Inhibitory activity of chia (Salvia hispanica L.) protein fractions against angiotensin I-converting enzyme and antioxidant capacity

LWT ◽  
2015 ◽  
Vol 64 (1) ◽  
pp. 236-242 ◽  
Author(s):  
Domancar Orona-Tamayo ◽  
María Elena Valverde ◽  
Blanca Nieto-Rendón ◽  
Octavio Paredes-López
Keyword(s):  
Antioxidant Capacity ◽  
Inhibitory Activity ◽  
Protein Fractions ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Salvia Hispanica ◽  
L Protein ◽  
Angiotensin I Converting Enzyme ◽  
Salvia Hispanica L

Angiotensin I-converting enzyme inhibitory activity of enzymatic hydrolysates of goat milk protein fractions

2013 ◽  
Vol 32 (2) ◽  
pp. 175-183 ◽  
Author(s):  
F. Javier Espejo-Carpio ◽  
Cristian De Gobba ◽  
Antonio Guadix ◽  
Emilia M. Guadix ◽  
Jeanette Otte
Keyword(s):  
Inhibitory Activity ◽  
Milk Protein ◽  
Goat Milk ◽  
Protein Fractions ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Enzymatic Hydrolysates ◽  
Angiotensin I Converting Enzyme

scholarly journals Angiotensin I-Converting Enzyme Inhibitory Peptides of Chia (Salvia hispanica) Produced by Enzymatic Hydrolysis

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Maira Rubi Segura Campos ◽  
Fanny Peralta González ◽  
Luis Chel Guerrero ◽  
David Betancur Ancona
Keyword(s):  
Amino Acid ◽  
Side Effects ◽  
Amino Acid Composition ◽  
Acid Composition ◽  
Inhibitory Activity ◽  
Gel Filtration ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Salvia Hispanica ◽  
Angiotensin I Converting Enzyme

Synthetic angiotensin I-converting enzyme (ACE-I) inhibitors can have undesirable side effects, while natural inhibitors have no side effects and are potential nutraceuticals. A protein-rich fraction from chia (Salvia hispanicaL.) seed was hydrolyzed with an Alcalase-Flavourzyme sequential system and the hydrolysate ultrafiltered through four molecular weight cut-off membranes (1 kDa, 3 kDa, 5 kDa, and 10 kDa). ACE-I inhibitory activity was quantified in the hydrolysate and ultrafiltered fractions. The hydrolysate was extensive (DH = 51.64%) and had 58.46% ACE-inhibitory activity. Inhibition ranged from 53.84% to 69.31% in the five ultrafiltered fractions and was highest in the <1 kDa fraction (69.31%). This fraction’s amino acid composition was identified and then it was purified by gel filtration chromatography and ACE-I inhibition measured in the purified fractions. Amino acid composition suggested that hydrophobic residues contributed substantially to chia peptide ACE-I inhibitory strength, probably by blocking angiotensin II production. Inhibitory activity ranged from 48.41% to 62.58% in the purified fractions, but fraction F1 (1.5–2.5 kDa) exhibited the highest inhibition (IC50= 3.97 μg/mL; 427–455 mL elution volume). The results point out the possibility of obtaining bioactive peptides from chia proteins by means of a controlled protein hydrolysis using Alcalase-Flavourzyme sequentional system.

Antioxidant capacity and angiotensin I converting enzyme inhibitory activity of a melon concentrate rich in superoxide dismutase

2012 ◽  
Vol 135 (3) ◽  
pp. 1298-1302 ◽  
Author(s):  
Julie Carillon ◽  
Daniele Del Rio ◽  
Pierre-Louis Teissèdre ◽  
Jean-Paul Cristol ◽  
Dominique Lacan ◽  
...  
Keyword(s):  
Superoxide Dismutase ◽  
Antioxidant Capacity ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

2005 ◽  
Vol 10 (3) ◽  
pp. 239-243 ◽  
Author(s):  
Rohan Karawita ◽  
Pyo-Jam park ◽  
Nalin Siriwardhana ◽  
Byong-Tae Jeon ◽  
Sang-Ho Moon ◽  
...  
Keyword(s):  
Cervus Elaphus ◽  
Inhibitory Activity ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Velvet Antler ◽  
Ace Inhibitory
Sign in / Sign up

Export Citation Format

Share Document