Identification of bioactive peptides from a papain hydrolysate of bovine serum albumin and assessment of an antihypertensive effect in spontaneously hypertensive rats. (March 2016)
- Record Type:
- Journal Article
- Title:
- Identification of bioactive peptides from a papain hydrolysate of bovine serum albumin and assessment of an antihypertensive effect in spontaneously hypertensive rats. (March 2016)
- Main Title:
- Identification of bioactive peptides from a papain hydrolysate of bovine serum albumin and assessment of an antihypertensive effect in spontaneously hypertensive rats
- Authors:
- Lafarga, Tomas
Aluko, Rotimi E.
Rai, Dilip K.
O'Connor, Paula
Hayes, Maria - Abstract:
- Abstract: Inhibition of angiotensin-I-converting enzyme (ACE-I), renin, and dipeptidyl peptidase-IV (DPP-IV) plays a key role in the treatment of hypertension and type-2 diabetes. The aim of this study was to isolate and characterize novel ACE-I, renin, and DPP-IV inhibitory peptides from a papain hydrolysate of bovine serum albumin (BSA). BSA was obtained from whole bovine blood and hydrolyzed with the food-grade enzyme papain. The generated hydrolysate was further purified using ultrafiltration and high performance liquid chromatography (HPLC), and a number of novel bioactive peptides were identified using de novo peptide sequencing. These included SLR, YY, ER, and FR which inhibited the activity of the enzyme ACE-I by half at a concentration of 0.17 ± 0.02, 0.18 ± 0.04, 0.27 ± 0.01, and 0.42 ± 0.02 mM, respectively. In addition, the 1 kDa fraction of the papain hydrolysate was assessed for antihypertensive activity in vivo using spontaneously hypertensive rats (SHRs) and reduced systolic blood pressure over a 24 h period when compared with the control (p < 0.001). Results demonstrated the potential of bovine serum albumin as a source of bioactive peptides with health-promoting properties and potential for use as functional food ingredients. Highlights: Utilization of bovine blood proteins for the generation of biologically active peptides In silico analysis used for selection of enzymes and proteins for bioactive peptide generation Identification of bioactive hydrolysatesAbstract: Inhibition of angiotensin-I-converting enzyme (ACE-I), renin, and dipeptidyl peptidase-IV (DPP-IV) plays a key role in the treatment of hypertension and type-2 diabetes. The aim of this study was to isolate and characterize novel ACE-I, renin, and DPP-IV inhibitory peptides from a papain hydrolysate of bovine serum albumin (BSA). BSA was obtained from whole bovine blood and hydrolyzed with the food-grade enzyme papain. The generated hydrolysate was further purified using ultrafiltration and high performance liquid chromatography (HPLC), and a number of novel bioactive peptides were identified using de novo peptide sequencing. These included SLR, YY, ER, and FR which inhibited the activity of the enzyme ACE-I by half at a concentration of 0.17 ± 0.02, 0.18 ± 0.04, 0.27 ± 0.01, and 0.42 ± 0.02 mM, respectively. In addition, the 1 kDa fraction of the papain hydrolysate was assessed for antihypertensive activity in vivo using spontaneously hypertensive rats (SHRs) and reduced systolic blood pressure over a 24 h period when compared with the control (p < 0.001). Results demonstrated the potential of bovine serum albumin as a source of bioactive peptides with health-promoting properties and potential for use as functional food ingredients. Highlights: Utilization of bovine blood proteins for the generation of biologically active peptides In silico analysis used for selection of enzymes and proteins for bioactive peptide generation Identification of bioactive hydrolysates with in vitro ACE-I inhibitory activity Identification of bioactive di- and tri-peptides including the renin inhibitor SLR and the ACE-I inhibitors YY, ER, and FR Assessment of hypotensive effects in vivo in spontaneously hypertensive rats … (more)
- Is Part Of:
- Food research international. Volume 81(2016:Mar.)
- Journal:
- Food research international
- Issue:
- Volume 81(2016:Mar.)
- Issue Display:
- Volume 81 (2016)
- Year:
- 2016
- Volume:
- 81
- Issue Sort Value:
- 2016-0081-0000-0000
- Page Start:
- 91
- Page End:
- 99
- Publication Date:
- 2016-03
- Subjects:
- DPP-IV dipeptidyl peptidase-IV -- GLP-1 glucagon-like peptide-1 -- GIP gastric-inhibitory peptide -- ACE-I angiotensin-I-converting enzyme -- RAAS renin-angiotensin-aldosterone system -- EFSA European Food Safety Authority -- BSA bovine serum albumin -- MWCO molecular weight cut-off -- HPLC high performance liquid chromatography -- SHRs spontaneously hypertensive rats -- FA formic acid -- DMSO dimethyl sulfoxide -- ACN acetonitrile -- NUFH non-ultrafiltrated hydrolysate -- 1UFH hydrolysate ultrafiltrated with a 1 kDa MWCO membrane -- 3UFH hydrolysate ultrafiltrated with a 3 kDa MWCO membrane -- 10UFH hydrolysate ultrafiltrated with a 10 kDa MWCO membrane -- DDA data-dependent acquisition -- MW molecular weight -- MW-SPPS microwave-assisted solid phase peptide synthesis -- MALDI matrix assisted laser desorption/ionization -- TOF time of flight -- MS mass spectrometry -- S.D. standard deviation -- PBS phosphate buffer saline -- SBP systolic blood pressure -- QSAR quantitative structure–activity relationship -- SEM standard error of the mean
Bioactive peptides -- Renin -- ACE-I -- Hypertension -- Spontaneously hypertensive rats -- Serum albumin
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
Electronic journals
664.005 - Journal URLs:
- http://www.sciencedirect.com/science/journal/09639969 ↗
http://www.elsevier.com/journals ↗ - DOI:
- 10.1016/j.foodres.2016.01.007 ↗
- Languages:
- English
- ISSNs:
- 0963-9969
- Deposit Type:
- Legaldeposit
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- Available online (eLD content is only available in our Reading Rooms) ↗
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