title: Inhibitory properties of bambara groundnut protein hydrolysate and peptide fractions against angiotensin-converting enzymes, renin and free radicals.
abstract: BACKGROUND
  An increased rate of high blood pressure has led to critical human hypertensive conditions in most nations. In the present study, bambara protein hydrolysates (BPHs) obtained using three different proteases (alcalase, trypsin and pepsin) and their peptide fractions (molecular weight: 10, 5, 3 and 1 kDa) were investigated for antihypertensive and antioxidant activities.
  
  
  RESULTS
  Alcalase hydrolysate contained the highest amount of low molecular weight (LMW) peptides compared to pepsin and trypsin hydrolysates. LMW peptides fractions (<1 kDa) exhibited the highest inhibitory activity against angiotensin-converting enzyme (ACE) for all the enzymes hydrolysates. For renin inhibition, alcalase hydrolysate showed the highest inhibition at 59% compared to other hydrolysates and their corresponding membrane fractions. The antioxidant power of bambara protein hydrolysates and peptide fractions was evaluated through the inhibition of linoleic acid peroxidation and ABTS scavenging activity. Among the hydrolysates, alcalase exhibited the highest inhibition of linoleic acid oxidation. Furthermore, all BPHs were able to scavenge ABTS•+to a three-fold greater extent compared to the isolate.
  
  
  CONCLUSIONS
  BPH and LMW peptide fractions could potentially serve as useful ingredients in the formulation of functional foods and nutraceuticals against high blood pressure and oxidative stress. © 2016 Society of Chemical Industry.
authors: Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, PO Box 1334, Durban 4001, South Africa.|Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2 N2, Canada.
authors: Abimbola K
authors: AK
authors: Arise
authors: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2 N2, Canada.
authors: Adeola M
authors: AM
authors: Alashi
authors: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2 N2, Canada.
authors: Ifeanyi D
authors: ID
authors: Nwachukwu
authors: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2 N2, Canada.
authors: Sunday A
authors: SA
authors: Malomo
authors: Department of Human Nutritional Sciences, University of Manitoba, Winnipeg, MB, R3T 2 N2, Canada.
authors: Rotimi E
authors: RE
authors: Aluko
authors: Department of Biotechnology and Food Technology, Faculty of Applied Sciences, Durban University of Technology, PO Box 1334, Durban 4001, South Africa.
authors: Eric O
authors: EO
authors: Amonsou
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D000959:Antihypertensive Agents / Q000737:chemistry*; D007887:Fabaceae / Q000737:chemistry*; D016166:Free Radical Scavengers / Q000737:chemistry*; D005609:Free Radicals / Q000737:chemistry; D007700:Kinetics; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism; D010940:Plant Proteins / Q000737:chemistry*; D011492:Protein Hydrolysates / Q000737:chemistry; D012083:Renin / Q000737:chemistry
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000959:Antihypertensive Agents; D016166:Free Radical Scavengers; D005609:Free Radicals; D010940:Plant Proteins; D011492:Protein Hydrolysates; D007703:Peptidyl-Dipeptidase A; D012083:Renin
keywords: angiotensin-converting enzyme; antioxidant activity; bambara; membrane ultrafiltration; protein hydrolysate; renin