scholarly journals Angiotensin I-Converting Enzyme Inhibitor Derived from Cross-Linked Oyster Protein

2014 ◽  
Vol 2014 ◽  
pp. 1-9 ◽  
Author(s):  
Cheng-Liang Xie ◽  
Jin-Soo Kim ◽  
Jong-Myung Ha ◽  
Se-Young Choung ◽  
Yeung-Joon Choi
Keyword(s):  
Inhibitory Activity ◽  
Enzyme Inhibitor ◽  
Reversed Phase ◽  
Size Exclusion ◽  
Converting Enzyme ◽  
Spontaneously Hypertensive ◽  
Angiotensin I Converting Enzyme ◽  
Chromatographic Procedure ◽  
Phase Liquid ◽  
Ace Inhibitory

Following cross-linking by microbial transglutaminase, modified oyster proteins were hydrolyzed to improve inhibitory activity against angiotensin-converting enzyme (ACE) inhibitory activity with the use of a single protease, or a combination of six proteases. The oyster hydrolysate with the lowest 50% ACE inhibitory concentration (IC50) of 0.40 mg/mL was obtained by two-step hydrolysis of the cross-linked oyster protein using Protamex and Neutrase. Five ACE inhibitory peptides were purified from the oyster hydrolysate using a multistep chromatographic procedure comprised of ion-exchange, size exclusion, and reversed-phase liquid chromatography. Their sequences were identified as TAY, VK, KY, FYN, and YA, using automated Edman degradation and mass spectrometry. These peptides were synthesized, and their IC50values were measured to be 16.7, 29.0, 51.5, 68.2, and 93.9 μM, respectively. Toxicity of the peptides on the HepG2 cell line was not detected. The oyster hydrolysate also significantly decreased the systolic blood pressure of spontaneously hypertensive rats (SHR). The antihypertensive effect of the oyster hydrolysate on SHR was rapid and long-lasting, compared to commercially obtained sardine hydrolysate. These results suggest that the oyster hydrolysate could be a source of effective nutraceuticals against hypertension.

A novel angiotensin-I converting enzyme inhibitory peptide derived from the glutelin of vinegar soaked black soybean and its antihypertensive effect in spontaneously hypertensive rats

2019 ◽  
Vol 166 (3) ◽  
pp. 223-230 ◽  
Author(s):  
Yueyuan Zhang ◽  
Yanling Zhang ◽  
Peiyao Chen ◽  
Fengjue Shu ◽  
Kai Li ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Spontaneously Hypertensive Rats ◽  
Converting Enzyme ◽  
Hypertensive Rats ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Spontaneously Hypertensive ◽  
Black Soybean ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

AbstractVinegar soaked black soybean is a traditional Chinese food widely used for the treatment of hypertension. While its pharmacodynamic substance was not fully unveiled. It contained abundant glutelin, thus the purpose of this study was to obtain potent antihypertensive peptides from vinegar soaked black soybean. Black soybean was soaked with vinegar and then glutelin was first catalyzed by alcalase. Ultrafiltration, ion exchange chromatography and reversed-phase high performance liquid chromatography were sequentially applied to separate and purify the angiotensin-I converting enzyme (ACE) inhibitory peptides from glutelin hydrolysates. As a result, the fraction L1-4 with the highest ACE inhibitory activity (83.41%) at the final concentration of 0.01 mg/ml was obtained and five peptides were then identified. These peptides were further optimized by virtual screening combining with in silico proteolysis. Finally, a novel tetrapeptide Phe-Gly-Ser-Phe (FGSF) was obtained. FGSF exhibited high in vitro ACE inhibitory activity (IC50 = 117.11 μM) and in vivo hypotensive effect which maximally reduced systolic blood pressure of 21.95 mmHg at 20 mg/kg body weight in spontaneously hypertensive rats. Our study demonstrated that FGSF derived from vinegar soaked black soybean might be used as a promising ingredient for pharmaceuticals against hypertension and its related diseases.

Assessment and Separation of Angiotensin I-Converting Enzyme Inhibitory Peptides in Chinese Soypaste

2015 ◽  
Vol 11 (2) ◽  
pp. 301-305 ◽  
Author(s):  
Fengjuan Li ◽  
Kohji Yamaki ◽  
Yongqiang Cheng ◽  
Yuanyuan Fang
Keyword(s):  
Inhibitory Activity ◽  
Reversed Phase ◽  
Substantial Contribution ◽  
Spectrometric Analysis ◽  
Dependent Manner ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Angiotensin I Converting Enzyme ◽  
Ace Inhibitory

Abstract A Chinese soypaste-derived fraction with potent angiotensin I-converting enzyme (ACE) inhibitory activity (IC50 = 25.9 μg/mL) was obtained by treating soypaste extract with 80% ethanol. The result of gradient reversed-phase high-performance liquid chromatography (RP-HPLC) suggested that bioactive peptides bearing some polarity groups made a substantial contribution to the ACE inhibitory activity. By mass spectrometric analysis, a component was separated as Glu-Ser-Gly-Asp which was then found to act in a dose-dependent manner against ACE activity as a non-competitive inhibitor, with an IC50 value of 2.297 mM.

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

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 Isolation and evaluation of two angiotensin-I-converting enzyme inhibitory peptides from fermented grains (Jiupei) used in Chinese Baijiu production

RSC Advances ◽  
2018 ◽  
Vol 8 (65) ◽  
pp. 37451-37461 ◽  
Author(s):  
Limo Zhang ◽  
Yunsong Jiang ◽  
Zhongtian Yin ◽  
Jinyuan Sun ◽  
Hehe Li ◽  
...  
Keyword(s):  
Inhibitory Activity ◽  
Raw Material ◽  
Converting Enzyme ◽  
Angiotensin I ◽  
Ace Inhibitory Activity ◽  
Inhibitory Peptides ◽  
Angiotensin I Converting Enzyme ◽  
Fermented Grains ◽  
Ace Inhibitory

Two tripeptides with ACE inhibitory activity were isolated from Jiupei (the raw material of Baijiu) distillation.

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