Impact of in Vitro Gastrointestinal Digestion and Transepithelial Transport on Antioxidant and ACE-Inhibitory Activities of Brewer’s Spent Yeast Autolysate

2016 ◽  
Vol 64 (39) ◽  
pp. 7335-7341 ◽  
Author(s):  
Elsa F. Vieira ◽  
José das Neves ◽  
Rui Vitorino ◽  
Diana Dias da Silva ◽  
Helena Carmo ◽  
...  
Keyword(s):  
Transepithelial Transport ◽  
Gastrointestinal Digestion ◽  
In Vitro Gastrointestinal Digestion ◽  
Yeast Autolysate ◽  
Inhibitory Activities ◽  
Brewer’S Spent Yeast ◽  
Ace Inhibitory

Angiotensin I Converting Enzyme–Inhibitory Activity of Bovine, Ovine, and Caprine κ-Casein Macropeptides and Their Tryptic Hydrolysates

2003 ◽  
Vol 66 (9) ◽  
pp. 1686-1692 ◽  
Author(s):  
M. A. MANSO ◽  
R. LÓPEZ-FANDIÑO
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Gastrointestinal Conditions ◽  
Tryptic Hydrolysate ◽  
Inhibitory Activities ◽  
Ace Inhibitory

This work evaluated the angiotensin-converting enzyme (ACE)–inhibitory activities of bovine, ovine, and caprine κ-casein macropeptides (CMPs) and their tryptic hydrolysates. The results obtained indicate that bovine, ovine, and caprine CMPs exhibited moderate in vitro ACE-inhibitory activities that increased considerably after digestion under simulated gastrointestinal conditions. Active peptides could also be produced from CMPs via proteolysis with trypsin, with tryptic hydrolysates exhibiting a more extensive ACE-inhibitory activity than intact CMPs during simulated gastrointestinal digestion. Two active fractions were chromatographically separated from the tryptic hydrolysate of the bovine CMP, but their complexity hampered the assignment of the ACE-inhibitory activity to specific peptide sequences. Evidence for the release of the strong ACE-inhibitory tripeptide IPP was found upon simulation of the gastrointestinal digestion of peptides released by trypsin from the CMP sequence. These findings might help to promote further exploitation of cheese whey in the preparation of nutraceuticals for inclusion in the composition of functional food products with high added values.

scholarly journals Antioxidant and ACE-inhibitory activities of hydrolysates obtained from lupin and faba bean proteins via enzymatic hydrolysis and fermentation

2020 ◽  
Vol 12 (2) ◽  
pp. 99-114
Author(s):  
Blanca Elizabeth Hernández-Rodríguez ◽  
Eleazar Aguirre-Mandujano ◽  
Arely Prado-Barragán ◽  
Guillermo Ismael Koh-Kantún ◽  
Consuelo Lobato-Calleros
Keyword(s):  
Faba Bean ◽  
Radical Scavenging Activity ◽  
Radical Scavenging ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Native Proteins ◽  
Health Promoting ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Introduction: Legumes and pseudocereals protein hydrolysates have been recognized as having improved potential health-promoting properties as compared with native proteins. Objectives: 1) Produce bioactive hydrolysates from lupin and faba bean proteins by enzymatic hydrolysis (EH) and solid-state fermentation (SF), 2) compare the angiotensin converting enzyme (ACE)-inhibitory and antioxidant activities of the hydrolysates and 3) evaluate the effect of in vitro gastrointestinal digestion on the antioxidant and antihypertensive activities of the hydrolysates. Methodology: Hydrolysates from proteins of faba bean (Vicia faba) and lupin (Lupinus gredensis) were obtained by EH using Flavourzyme and SF by Aspergillus niger. The antioxidant and ACE-inhibitory activities of the hydrolysates were assessed. Results: All the hydrolysates presented DPPH radical scavenging activity, with IC50 ranging from 1.23-2.08 mgprotein·mL-1. Only EH and SF hydrolysates obtained from lupin proteins had ACE-inhibitory activity (IC50: 2.39 and 14.08 mgprotein·mL-1, respectively). Radical scavenging activity hydrolysates was significantly reduced after in vitro gastrointestinal digestion, while ACE-inhibitory activity showed variable behavior. Study limitations: Specific molecules responsible for the in vitro health-promoting properties should be identified. Originality: Relevant information is provided on health-promoting attributes of faba bean and lupin hydrolysates obtained by EH and SF. Conclusions: EH and SF improved the health-promoting properties of faba bean and lupin native proteins.

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