Structural and functional characterization of yellow field pea seed (Pisum sativum L.) protein-derived antihypertensive peptides. (November 2015)
- Record Type:
- Journal Article
- Title:
- Structural and functional characterization of yellow field pea seed (Pisum sativum L.) protein-derived antihypertensive peptides. (November 2015)
- Main Title:
- Structural and functional characterization of yellow field pea seed (Pisum sativum L.) protein-derived antihypertensive peptides
- Authors:
- Aluko, Rotimi E.
Girgih, Abraham T.
He, Rong
Malomo, Sunday
Li, Huan
Offengenden, Marina
Wu, Jianping - Abstract:
- Abstract: The aim of this study was to identify and test the in vivo effectiveness of antihypertensive peptides present in a pea protein hydrolysate. Yellow field pea protein isolate was digested with thermolysin and the hydrolysate passed through a 3 kDa ultrafiltration membrane. The permeate was collected as the PPH-3 and separated on a reverse-phase HPLC column into 10 peptide fractions. Fractions 3–8 showed inhibition of in vitro renin activity that ranged from approx. 21–68% while ACE activity was inhibited by fractions 2–10 in the range of 22–95%. Fraction 7 had the highest dual inhibitions of the two enzymes with 52.16 and 95.17% for renin and ACE, respectively. Fraction 7 was therefore, chosen for peptide characterization by tandem mass spectrometry, which led to sequencing of the following five peptides: LTFPG (534 Da); IIPLEN (698 Da); LSSGDVF (724 Da); IFENLQN (877 Da); and FEGTVFENG (999 Da). LTFPG, IFENLQN and FEGTVFENG had significantly (P < 0.05) higher inhibitions of ACE and renin activities and were orally administered to spontaneously hypertensive rats at a dose of 30 mg/kg body weight. LTFPG showed significantly (P < 0.05) the fastest decrease in systolic blood pressure (SBP) with a maximum of − 37 mmHg after 2 h. In contrast the maximum effects of IFENLQN (− 37 mmHg) and FEGTVFENG (− 25 mmHg) were observed after 4 h. Overall, the three peptides had significantly (P < 0.05) better SBP-reducing effects than the PPH-3, which gave a maximum of − 14 mmHg afterAbstract: The aim of this study was to identify and test the in vivo effectiveness of antihypertensive peptides present in a pea protein hydrolysate. Yellow field pea protein isolate was digested with thermolysin and the hydrolysate passed through a 3 kDa ultrafiltration membrane. The permeate was collected as the PPH-3 and separated on a reverse-phase HPLC column into 10 peptide fractions. Fractions 3–8 showed inhibition of in vitro renin activity that ranged from approx. 21–68% while ACE activity was inhibited by fractions 2–10 in the range of 22–95%. Fraction 7 had the highest dual inhibitions of the two enzymes with 52.16 and 95.17% for renin and ACE, respectively. Fraction 7 was therefore, chosen for peptide characterization by tandem mass spectrometry, which led to sequencing of the following five peptides: LTFPG (534 Da); IIPLEN (698 Da); LSSGDVF (724 Da); IFENLQN (877 Da); and FEGTVFENG (999 Da). LTFPG, IFENLQN and FEGTVFENG had significantly (P < 0.05) higher inhibitions of ACE and renin activities and were orally administered to spontaneously hypertensive rats at a dose of 30 mg/kg body weight. LTFPG showed significantly (P < 0.05) the fastest decrease in systolic blood pressure (SBP) with a maximum of − 37 mmHg after 2 h. In contrast the maximum effects of IFENLQN (− 37 mmHg) and FEGTVFENG (− 25 mmHg) were observed after 4 h. Overall, the three peptides had significantly (P < 0.05) better SBP-reducing effects than the PPH-3, which gave a maximum of − 14 mmHg after 6 h. Highlights: Five peptides were identified to be present in a pea protein hydrolysate. LTFPG and FEGTVFENG showed moderate renin inhibition. IIPLEN, LSSGDVF, and IFENLQN had nil to poor renin inhibition. IFENLQN and FEGTVFENG had strong ACE inhibition. LTFPG and FEGTVFENG had the highest blood pressure reducing effects. … (more)
- Is Part Of:
- Food research international. Volume 77:Part 1(2015:Nov.)
- Journal:
- Food research international
- Issue:
- Volume 77:Part 1(2015:Nov.)
- Issue Display:
- Volume 77, Part 1 (2015)
- Year:
- 2015
- Volume:
- 77
- Part:
- 1
- Issue Sort Value:
- 2015-0077-0000-0001
- Page Start:
- 10
- Page End:
- 16
- Publication Date:
- 2015-11
- Subjects:
- Pea seed -- Antihypertensive peptides -- Protein hydrolysate -- Angiotensin converting enzyme -- Renin -- Spontaneously hypertensive rats
Food -- Analysis -- Periodicals
Food industry and trade -- Periodicals
Food industry and trade -- Canada -- Periodicals
Food Technology -- Periodicals
Food -- Periodicals
Food-Processing Industry -- Periodicals
Aliments -- Industrie et commerce -- Périodiques
Aliments -- Industrie et commerce -- Canada -- Périodiques
Aliments -- Recherche -- Périodiques
Food industry and trade
Canada
Periodicals
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664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09639969 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodres.2015.03.029 ↗
- Languages:
- English
- ISSNs:
- 0963-9969
- Deposit Type:
- Legaldeposit
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