scholarly journals Characterization and Antioxidant and Angiotensin I-Converting Enzyme (ACE)-Inhibitory Activities of Gelatin Hydrolysates Prepared from Extrusion-Pretreated Milkfish (Chanos chanos) Scale

Marine Drugs ◽  
2018 ◽  
Vol 16 (10) ◽  
pp. 346 ◽  
Author(s):  
Chun-Yung Huang ◽  
Yung-Hsiang Tsai ◽  
Yong-Han Hong ◽  
Shu-Ling Hsieh ◽  
Ren-Han Huang
Keyword(s):  
Antioxidant Activity ◽  
Biological Activities ◽  
Sodium Dodecyl ◽  
Degree Of Hydrolysis ◽  
Fish Scale ◽  
Fish Gelatin ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Fish gelatin hydrolysates have been shown to possess various biological activities due to their unique Gly-Pro-Y and Gly-X-Hyp sequences. In the current study, fish gelatin was extracted from non-extruded milkfish scale (FSG1) or extrusion-pretreated milkfish scale (FSG2); extracted gelatins were hydrolyzed with different combinations of Flavourzyme and Alcalase to give four different hydrolysates, namely: FSGH1 (FSG1 hydrolyzed with Flavourzyme), FSGH2 (FSG1 hydrolyzed with Alcalase + Flavourzyme), FSGH3 (FSG2 hydrolyzed with Flavourzyme), and FSGH4 (FSG2 hydrolyzed with Alcalase + Flavourzyme). The extrusion-pretreatment process enhanced the extraction yield of gelatin from fish scale. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and Fourier transform infrared (FTIR) analyses showed the extracts FSG1 and FSG2 possessed characteristics of gelatin. Moreover, the physicochemical characteristics of FSGH1–FSGH4 were examined by analyses of their degree of hydrolysis, amino acid composition, UV spectrum, FTIR spectrum, molecular weight, and RP-HPLC profile. Additional biological functional analyses showed that all of the studied gelatin hydrolysates FSGH1–FSGH4 possessed antioxidant activity dose-dependently as revealed by DPPH scavenging, ABTS scavenging, and reducing power analyses. In addition, FSGH2 and FSGH4 showed higher angiotensin-I-converting enzyme (ACE)-inhibitory activity as compared to FSGH1 and FSGH3. Taken together, FSGH2 and FSGH4 showed high antioxidant activity and potent anti-ACE activity. Due to the potential antioxidant and antihypertensive properties of FSGH2 and FSGH4, further research is needed to explore their possible use as natural supplementary raw materials in food and nutraceutical 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.

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 Isolation, Evaluation, and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides from Game Meat

Foods ◽  
2020 ◽  
Vol 9 (9) ◽  
pp. 1168
Author(s):  
Shiro Takeda ◽  
Sakurako Kaneko ◽  
Kazuyuki Sogawa ◽  
Abdulatef M Ahhmed ◽  
Hirofumi Enomoto ◽  
...  
Keyword(s):  
Glutamic Acid ◽  
Polyacrylamide Gel Electrophoresis ◽  
Sodium Dodecyl ◽  
Mass Spectrometry Analysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Game Meat ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Game meat has been underutilized, while it offers the potential to diversify not only the human diet but also increase food production and the nutritional value of meat products. This study aimed to determine the angiotensin I-converting enzyme (ACE) inhibitory activities of the digested game meats (venison and boar meat) compared with those of livestock meats (beef and pork). Through the sodium dodecyl sulfate polyacrylamide gel electrophoresis and size chromatography results, we found that the digested products from each meat had different molecular weights. The ACE inhibitory ratio in all tested samples had gradually increased following by the enzyme treatments. ACE inhibitory ratios and the half maximal inhibitory concentration values indicated that digested venison was the most potent inhibitor of ACE activity, followed by the digested boar meat. The level of anserine in digested venison was higher than that in the other meats, but the carnosine level was lower. Through fractionations and liquid chromatography–tandem mass spectrometry analysis, five ACE inhibitory peptides were identified from the digested venison. Of these peptides, Isoleucine-Lysine- Glutamic Acid-Valine-Threonine-Glutamic Acid-Arginine (IKEVTER) demonstrated the highest ACE inhibitory activity. Therefore, the game meat is food that is believed potentially to offer high bioactivities, particularly antihypertensive forces.

scholarly journals Angiotensin I Converting Enzyme Inhibitory Peptides Obtained afterIn VitroHydrolysis of Pea (Pisum sativumvar. Bajka) Globulins

2014 ◽  
Vol 2014 ◽  
pp. 1-8 ◽  
Author(s):  
Anna Jakubczyk ◽  
Barbara Baraniak
Keyword(s):  
Inhibitory Activity ◽  
Deae Cellulose ◽  
Degree Of Hydrolysis ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory Peptides ◽  
Ace Inhibitory

Pea seeds represent a valuable source of active compounds that may positively influence health. In this study, the pea globulins were digestedin vitrounder gastrointestinal condition and potentially bioaccessible angiotensin I converting enzyme (ACE) inhibitory peptides were identified. The degree of hydrolysis after pepsin, 14.42%, and pancreatin, 30.65%, were noted. The peptides with the highest ACE inhibitory properties were separated using ion exchange chromatography on DEAE-cellulose. Thirteen peptides fractions were obtained but only four showed potential antihypertensive properties. The highest inhibitory activity was determined for the fraction F8 (IC50 = 0.0014 mg/mL). This fraction was separated on Sephadex G10 and two peptide fractions were obtained. The peptides fraction (B) with the highest ACE inhibitory activity (IC50 = 0.073 mg/mL) was identified by ESI-MS/MS. The sequences of ACE inhibitory peptides were GGSGNY, DLKLP, GSSDNR, MRDLK, and HNTPSR. Based on Lineweaver-Burk plots for the fraction B, the kinetic parameters asKm,Vmax, andKiand mode of inhibition were determined. This fraction belongs to uncompetitive inhibitor of ACE activity. The seeds of pea are the source of precursor protein, which releases the ACE inhibitory peptides as a result of enzymatic hydrolysis.

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.

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
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