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Ingeniería agrícola y biosistemas
versión On-line ISSN 2007-4026versión impresa ISSN 2007-3925
Resumen
HERNANDEZ-RODRIGUEZ, Blanca Elizabeth et al. Antioxidant and ACE-inhibitory activities of hydrolysates obtained from lupin and faba bean proteins via enzymatic hydrolysis and fermentation. Ing. agric. biosist. [online]. 2020, vol.12, n.2, pp.99-114. Epub 13-Jun-2022. ISSN 2007-4026. https://doi.org/10.5154/r.inagbi.2020.02.020.
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.
Palabras llave : faba bean; Lupinus gredensis; protein hydrolysates; flavourzyme; solid-state fermentation.