Evaluation of angiotensin I-converting enzyme (ACE) inhibitory activities of smooth hound (Mustelus mustelus) muscle protein hydrolysates generated by gastrointestinal proteases: identification of the most potent active peptide

2010 ◽  
Vol 231 (1) ◽  
pp. 127-135 ◽  
Author(s):  
Ali Bougatef ◽  
Rafik Balti ◽  
Naïma Nedjar-Arroume ◽  
Rozenn Ravallec ◽  
Estelle Yaba Adjé ◽  
...  
Keyword(s):  
Muscle Protein ◽  
Protein Hydrolysates ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Active Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Inhibitory Activities ◽  
Ace Inhibitory

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 A novel angiotensin I-converting enzyme inhibitory peptide derived from the trypsin hydrolysates of salmon bone proteins

PLoS ONE ◽  
2021 ◽  
Vol 16 (9) ◽  
pp. e0256595
Author(s):  
Thanakrit Kaewsahnguan ◽  
Sajee Noitang ◽  
Papassara Sangtanoo ◽  
Piroonporn Srimongkol ◽  
Tanatorn Saisavoey ◽  
...  
Keyword(s):  
Response Surface ◽  
Inhibitory Activity ◽  
Fish Bone ◽  
Protein Hydrolysates ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptide ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

When fish are processed, fish bone becomes a key component of the waste, but to date very few researchers have sought to use fish bone to prepare protein hydrolysates as a means of adding value to the final product. This study, therefore, examines the potential of salmon bone, through an analysis of the benefits of its constituent components, namely fat, moisture, protein, and ash. In particular, the study seeks to optimize the process of enzymatic hydrolysis of salmon bone with trypsin in order to produce angiotensin-I converting enzyme (ACE) inhibitory peptides making use of response surface methodology in combination with central composite design (CCD). Optimum hydrolysis conditions concerning DH (degree of hydrolysis) and ACE-inhibitory activity were initially determined using the response surface model. Having thus determined which of the salmon bone protein hydrolysates (SBPH) offered the greatest level of ACE-inhibitory activity, these SBPH were duly selected to undergo ultrafiltration for further fractionation. It was found that the greatest ACE-inhibitory activity was achieved by the SBPH fraction which had a molecular weight lower than 0.65 kDa. This fraction underwent further purification using RP-HPLC, revealing that the F7 fraction offered the best ACE-inhibitory activity. For ACE inhibition, the ideal peptide in the context of the F7 fraction comprised eight amino acids: Phe-Cys-Leu-Tyr-Glu-Leu-Ala-Arg (FCLYELAR), while analysis of the Lineweaver-Burk plot revealed that the FCLYELAR peptide can serve as an uncompetitive ACE inhibitor. An examination of the molecular docking process showed that the FCLYELAR peptide was primarily able to provide ACE-inhibitory qualities as a consequence of the hydrogen bond interactions taking place between ACE and the peptide. Furthermore, upon isolation form the SBPH, the ACE-inhibitory peptide demonstrated ACE-inhibitory capabilities in vitro, underlining its potential for applications in the food and pharmaceutical sectors.

scholarly journals Production of Protein Hydrolysate Containing Antioxidant and Angiotensin -I-Converting Enzyme (ACE) Inhibitory Activities from Tuna (Katsuwonus pelamis) Blood

Processes ◽  
2020 ◽  
Vol 8 (11) ◽  
pp. 1518
Author(s):  
Natthaphon Mongkonkamthorn ◽  
Yuwares Malila ◽  
Suthasinee Yarnpakdee ◽  
Sakunkhun Makkhun ◽  
Joe M. Regenstein ◽  
...  
Keyword(s):  
Amino Acids ◽  
Radical Scavenging ◽  
Sensory Properties ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Antioxidant Power ◽  
Angiotensin I Converting Enzyme ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Tuna blood (TB) was subjected to enzymatic hydrolysis. The effects of the relationship of hydrolysis time (30–180 min) and enzyme concentration (0.5–3.0% w/w protein) on the degree of hydrolysis (DH), yield, antioxidant and angiotensin-I-converting enzyme (ACE) inhibitory activities were determined. The response surface methodology (RSM) showed that TB hydrolysis’s optimum conditions were hydrolysis for 180 min and Alcalase, Neutrase or Flavourzyme at 2.81%, 2.89% or 2.87% w/w protein, respectively. The hydrolysates with good DH (40–46%), yield (3.5–4.6%), the IC50 of DPPH (0.8–1.6 mg/mL) and ABTS (1.0–1.4 mg/mL) radical scavenging activity, ferric reducing antioxidant power (FRAP) value (0.28–0.65 mmol FeSO4/g) and IC50 of ACE inhibitory activity (0.15–0.28 mg/mL) were obtained with those conditions. The TB hydrolysate using Neutrase (TBHN) was selected for characterization in terms of amino acid composition, peptide fractions and sensory properties. The essential, hydrophobic and hydrophilic amino acids in TBHN were ~40%, 60% and 20% of total amino acids, respectively. The fraction of molecular weight <1 kDa showed the highest antioxidant and ACE inhibitory activities. Fishiness and bitterness were the main sensory properties of TBHN. Fortification of TBHN in mango jelly at ≤ 0.5% (w/w) was accepted by consumers as like moderately to like slightly, while mango jelly showed strong antioxidant and ACE inhibitory activities. TBHN could be developed for natural antioxidants and antihypertensive peptides in food and functional products.

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