Two novel peptides with angiotensin I converting enzyme inhibitory and antioxidative activities from Scorpaena notata muscle protein hydrolysate

2016 ◽  
Vol 64 (2) ◽  
pp. 201-210 ◽  
Author(s):  
Neyssene Aissaoui ◽  
Ferid Abidi ◽  
Julie Hardouin ◽  
Zaineb Abdelkafi ◽  
Naziha Marrakchi ◽  
...  
Keyword(s):  
Muscle Protein ◽  
Protein Hydrolysate ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Scorpaena Notata

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.

scholarly journals Effect ofJatropha curcasPeptide Fractions on the Angiotensin I-Converting Enzyme Inhibitory Activity

2013 ◽  
Vol 2013 ◽  
pp. 1-8 ◽  
Author(s):  
Maira R. Segura-Campos ◽  
Fanny Peralta-González ◽  
Arturo Castellanos-Ruelas ◽  
Luis A. Chel-Guerrero ◽  
David A. Betancur-Ancona
Keyword(s):  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Ace Inhibition ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Hypertension is one of the most common worldwide diseases in humans. Angiotensin I-converting enzyme (ACE) plays an important role in regulating blood pressure and hypertension. An evaluation was done on the effect of Alcalase hydrolysis of defattedJatropha curcaskernel meal on ACE inhibitory activity in the resulting hydrolysate and its purified fractions. Alcalase exhibited broad specificity and produced a protein hydrolysate with a 21.35% degree of hydrolysis and 34.87% ACE inhibition. Ultrafiltration of the hydrolysate produced peptide fractions with increased biological activity (24.46–61.41%). Hydrophobic residues contributed substantially to the peptides’ inhibitory potency. The 5–10 and <1 kDa fractions were selected for further fractionation by gel filtration chromatography. ACE inhibitory activity (%) ranged from 22.66 to 45.96% with the 5–10 kDa ultrafiltered fraction and from 36.91 to 55.83% with the <1 kDa ultrafiltered fraction. The highest ACE inhibitory activity was observed inF2 ( μg/mL) from the 5–10 kDa fraction andF1 ( μg/mL) from the <1 kDa fraction. ACE inhibitory fractions fromJatrophakernel have potential applications in alternative hypertension therapies, adding a new application for theJatrophaplant protein fraction and improving the financial viability and sustainability of a Jatropha-based biodiesel industry.

Determination of angiotensin-I converting enzyme inhibitory peptides in chicken leg bone protein hydrolysate with alcalase

2009 ◽  
Vol 80 (1) ◽  
pp. 91-97 ◽  
Author(s):  
Fu-Yuan CHENG ◽  
Tien-Chun WAN ◽  
Yu-Tse LIU ◽  
Chi-Ming CHEN ◽  
Liang-Chuan LIN ◽  
...  
Keyword(s):  
Protein Hydrolysate ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme
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