title: High-Pressure-Assisted Enzymatic Release of Peptides and Phenolics Increases Angiotensin Converting Enzyme I Inhibitory and Antioxidant Activities of Pinto Bean Hydrolysates.
abstract: Pinto bean protein concentrate was hydrolyzed by subtilisins at 0.1, 100, and 200 MPa and 50 °C for 15 min. Alcalase hydrolysis at 100 MPa led to higher ACE inhibition, reducing power, and free radical scavenging activity of hydrolysates. However, hydrolysate obtained by Savinase at 200 MPa showed the best ACE-inhibitory and radical scavenging activities. Proteolysis by Savinase at 200 MPa was considered the most effective treatment to increase small peptides (<3 kDa), flavonoids, total phenolic compounds, and oxygen radical absorbance capacity in hydrolysates. In this hydrolysate, small phaseolin fragments with reported ACE-inhibitory and antioxidant sequences were identified. Catechin, pelargonidin 3-glucoside, and ferulic acid were the main phenolic compounds. Hihg-pressure-assisted hydrolysis of common bean protein concentrates would provide benefits in the production of functional hydrolysates providing higher functionality and added value to the resulting hydrolysate due to synergistic effects of bioactive peptides and soluble phenolics.
authors: Department of Characterization, Quality and Safety, Institute of Food Science, Technology and Nutrition (ICTAN-CSIC) , Juan de la Cierva 3, Madrid 28006, Spain.
authors: Patricia
authors: P
authors: Garcia-Mora
authors: Department of Characterization, Quality and Safety, Institute of Food Science, Technology and Nutrition (ICTAN-CSIC) , Juan de la Cierva 3, Madrid 28006, Spain.
authors: Elena
authors: E
authors: Peñas
authors: Department of Characterization, Quality and Safety, Institute of Food Science, Technology and Nutrition (ICTAN-CSIC) , Juan de la Cierva 3, Madrid 28006, Spain.
authors: Juana
authors: J
authors: Frias
authors: Division of Food Science, Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences , Tuwima 10, P.O. Box 55, 10-748 Olsztyn, Poland.
authors: Henryk
authors: H
authors: Zieliński
authors: Division of Food Science, Institute of Animal Reproduction and Food Research of the Polish Academy of Sciences , Tuwima 10, P.O. Box 55, 10-748 Olsztyn, Poland.
authors: Wiesław
authors: W
authors: Wiczkowski
authors: Department of Chemistry, University of Warmia and Mazury in Olsztyn , Plac Lodzki 4, 10-727 Olsztyn, Poland.
authors: Danuta
authors: D
authors: Zielińska
authors: Department of Characterization, Quality and Safety, Institute of Food Science, Technology and Nutrition (ICTAN-CSIC) , Juan de la Cierva 3, Madrid 28006, Spain.
authors: Cristina
authors: C
authors: Martínez-Villaluenga
mesh_terms: D000595:Amino Acid Sequence; D000806:Angiotensin-Converting Enzyme Inhibitors / Q000737:chemistry* / Q000302:isolation & purification; D000975:Antioxidants / Q000737:chemistry*; D007887:Fabaceae / Q000737:chemistry*; D008969:Molecular Sequence Data; D010449:Peptide Mapping; D010455:Peptides / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D007703:Peptidyl-Dipeptidase A / Q000737:chemistry; D010636:Phenols / Q000737:chemistry* / Q000302:isolation & purification; D010936:Plant Extracts / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D000806:Angiotensin-Converting Enzyme Inhibitors; D000975:Antioxidants; D010455:Peptides; D010636:Phenols; D010936:Plant Extracts; D007703:Peptidyl-Dipeptidase A
keywords: antioxidant activity; bioactive peptides; biological activity; high-pressure-assisted proteolysis; phenolic compounds; pinto bean; reducing power