Influence of degree of hydrolysis on functional properties and angiotensin I-converting enzyme-inhibitory activity of protein hydrolysates from cuttlefish (Sepia officinalis) by-products

2010 ◽  
pp. n/a-n/a ◽  
Author(s):  
Rafik Balti ◽  
Ali Bougatef ◽  
Nedra El-Hadj Ali ◽  
Dorra Zekri ◽  
Ahmed Barkia ◽  
...  
Keyword(s):  
Functional Properties ◽  
Inhibitory Activity ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Sepia Officinalis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
By Products

scholarly journals Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽  
2018 ◽  
Vol 8 (4) ◽  
pp. 101 ◽  
Author(s):  
Guowei Shu ◽  
Jie Huang ◽  
Chunju Bao ◽  
Jiangpeng Meng ◽  
He Chen ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Goat Milk ◽  
Cow Milk ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Angiotensin I-converting enzyme (ACE) peptides are bioactive peptides that have important value in terms of research and application in the prevention and treatment of hypertension. While widespread literature is concentrated on casein or whey protein for production of ACE-inhibitory peptides, relatively little information is available on selecting the proper proteases to hydrolyze the protein. In this study, skimmed cow and goat milk were hydrolyzed by four commercial proteases, including alkaline protease, trypsin, bromelain, and papain. Angiotensin I-converting enzyme-inhibitory peptides and degree of hydrolysis (DH) of hydrolysates were measured. Moreover, we compared the difference in ACE-inhibitory activity between cow and goat milk. The results indicated that the DH increased with the increase in hydrolysis time. The alkaline protease-treated hydrolysates exhibited the highest DH value and ACE-inhibitory activity. Additionally, the ACE-inhibitory activity of hydrolysates from goat milk was higher than that of cow milk-derived hydrolysates. Therefore, goat milk is a good source to obtain bioactive peptides with ACE-inhibitory activity, as compared with cow milk. A proper enzyme to produce ACE-inhibitory peptides is important for the development of functional milk products and will provide the theoretical basis for industrial production.

Functional properties and Angiotensin-I converting enzyme inhibitory activity of soy–whey proteins and fractions

2014 ◽  
Vol 64 ◽  
pp. 598-602 ◽  
Author(s):  
Tajudini Akande Lassissi ◽  
Navam S. Hettiarachchy ◽  
Srinivas J. Rayaprolu ◽  
Arvind Kannan ◽  
Michael Davis
Keyword(s):  
Functional Properties ◽  
Inhibitory Activity ◽  
Whey Proteins ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme

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.

scholarly journals The analysis of Angiotensin-I Converting Enzyme (ACE) by maitake (Grifrola frondosa) mycelia

2021 ◽  
Vol 8 (2) ◽  
pp. 69-72
Author(s):  
Yuen Sim Kheng ◽  
Young Liew Jeng ◽  
Maryana Mohamad Nor ◽  
Geng Boon Jia
Keyword(s):  
Inhibitory Activity ◽  
Protein Concentration ◽  
Bioactive Peptides ◽  
Biological Properties ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Hydrolysis Time ◽  
Angiotensin I Converting Enzyme ◽  
Freeze Dried

The Maitake (Grifola frondosa) is useful in treating diseases, specifically hypertension. Research on the maitake mycelia’s biological properties, nevertheless, are limited in the literature. This study aimed to (i) produce mushroom biomass adopting submerged fermentation, and (ii) investigate the Angiotensin-I Converting Enzyme inhibitory activity. Maitake mycelia’s yield after 14 days of fermentation under controlled conditions (approx. 1.32 g/L) were freeze-dried into powder and later were hydrolysed for analyses of Angiotensin-I Converting Enzyme inhibitory activity. Current results showed that the degree of hydrolysis increased in line with hydrolysis time, as the protein concentration for hydrolysed sample was 283.61 ± 7.14 µg/mL, however, the non-hydrolysed sample resulted in lesser protein content (46.76 ± 1.09 µg/mL). The hydrolysate maitake mycelia has higher Angiotensin-I Converting Enzyme inhibitory activity (46.48%) as compared to the non-hydrolysate maitake mycelia (20.19 ± 0.17%). This finding suggested maitake mycelia hydrolysate can be a source of potential bioactive peptides used in treating hypertension.

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.

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