scholarly journals Angiotensin Converting Enzyme Inhibitory and Antioxidant Activities of Enzymatic Hydrolysates of Korean Native Cattle (Hanwoo) Myofibrillar Protein

2017 ◽  
Vol 2017 ◽  
pp. 1-9 ◽  
Author(s):  
Seung Yun Lee ◽  
Sun Jin Hur
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Antioxidant Activities ◽  
Radical Scavenging ◽  
Myofibrillar Protein ◽  
Raw 264.7 Cells ◽  
Converting Enzyme ◽  
Molecular Weights ◽  
Native Cattle ◽  
Ace Inhibitory

The purpose of this study was to determine the angiotensin converting enzyme (ACE) inhibitory and antioxidant activities of myofibrillar protein hydrolysates (HMPHs) of different molecular weights (<3 and <10 kDa) derived from Korean native cattle (Hanwoo breed) using a commercially available and inexpensive enzyme (Alkaline-AK). HMPH of both tested molecular weights had ACE inhibitory activity. Among the antioxidant activities, iron chelation and nitrite scavenging activities were higher in low-molecular-weight peptide of HMPH (<3 kDa), whereas 2,2-diphenyl-1-picrylhydrazyl (DPPH) radical scavenging activity was higher in high-molecular-weight peptide of HMPH (<10 kDa). HMPH did not induce cytotoxicity in RAW 264.7 cells at concentrations of 5–20 mg/mL. These results indicate that HMPH can be cheaply produced using Alkaline-AK and applied as a potential ACE inhibitor and antioxidant.

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 The Potential of Hydrolysate from Rabbit Meat Protein as an Angiotensin Converting Enzyme Inhibitor

2019 ◽  
Vol 43 (1) ◽  
Author(s):  
Edy Permadi ◽  
Jamhari Jamhari ◽  
Edi Suryanto ◽  
Zaenal Bachruddin ◽  
Yuny Erwanto
Keyword(s):  
Molecular Weight ◽  
Angiotensin Converting Enzyme ◽  
Soluble Protein ◽  
Ace Inhibitor ◽  
Water Soluble ◽  
Converting Enzyme ◽  
Soluble Protein Content ◽  
Water Soluble Protein ◽  
Rabbit Meat ◽  
Ace Inhibitory

This research aimed to investigate the rabbit meat hydrolysate potential as an angiotensin-converting enzyme (ACE) inhibitor. Indonesian local rabbit meats were used in this study. The research was conducted in Department of Animal Product Technology, Faculty of Animal Science, Universitas Gadjah Mada, from August 2016 to February 2017. The local rabbit meats were hydrolyzed by pepsin, trypsin, and pancreatic. The obtained hydrolysates were then analyzed to identify the water-soluble protein content. The molecular weight of the hydrolysates were also confirmed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). The ACE inhibitory properties of the hydrolysates were analyzed in vitro. The results showed that pepsin, trypsin, and pancreatic hydrolysis showed a significant effect on the water-soluble protein content of rabbit meat (p<0.05). The water-soluble protein of rabbit meat hydrolysed by pepsin, trypsin, and pancreatic were 9.41, 7.66, and 9.75 mg/mL respectively. The molecular weight of the rabbit meat hydrolysate were increased from 10 to 43 kDa; 17 to 43 kDa; and 10 to 43 kDa, after hydrolysed by by pepsin, trypsin, and pancreatic respectively. Furthermore, the ACE inhibitory properties ) of the hydrolysed rabbit meat by pepsin, trypsin, and pancreatic were 439, 170, and 380 μg/mL, respectively. The rabbit meat hydrolysate showed a potential to be ACE inhibitor after hydrolyzed with pepsin, trypsin and pancreatic. Moreover, it also showed a promising potential to be used as bioactive components in different pharmaceutical applications. The highest ACE inhibitory capability was showed on trypsin hydrolysis with the total of 65.45% and 170 μg/mL ACE inhibition

scholarly journals Extraction of Collagen from the Skin of Kacang Goat and Production of Its Hydrolysate as an Inhibitor of Angiotensin Converting Enzyme

2021 ◽  
Vol 44 (2) ◽  
pp. 222-228
Author(s):  
T. R. Hakim ◽  
A. Pratiwi ◽  
Jamhari Jamhari ◽  
N. A. Fitriyanto ◽  
Rusman Rusman ◽  
...  
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Dry Matter ◽  
Ace Inhibition ◽  
Converting Enzyme ◽  
Inhibition Activity ◽  
Collagen Hydrolysate ◽  
Molecular Weights ◽  
Ic50 Value ◽  
Inhibitory Potential ◽  
Ace Inhibitory

The study was designed to determine the potential of collagen hydrolysate produced from the skin of Kacang goat through chymotrypsin hydrolysis to be used as an inhibitor of angiotensin converting enzyme (ACE). This research was conducted in three replications, with the measured parameters include ACE inhibitory potential and collagen hydrolysate fractionation. The results showed that collagen extraction of Kacang goat skin by chymotrypsin hydrolysis yielded 9.74% (dry matter, v/v) collagen, with pH at 6.6. The extracted collagen contained α1, α2, and β collagen chains with molecular weights of 151 kDa, 141 kDa, and 240 kDa, respectively. Furthermore, the collagen hydrolysis produced protein peptides confirmed at molecular weights of 43 to 107 kDa. The hydrolysate fractionation at molecular weights of <3 kDa, 3-5 kDa, and >5 kDa showed proteins concentrations of 2.33 mg/mL, 3.81 mg/mL, and 3.93 mg/mL, respectively. The hydrolysate fractionation with molecular weight <3 kDa showed to have ACE inhibition activity with the IC50 value of 0.47 mg/mL. The study concluded that collagen hydrolysate extracted from the skin of Kacang goat had a promising potential as a source of antihypertensive agent.

