title: High-pressure improves enzymatic proteolysis and the release of peptides with angiotensin I converting enzyme inhibitory and antioxidant activities from lentil proteins.
abstract: Angiotensin I converting enzyme (ACE) inhibitory and antioxidant peptides are receiving attention due to their beneficial effects in the prevention/treatment of hypertension. The objective was to explore the effect of high hydrostatic pressure (HP) on proteolysis by different proteases and the release of bioactive peptides from lentil proteins. Pressurisation (100-300 MPa) enhanced the hydrolytic efficiency of Protamex, Savinase and Corolase 7089 compared to Alcalase. Proteolysis at 300 MPa led to a complete degradation of lentil proteins and increased peptide (<3 kDa) concentration by all enzymes. Proteolysis at 300 MPa by Savinase gave rise to lentil hydrolysates (S300) with the highest ACE-inhibitory and antioxidant activities that were retained upon in vitro gastrointestinal digestion. The peptides responsible for the multifunctional properties of S300 hydrolysate were identified as different fragments from storage proteins and the allergen Len c 1. These results support the potential of HP as a technology for the cost-effective production of bioactive peptides from lentil proteins during enzymatic proteolysis.
authors.affiliation: Institute of Food Science, Technology and Nutrition, C/ Juan de la Cierva 3, 28006 Madrid, Spain.
authors.forename: P
authors.initials: P
authors.lastname: Garcia-Mora
authors.affiliation: Institute of Food Science, Technology and Nutrition, C/ Juan de la Cierva 3, 28006 Madrid, Spain.
authors.forename: E
authors.initials: E
authors.lastname: Peñas
authors.affiliation: Institute of Food Science, Technology and Nutrition, C/ Juan de la Cierva 3, 28006 Madrid, Spain.
authors.forename: J
authors.initials: J
authors.lastname: Frias
authors.affiliation: Institute of Food Science, Technology and Nutrition, C/ Juan de la Cierva 3, 28006 Madrid, Spain.
authors.forename: R
authors.initials: R
authors.lastname: Gomez
authors.affiliation: Institute of Food Science, Technology and Nutrition, C/ Juan de la Cierva 3, 28006 Madrid, Spain. Electronic address: c.m.villaluenga@csic.es.
authors.forename: C
authors.initials: C
authors.lastname: Martinez-Villaluenga
mesh_terms: D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry*; D000975:Antioxidants / Q000737:chemistry*; D010450:Endopeptidases / Q000378:metabolism; D041981:Gastrointestinal Tract / Q000378:metabolism; D006801:Humans; D006863:Hydrogen-Ion Concentration; D006868:Hydrolysis; D027806:Lens Plant / Q000378:metabolism*; D010100:Oxygen / Q000737:chemistry; D010447:Peptide Hydrolases / Q000737:chemistry; D010455:Peptides / Q000737:chemistry; D007703:Peptidyl-Dipeptidase A / Q000378:metabolism*; D011312:Pressure; D011492:Protein Hydrolysates / Q000737:chemistry; D059748:Proteolysis; D012995:Solubility; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D010455:Peptides; D011492:Protein Hydrolysates; D010450:Endopeptidases; D010447:Peptide Hydrolases; D007703:Peptidyl-Dipeptidase A; D010100:Oxygen
keywords: Angiotensin I converting enzyme; Antioxidant activity; High-hydrostatic pressure; Lentil peptides; Proteolysis