

J Sci Food Agric

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“…After centrifugation for 10 min at 4°C and 10,000 rpm, the supernatant fluid was subjected to evaporation and freeze drying. Finally, the ACE inhibitory peptides were obtained [18,19].…”

Section: Preparation Of Ace Inhibitory Peptides From Coasmmentioning

confidence: 99%

Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

Yao

et al. 2019

Journal of Food Quality

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China is a large country that produces Camellia oleifera Abel seed meal (COASM), a by-product of tea-seed oil, which is only used as an organic fertilizer, resulting in a serious waste of high-quality resources. The preparation of the ACE inhibitory peptide from COASM and the study of its functional properties are of practical importance in improving the comprehensive utilization of COASM. Our manuscript presents an optimized preparation of ACE inhibitory peptides with alkaline protease and enzyme kinetics parameters. Ultrafiltration, gel chromatography, and RP-HPLC purification were conducted for ACE inhibitory peptides, and peptide molecular weight distribution and amino acid composition were analyzed in the enzymolysis liquid. The following were the conditions of the optimized enzymatic hydrolysis to obtain ACE inhibitory peptides from COASM: 15 times of hydrolysis in distilled water for 3.5 h at 50°C, pH = 8.5, substrate concentration of 17 mg/g, and addition of 6% (w/w) alkaline protease. Under this condition, the peptides produced exhibited an ACE inhibition rate of 79.24%, and the reaction kinetics parameters are as follows: Km = 0.152 mg/mL and Vmax = 0.130 mg/mL·min. The majority of ACE inhibitory peptides from COASM have molecular weight below 1 kDa, and a high ACE inhibitory rate was achieved after dextran gel chromatography separation and purification (whose IC50 was 0.678 mg/mL). The hydrophobic amino acid content in this fraction reached 51.21%.

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Peptide identification in a porcine gelatin prolyl endoproteinase hydrolysate with angiotensin converting enzyme (ACE) inhibitory and hypotensive activity

Cited by 65 publications

References 39 publications

Antihypertensive properties of aqueous extracts of vegetable leaf‐fortified bread after oral administration to spontaneously hypertensive rats

Antihypertensive properties of aqueous extracts of vegetable leaf‐fortified bread after oral administration to spontaneously hypertensive rats

Identification and molecular docking study of novel angiotensin‐converting enzyme inhibitory peptides from Salmo salar using in silico methods

Purification of Angiotensin-I-Converting Enzyme Inhibitory Peptides Derived from Camellia oleifera Abel Seed Meal Hydrolysate

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