Purification and identification of a novel ACE inhibitory peptide from marine alga Gracilariopsis lemaneiformis protein hydrolysate

Cao, Dequn; Lv, Xiaojing; Xu, Xiaoting; Yu, Haiyang; Sun, Xue; Xu, Nianjun

doi:10.1007/s00217-017-2886-2

Cited by 65 publications

(42 citation statements)

References 51 publications

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“…As shown in Figure 3b, the fraction with one single peak, named FII-2-P, was obtained with the purity of 95%, and the ACE inhibitory IC 50 value of 46.7 μg/mL. The IC 50 value of FII-2-P from cottonseed protein was found to be lower than other food protein hydrolysates like yeast (420 µg/mL), [37] algal (255 µg/mL), [38] and small red bean (67.2 µg/mL), [39] but was higher than those of chlorella (15 µg/mL), [40] fresh chickpeas (0.039 µg/mL and 0.307 µg/mL, respectively) [41] and hard-to-cook bean (2.7 µg/mL). [42] Thus, FII-2-P (46.7 μg/mL) could be a potential ACE inhibitor to be used in the development of functional foods.…”

Section: Purification Of the Ace Inhibitory Peptidesmentioning

confidence: 98%

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

Gao

Zhang²,

Ma³

et al. 2019

International Journal of Food Properties

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Peptides derived from food proteins have exhibited significant antihypertensive effects without side effects. In this study, the cottonseed protein was hydrolyzed by papain for preparing peptide with angiotensin I converting enzyme (ACE) inhibitory activity. The influence of hydrolysis temperature (33°C, 40°C, and 47°C), pH (6.5, 7.0, and 7.5), and enzyme to substrate (E/S) ratio (0.9%, 1.2%, and 1.5%) on the degree of hydrolysis (DH) and ACE-inhibitory activity were analyzed. The hydrolysis conditions were further optimized by central composite design (CCD) and response surface methodology (RSM). The DH of cottonseed protein and ACE inhibitory rate of hydrolysates reached 25.7% and 88.2%, respectively, under the optimal hydrolysis conditions (hydrolysis temperature 39°C, pH 7.5, and E/S ratio 1.04%). We further separated the cottonseed protein hydrolysates (CPH) using a combined strategy of ultrafiltration membrane bioreactor system, sephadex G-25 gel filtration chromatography and reversed-phase high-performance liquid chromatography (RP-HPLC). An ACE inhibitory peptide, named as FII-2-P, with ACE inhibitory IC 50 value of 46.7 μg/mL, was obtained. MALDI-TOF-TOF mass spectrometry analysis revealed that the molecular weight of FII-2-P was 763.4 Da and its amino acids sequence was Phe-Pro-Ala-Ile-Gly-Met-Lys. These results demonstrated that the cottonseed protein is a potential source of ACE inhibitory ingredients to be used in the development of functional foods.

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Section: Purification Of the Ace Inhibitory Peptidesmentioning

confidence: 98%

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

Gao

Zhang²,

Ma³

et al. 2019

International Journal of Food Properties

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“…Peptides can bind to the active site of the angiotensin-I converting enzyme, thereby reducing blood pressure. For example, peptides extracted from Gracilariopsis lemaneiformis had potent ACEinhibitory activity in vitro (Cao et al 2017). Compounds such as sulphated polysaccharides, from Ulva prolifera (as Enteromorpha) reduce hyperlipidaemia in animal modelsone of the principle causes of heart disease (Ren et al 2017(Ren et al , 2018.…”

Section: Hypertension and Cardiac Diseasementioning

confidence: 99%

Seaweeds as nutraceuticals for health and nutrition

2019

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Throughout human history, seaweeds have been used as food, folk remedies, dyes, and mineral-rich fertilisers. Seaweeds as nutraceuticals or functional foods with dietary benefits beyond their fundamental macronutrient content, are now a major research and industrial development concept. The occurrence of dietary and lifestyle-related diseases, notably type 2 diabetes, obesity, cancer, and metabolic syndrome has become a health epidemic in developed countries. Global epidemiological studies have shown that countries where seaweed is consumed on a regular basis have significantly fewer instances of obesity and dietary-related disease. This review outlines recent developments in seaweed applications for human health from an epidemiological perspective and as a functional food ingredient.

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“…D.Q. Cao et al have reported that a peptide (QVEY, IC50 = 474.36 μM) isolated from trypsin hydrolyzate of G. lemaneiformis had ACE inhibitory activity [ 31 ]. FQIN [M(O)] CILR (IC50 = 9.64 ± 0.36 μM) and TGAPCR (IC50 = 23.94 ± 0.82 μM) were also screened from trypsin hydrolyzate of G. lemaneiformis , but the two peptides have lower IC50 values than the ACE inhibitory peptide reported above.…”

Section: Discussionmentioning

confidence: 99%

Antihypertensive Effects of Two Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Gracilariopsis lemaneiformis (Rhodophyta) in Spontaneously Hypertensive Rats (SHRs)

et al. 2018

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A variety of biologically active products have been isolated from Gracilariopsis lemaneiformis. In the present study, two novel angiotensin-converting enzyme (ACE) inhibitory peptides, FQIN [M(O)] CILR, and TGAPCR, were screened and identified from G. lemaneiformis protein hydrolysates by LC-MS/MS. The IC50 values of FQIN [M(O)] CILR and TGAPCR were 9.64 ± 0.36 μM and 23.94 ± 0.82 μM, respectively. In the stability study, both peptides showed stabilities of pH, temperature, simulated gastrointestinal digestion, and ACE hydrolysis. The Lineweaver–Burk plot showed that the two peptides were noncompetitive inhibitors of ACE. Molecular docking simulated the intermolecular interactions of two peptides and ACE, and the two peptides formed hydrogen bonds with the active pockets of ACE. However, FQIN [M(O)] CILR was more closely linked to the active pockets of ACE, thereby exerting better ACE inhibition. Spontaneously hypertensive rats (SHRs) were studied with an oral dose of 10 mg/kg body weight. Both peptides reduced systolic blood pressure (SBP) and diastolic blood pressure (DBP) in SHRs, of which FQIN [M(O)] CILR was able to reduce the systolic blood pressure by 34 mmHg (SBP) (p < 0.05). Therefore, FQIN [M(O)] CILR was an excellent ACE inhibitory peptide.

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Purification and identification of a novel ACE inhibitory peptide from marine alga Gracilariopsis lemaneiformis protein hydrolysate

Cited by 65 publications

References 51 publications

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

Isolation and identification of the angiotensin-I converting enzyme (ACE) inhibitory peptides derived from cottonseed protein: optimization of hydrolysis conditions

Seaweeds as nutraceuticals for health and nutrition

Antihypertensive Effects of Two Novel Angiotensin I-Converting Enzyme (ACE) Inhibitory Peptides from Gracilariopsis lemaneiformis (Rhodophyta) in Spontaneously Hypertensive Rats (SHRs)

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