scholarly journals Antioxidant and Angiotensin-Converting Enzyme (ACE) Inhibitory Activities of Yogurt Supplemented with Lactiplantibacillus plantarum NK181 and Lactobacillus delbrueckii KU200171 and Sensory Evaluation

Foods ◽  
2021 ◽  
Vol 10 (10) ◽  
pp. 2324
Author(s):  
Eun-Deok Kim ◽  
Hyun-Sook Lee ◽  
Kee-Tae Kim ◽  
Hyun-Dong Paik
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Sensory Evaluation ◽  
Antioxidant Activities ◽  
Reference Group ◽  
Lactobacillus Delbrueckii ◽  
Control Group ◽  
Converting Enzyme ◽  
Freeze Dried ◽  
Significant Difference ◽  
Ace Inhibitory

This study was carried out to develop a functional yogurt with inhibitory effects on angiotensin-converting enzyme (ACE) and antioxidant activity using various probiotic strains. Yogurts were prepared using a commercial LAB freeze-dried product and probiotics.Yogurt with only commercial LAB product as control group (C) and probiotics supplemented with Lacticaseibacillus rhamnosus GG KCTC 12202 BP, as a reference group (T1), Lactiplantibacillus plantarum KU15003 (T2), Lactiplantibacillus plantarum KU15031 (T3), Lactiplantibacillus plantarum NK181 (T4), and Lactobacillus delbrueckii KU200171 (T5). The T5 sample showed high antioxidant activities (86.5 ± 0.3% and 39.3 ± 1.0% in DPPH and ABTS assays, respectively). The T4 sample had the highest ACE inhibitory activity (51.3 ± 10.3%). In the case of sensory evaluation, the T4 and T5 samples did not show a significant difference (p > 0.05) compared to the reference group. These results suggest that L. plantarum NK181 and L. delbrueckii KU200171 can be used in the food industry especially dairy to improve health benefits for hypertensive patients.

scholarly journals Angiotensin-converting enzyme (ACE) inhibitory activity of Solanum torvum and isolation of a novel methyl salicylate glycoside

2014 ◽  
Vol 11 ◽  
pp. 557-562 ◽  
Author(s):  
Arunee Simaratanamongkol ◽  
Kaoru Umehara ◽  
Hiroki Niki ◽  
Hiroshi Noguchi ◽  
Pharkphoom Panichayupakaranant
Keyword(s):  
Angiotensin Converting Enzyme ◽  
Inhibitory Activity ◽  
Methyl Salicylate ◽  
Converting Enzyme ◽  
Ace Inhibitory Activity ◽  
Solanum Torvum ◽  
Ace Inhibitory

scholarly journals ANGIOTENSIN CONVERTING ENZYME INHIBITORY ACTIVITY OF MELINJO (GNETUM GNEMON L.) SEED EXTRACTS AND MOLECULAR DOCKING OF ITS STILBENE CONSTITUENTS

2017 ◽  
Vol 10 (3) ◽  
pp. 243
Author(s):  
Abdul Mun'im ◽  
Muhammad Ashar Munadhil ◽  
Nuraini Puspitasari ◽  
Azminah . ◽  
Arry Yanuar
Keyword(s):  
Molecular Docking ◽  
Angiotensin Converting Enzyme ◽  
Ethyl Acetate ◽  
Inhibitory Activity ◽  
Phenolic Content ◽  
Ethyl Acetate Extract ◽  
Total Phenolic ◽  
Converting Enzyme ◽  
Gnetum Gnemon ◽  
Ace Inhibitory

ABSTRACTObjectives: To evaluate the angiotensin converting enzyme (ACE) inhibitory activity of melinjo (Gnetum gnemon) seed extract and to study moleculardocking of stilbene contained in melinjo seeds.Methods: Melinjo seed powders were extracted with n-hexane, dichloromethane, ethyl acetate, methanol, and water successively. The extracts wereevaluated ACE inhibitory activities using ACE kit-Wist and the phenolic content using Folin–Ciocalteu method. The extract demonstrated the highestACE inhibitory activity was subjected to liquid chromatography-mass spectrometry (LC-MS) to know its stilbene constituent. The stilbene constituentsin melinjo seed were performed molecular docking using AutoDock Vina, and ligand-receptor Interactions were processed using Ligand Scout.Results: The ethyl acetate extract demonstrated the highest ACE inhibition activity with inhibitory concentration 50% value of 9.77 × 10−8 μg/mLand the highest total phenolic content (575.9 mg gallic acid equivalent/g). Ultra-performance LC-MS analysis of ethyl acetate extract has detected theexistency of resveratrol, gnetin C, ε-viniferin, and gnemonoside A/B. These compounds displayed similar physiochemical properties to lisinopril (ACEinhibitor), as in silico molecular docking studies demonstrated that they fit into the lisinopril receptors.Conclusion: In vitro analysis ethyl acetate extract from melinjo seeds demonstrated the highest ACE inhibitory activity. Molecular docking analysisindicated that resveratrol dimers, gnetin C and gnemonoside A can be considered ACE inhibitor.Keywords: Angiotensin converting enzyme inhibitor, Gnetum gnemon, Melinjo, Total phenolic, Antihypertension, Molecular docking.

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