Influence of degree of hydrolysis on functional properties, antioxidant activity and ACE inhibitory activity of peanut protein hydrolysate

2010 ◽  
Vol 121 (1) ◽  
pp. 178-184 ◽  
Author(s):  
S.N. Jamdar ◽  
V. Rajalakshmi ◽  
M.D. Pednekar ◽  
F. Juan ◽  
V. Yardi ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Functional Properties ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Peanut Protein ◽  
Degree Of Hydrolysis ◽  
Ace Inhibitory Activity ◽  
Ace Inhibitory

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 Effect of in Vitro Gastrointestinal Digestion on Bioactivity of Poultry Protein Hydrolysate

2016 ◽  
Vol 4 (Special-Issue-October) ◽  
pp. 77-86 ◽  
Author(s):  
Torkova Anna ◽  
Kononikhin Alexey ◽  
Bugrova Anna ◽  
Khotchenkov Vyacheslav ◽  
Tsentalovich Mikhail ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Gastrointestinal Digestion ◽  
Ace Inhibitory Activity ◽  
Food Ingredient ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

In vitro simulated gastrointestinal digestion (GID) was performed to evaluate changes in bioactive properties of Poultry protein hydrolysate HCP Premium P150 (PPH) showing strong antioxidant (448.2±37.0 µM TE/g of protein) and moderate Angiotensin-I converting enzyme inhibitory activity (IC50 0.617±0.022 mg/ml). Antioxidant and ACE-inhibitory activity were measured with use of ORAC assay and FRET-substrate methods, correspondingly. Gastric digestion (GD) increased ACE inhibitory activity 2.23 times and didn’t change antioxidant activity of PPH significantly. The subsequent intestinal digestion increased antioxidant activity 1.29 times and didn’t change ACE-inhibitory activity significantly. New potent ACE-inhibitory peptides: APGAPGPVG (IC50 16.2±3.8 µM), PDLVF (IC50 84.9±6.3 µM) and antioxidant dipeptide WG (2.29±0.04 µM TE/µM) were identified in the digested PPH. The digested PPH proved to be a rich source of antioxidant and ACE inhibiting molecules and could be a potential new food ingredient used for prevention or treatment of socially significant diseases.

scholarly journals Study of the antihypertensive peptide from soy protein hydrolysate produced by steam blasting treatment

2021 ◽  
Vol 2 (2) ◽  
pp. 149-156
Author(s):  
Sri Peni Wijayanti ◽  
◽  
Try Surya Anditya ◽  
Noer Laily ◽  
◽  
...  
Keyword(s):  
Soy Protein ◽  
Inhibitory Activity ◽  
Protein Hydrolysate ◽  
Protein Profile ◽  
Protein Solubility ◽  
Heating Time ◽  
Degree Of Hydrolysis ◽  
Ace Inhibitory Activity ◽  
Soy Protein Hydrolysate ◽  
Ace Inhibitory

The purpose of this study was to determine the effect of steam blasting on soybeans and to evaluate the soy protein hydrolysate (SPH) resulting from steam blasting on ace inhibitory activity. Steam blasting works on the principle of heat and pressure. The research conducted begins with a process of pressure treatment and the heating time of soybeans. The pressures used were 2, 3 and 5 bar with heating time (hydrolysis) of 10, 20, 30, 40, 50 and 60 min for each pressure. Furthermore, the soybean resulting from steam blasting was analyzed for the degree of hydrolysis (DH), dissolved protein concentration, protein profile, and also its fractions. Then the ace inhibitory activity was performed on the SPH fraction. The results showed that the higher the pressure and the longer the heating time, the soybean colour from the steam blasting would turn dark brown due to the Maillard reaction. The value of % DH and protein solubility increase with a higher pressure. The % DH values ranged from 76 - 96%. The steam blasting process for soybeans also eliminates anti-nutritional properties and off-flavour compounds in soybeans and cuts protein into peptides/polypeptides. The fractionation results showed that the SPH fraction produced from the soybean steam blasting process had the highest ace inhibitory activity value of 68%, produced by the SPH fraction of 2 bar of 40 min steam blasting treatment. The SPH produced from the steam blasting process can potentially be a source of protein/peptides that can lower blood pressure (hypertension).

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.

Physicochemical, conformational properties and ACE-inhibitory activity of peanut protein marinated by aged vinegar

LWT ◽  
2019 ◽  
Vol 101 ◽  
pp. 469-475 ◽  
Author(s):  
Shanguang Guo ◽  
Minmin Ai ◽  
Jielang Liu ◽  
Zifeng Luo ◽  
Jiayi Yu ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Peanut Protein ◽  
Ace Inhibitory Activity ◽  
Conformational Properties ◽  
Ace Inhibitory

Comparison of Yield, Antioxidant Activity and Functional Properties of Protein Hydrolysates from Tuna and Pollock Frame

2012 ◽  
Vol 554-556 ◽  
pp. 1327-1331
Author(s):  
Li Jun Zhang ◽  
Qian Cheng Zhao ◽  
Bing Bing Wang ◽  
Xue Wan ◽  
Zhi Bo Li ◽  
...  
Keyword(s):  
Antioxidant Activity ◽  
Functional Properties ◽  
Protein Hydrolysate ◽  
Protein Hydrolysates ◽  
Degree Of Hydrolysis ◽  
Basic Composition ◽  
Foaming Ability ◽  
Hydrolysis Of ◽  
Better Than

Protein hydrolysates from Tuna frame (TFPH) and Pollock frame (PFPH) were prepared by papain, respectively.The yield, the basic composition content, the antioxidant activity and functional properties (solubility, emulsifying and foaming ability) and the degree of hydrolysis of the protein hydrolysates were evaluated. Results suggest that solubility, antioxidant activity of protein hydrolysate from Pollock frame are better than that of tuna frame, but the yield is lower than that of tuna frame.

scholarly journals Partial Purification and Characterization of Bioactive Peptides from Cooked New Zealand Green-Lipped Mussel (Perna canaliculus) Protein Hydrolyzates

Foods ◽  
2020 ◽  
Vol 9 (7) ◽  
pp. 879
Author(s):  
Ramya Jayaprakash ◽  
Conrad O. Perera
Keyword(s):  
New Zealand ◽  
Inhibitory Activity ◽  
Bioactive Peptides ◽  
Protein Hydrolysate ◽  
Gel Filtration ◽  
Partial Purification ◽  
Ace Inhibitory Activity ◽  
Perna Canaliculus ◽  
Inhibitory Activities ◽  
Ace Inhibitory

Proteins from fresh New Zealand green-lipped mussels were hydrolyzed for 240 min using pepsin and alcalase. The extent of the hydrolysis, antioxidant, antimicrobial, and angiotensin-converting enzyme (ACE) inhibitory activities of each protein hydrolysate were investigated. Peptides obtained from pepsin hydrolysis after 30 min, named GPH, exhibited the highest antioxidant and ACE inhibitory activity, but no antimicrobial activity. Purification of the GPH using gel-filtration chromatography revealed that the protein fraction (GPH-IV*) containing peptides with a molecular weight (MW) below 5 kDa had the strongest antioxidant and ACE inhibitory activities. Further purification was done using reverse-phase HPLC (RP-HPLC) and the only major peak obtained (GPH-IV*-P2) had the highest antioxidant and ACE inhibitory activity. From this fraction, several bioactive peptides with an MW ≈ 5 kDa were identified using LC-MS and in silico analyses. This research highlights that green-lipped mussel protein hydrolysates could be used as a good source of bioactive peptides with potential therapeutic applications.

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