title: A Bovine Fibrinogen-Enriched Fraction as a Source of Peptides with in Vitro Renin and Angiotensin-I-Converting Enzyme Inhibitory Activities.
abstract: Bovine fibrinogen is currently used in the food industry as a binding agent in restructured meat products. However, this protein is underused as a source of bioactive peptides. In this study, a number of novel angiotensin-I-converting enzyme (ACE-I) and renin inhibitory peptides were identified and enriched from a bovine fibrinogen fraction. Fibrinogen was isolated and enriched from bovine blood and hydrolyzed with the food-grade enzyme papain, which was selected for use using in silico analysis. The generated hydrolysate was subjected to ultrafiltration and its peptide profile characterized by liquid chromatography-tandem mass spectrometry. A number of peptides were identified and chemically synthesized to confirm their bioactivity in vitro. Identified peptides included the multifunctional tripeptide SLR, corresponding to f(35-37) of the β-chain of bovine fibrinogen with ACE-I and renin IC50 values of 0.17 and 7.2 mM, respectively. Moreover, the resistance of identified peptides to gastrointestinal degradation and their bitterness were predicted using in silico methods.
authors.affiliation: Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Ashtown, Dublin 15, Dublin, Ireland.
authors.forename: Tomas
authors.initials: T
authors.lastname: Lafarga
authors.affiliation: Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Ashtown, Dublin 15, Dublin, Ireland.
authors.forename: Dilip K
authors.initials: DK
authors.lastname: Rai
authors.affiliation: Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Moorepark, Fermoy, Co. Cork, Ireland.
authors.forename: Paula
authors.initials: P
authors.lastname: O'Connor
authors.affiliation: Teagasc, The Irish Agricultural and Food Development Authority, Food BioSciences Department, Ashtown, Dublin 15, Dublin, Ireland.
authors.forename: Maria
authors.initials: M
authors.lastname: Hayes
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000818:Animals; D002417:Cattle; D005340:Fibrinogen / Q000737:chemistry*; D006868:Hydrolysis; D013058:Mass Spectrometry; D008969:Molecular Sequence Data; D009842:Oligopeptides / Q000737:chemistry* / Q000302:isolation & purification; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry / Q000302:isolation & purification; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry; D012083:Renin / Q000737:chemistry; D000092502:Renin Inhibitors
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D005340:Fibrinogen; D009842:Oligopeptides; D010455:Peptides; D007703:Peptidyl-Dipeptidase A; D012083:Renin; D000092502:Renin Inhibitors; C027509:renin inhibitory peptide
keywords: ACE-I; DPP-IV; bioactive peptides; blood; bovine fibrinogen; renin