Angiotensin-I converting enzyme inhibitory and antioxidant activities of peptide fractions extracted by ultrafiltration of cowpea Vigna unguiculata hydrolysates

2010 ◽  
Vol 90 (14) ◽  
pp. 2512-2518 ◽  
Author(s):  
Maira R Segura Campos ◽  
Luis A Chel Guerrero ◽  
David A Betancur Ancona
Keyword(s):  
Vigna Unguiculata ◽  
Antioxidant Activities ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Peptide Fractions

Peptides present in the non-digestible fraction of common beans (Phaseolus vulgaris L.) inhibit the angiotensin-I converting enzyme by interacting with its catalytic cavity independent of their antioxidant capacity

2015 ◽  
Vol 6 (5) ◽  
pp. 1470-1479 ◽  
Author(s):  
Diego A. Luna-Vital ◽  
Elvira González de Mejía ◽  
Sandra Mendoza ◽  
Guadalupe Loarca-Piña
Keyword(s):  
Phaseolus Vulgaris ◽  
Antioxidant Capacity ◽  
Common Bean ◽  
Antioxidant Activities ◽  
Common Beans ◽  
Converting Enzyme ◽  
Phaseolus Vulgaris L ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

Pure peptides present in common-bean non-digestible fraction inhibited ACE by interacting with its catalytic cavity, and presented antioxidant activities.

scholarly journals Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysate from Muscle of Barbel (Barbus callensis)

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Assaad Sila ◽  
Anissa Haddar ◽  
Oscar Martinez-Alvarez ◽  
Ali Bougatef
Keyword(s):  
Antioxidant Activities ◽  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Radical Scavenging ◽  
Reducing Power ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained byin vitrosystems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.

Angiotensin I-converting enzyme inhibitory activity in peptide fractions from hard-to-cook bean hydrolysates

2010 ◽  
Vol 150 ◽  
pp. 309-310
Author(s):  
Jorge Ruiz-Ruiz ◽  
Gloria Dávila-Ortíz ◽  
Luis Chel-Guerrero ◽  
David Betancur-Ancona
Keyword(s):  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Peptide Fractions

Angiotensin-I converting enzyme inhibitory and antioxidant activities of protein hydrolysates from Phaseolus lunatus and Phaseolus vulgaris seeds

LWT ◽  
2009 ◽  
Vol 42 (10) ◽  
pp. 1597-1604 ◽  
Author(s):  
Juan Torruco-Uco ◽  
Luis Chel-Guerrero ◽  
Alma Martínez-Ayala ◽  
Gloria Dávila-Ortíz ◽  
David Betancur-Ancona
Keyword(s):  
Phaseolus Vulgaris ◽  
Antioxidant Activities ◽  
Protein Hydrolysates ◽  
Phaseolus Lunatus ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

Angiotensin I-converting enzyme-inhibitory peptide fractions from albumin 1 and globulin as obtained of amaranth grain

2009 ◽  
Vol 116 (2) ◽  
pp. 437-444 ◽  
Author(s):  
E.G. Tovar-Pérez ◽  
I. Guerrero-Legarreta ◽  
A. Farrés-González ◽  
J. Soriano-Santos
Keyword(s):  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Amaranth Grain ◽  
Peptide Fractions
Sign in / Sign up

Export Citation Format

Share Document