scholarly journals Purification and Identification of Angiotensin I-Converting Enzyme Inhibitory Peptides and the Antihypertensive Effect of Chlorella sorokiniana Protein Hydrolysates

Nutrients ◽  
2018 ◽  
Vol 10 (10) ◽  
pp. 1397 ◽  
Author(s):  
Yu-Hsin Lin ◽  
Guan-Wen Chen ◽  
Chin Yeh ◽  
Helena Song ◽  
Jenn-Shou Tsai

Hot water was used to obtain Chlorella sorokiniana hot water extract (HWE). Subsequently, this byproduct was freeze-dried, hydrolysed at 50 °C using Protease N to obtain C. sorokiniana protein hydrolysates (PN-1), and then digested with a gastrointestinal enzyme (PN-1G). The inhibitory effects of the HWE and hydrolysates against angiotensin I-converting enzyme (ACE) were investigated. The soluble protein and peptide contents were 379.9 and 179.7 mg/g, respectively, for HWE and 574.8 and 332.8 mg/g, respectively, for PN-1. The IC50 values of the HWE, PN-1, and PN-1G on ACE were 1.070, 0.035, and 0.044 mg/mL, respectively. PN-1G was separated into seven fractions through size exclusion chromatography. The sixth fraction of the hydrolysate had a molecular weight between 270 and 340 Da, and the lowest IC50 value on ACE was 0.015 mg/mL. The amino acid sequences of the ACE-inhibitory peptides were Trp-Val, Val-Trp, Ile-Trp, and Leu-Trp, of which the IC50 values were 307.61, 0.58, 0.50, and 1.11 µΜ, respectively. Systolic blood pressure and diastolic blood pressure were reduced 20 and 21 mm Hg, respectively, in spontaneously hypertensive rats after 6 h of oral administration with a dose of 171.4 mg PN-1 powder/kg body weight.

2004 ◽  
Vol 92 (3) ◽  
pp. 357-366 ◽  
Author(s):  
Vanessa Vermeirssen ◽  
John Van Camp ◽  
Willy Verstraete

Hypertension or high blood pressure is a significant health problem worldwide. Bioactive peptides that inhibit angiotensin I converting enzyme (ACE) in the cardiovascular system can contribute to the prevention and treatment of hypertension. These ACE inhibitory peptides are derived from many food proteins, especially milk proteins. An ACE inhibitory activity in vitro does not always imply an antihypertensive effect in vivo. Even if it does, it is very difficult to establish a direct relationship between in vitro and in vivo activity. This is mainly due to the bioavailability of the ACE inhibitory peptides after oral administration and the fact that peptides may influence blood pressure by mechanisms other than ACE inhibition. To exert an antihypertensive effect after oral ingestion, ACE inhibitory peptides have to reach the cardiovascular system in an active form. Therefore, they need to remain active during digestion by human proteases and be transported through the intestinal wall into the blood. The bioavailability of some ACE inhibitory peptides has been studied. It is also known that (hydroxy)proline-containing peptides are generally resistant to degradation by digestive enzymes. Peptides can be absorbed intact through the intestine by paracellular and transcellular routes, but the potency of the bioactivity after absorption is inversely correlated to chain length. In addition, some strategies are proposed to increase the bioavailability of ACE inhibitory peptides. Further research into the bioavailability of ACE inhibitory peptides will lead to the development of more effective ACE inhibitory peptides and foods.


2016 ◽  
Vol 12 (4) ◽  
pp. 333-342 ◽  
Author(s):  
Hongyang Wu ◽  
Tailing Jiang ◽  
Xiaohua Dong ◽  
Guanghui Shen ◽  
Shanshan Li ◽  
...  

Abstract Prickly ash (Zanthoxylum bungeanum Maxim) seed protein was hydrolyzed with papain to obtain hydrolysates with inhibitory activity against angiotensin-I converting enzyme (ACE). ACE inhibitory peptides (ACEIPs) were successfully purified from seed protein hydrolysates through ultrafiltration and gel chromatography. In vitro ACE inhibitory assay revealed an IC50 value of 0.032± 0.008 mg·mL−1 for a component with <5 kDa molecular weight. Four fractions were isolated by Sephadex G-25 gel chromatography under the following elution conditions: flow rate, 0.6 mL·min−1; initial volume, 2.0 mL; and sample concentration, 30 mg·mL−1. The second fraction showed the highest inhibitory activity with an IC50 value of 0.021±0.007 mg·mL−1. The stability of the ACE inhibitory activity of the obtained ACEIPs was identified under storage conditions with varied temperature, pH, and gastrointestinal protease digestion. Peptides derived from prickly ash seed protein hydrolysates may be a potential resource for exploring functional food or pharmaceuticals against hypertension.


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