Towards a continuous adsorption process for the enrichment of ACE-inhibiting peptides from food protein hydrolysates

Hippauf, Felix; Huettner, Christiane; Lunow, Diana; Borchardt, Lars; Henle, Thomas; Kaskel, Stefan

doi:10.1016/j.carbon.2016.05.062

Cited by 23 publications

(14 citation statements)

References 33 publications

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“…The important role of angiotensin I-converting enzyme (ACE) in increasing blood pressure has been demonstrated in the past decades, as about 9.4 million patients die from hypertension worldwide every year and 1.6 billion people are suffering from high blood pressure [1]. Reducing blood pressure to normal levels is crucial, and thus more attention has been focused on the effects of ACE-inhibitory substances.…”

Section: Introductionmentioning

confidence: 99%

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

2020

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Sargassum maclurei is a potential protein resource because of its high protein content and relatively balanced amino acid composition. To promote its usage in food, medical, or other industries, S. maclurei protein was hydrolyzed by pepsin and papain to obtain bioactive peptides. The S. maclurei protein hydrolysates (SMPHs) were purified using gel chromatography and reversed-phase high performance liquid chromatography (RP-HPLC), and 12 major fractions were obtained. The fraction D11 with the highest angiotensin I-converting enzyme (ACE) inhibition (61.59%, at 1 mg/mL) was subjected to liquid chromatography-mass spectrometry (LC-MS/MS) analysis, and about 17 peptides were identified, of which the RWDISQPY (1063.5 Da) was chosen to be synthesized based on in silico analysis. The RWDISQPY demonstrated high ACE inhibition ability (IC 50 : 72.24 µM) with competitive inhibition mode, and could effectively (p < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 150 mg/kg body weight. The results of the molecular docking simulation demonstrated that RWDISQPY could bind with the active sites S1 and S2 of ACE via short hydrogen bonds. Moreover, RWDISQPY showed acceptable endothelin-1 suppressing capacity (26.21% at 1.5 mg/mL). These results indicate that S. maclurei could be developed into functional foods such as antihypertensive products.

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Section: Introductionmentioning

confidence: 99%

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

2020

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“…It was declared that the number of people suffering from high blood pressure will reach to 1.6 billion in 2025 in the world, and hypertension was responsible to about 9.4 million deaths worldwide every year (Hippauf et al., 2016). Reduce blood pressure to normal level is crucial and control and improvement of diet would be the easiest option to achieve a desirable blood pressure‐lowering effect (Lee & Hur, 2017).…”

Section: Introductionmentioning

confidence: 99%

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Zheng

Wang

Zhuang

et al. 2020

Journal of Food Science

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Naked oat globulin was hydrolyzed by alcalase, flavourzyme, pepsin, and trypsin in sequence. The hydrolysates (NOGH) were purified using gel chromatography, reversed-phase high performance liquid chromatography (RP-HPLC). Finally, fraction D7d with the highest ACE-inhibitory was subjected to liquid chromatography-mass spectrometry analysis and 14 peptides were identified. Of which, peptide SSYYPFK (890.4 Da) was chose to synthesize based on in silico analysis. The SSYYPFK demonstrated high ACE-inhibitory activity (IC 50 : 91.82 µM) with competitive inhibition mode, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats at the concentration of 100 to 150 mg/kg body weight. Molecular docking simulation demonstrated that SSYYPFK could bind with the active site S1 of ACE via short hydrogen bonds. It could remain the ACE-inhibitory activity after simulated gastrointestinal hydrolysis. Moreover, SSYYPFK showed acceptable renin and endothelin-1 suppressing capacity (47.59% and 27.88% at 1.5 mg/mL, respectively). These results indicated that SSYYPFK may have similar antihypertensive mechanism with captopril, and could be develop to natural antihypertensive products.Practical Application: One novel ACE-inhibitory peptide SSYYPFK (890.4 Da) was identified from naked oat globulin hydrolysates. It exhibited relatively high renin and intracellular endothelin-1 suppressing capacity, and could effectively (P < 0.05) lower the systolic blood pressure and diastolic pressure of spontaneously hypertensive rats. This peptide could be used as natural and safe nutraceuticals and/or functional ingredients.Additional supporting information may be found online in the Supporting Information section at the end of the article. Supplementary Table S1. Body weight (g) of the spontaneous hypertensive rats administrated with peptide SSYYPFK a Supplementary Table S2. Heart rate of the spontaneous hypertensive rats administrated with peptide SSYYPFK a

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“…Hypertension is a well-established risk factor for many problems like cardiovascular diseases, chronic kidney diseases, arteriosclerosis, and stroke [1]. The number of adults suffering from hypertension is estimated to increase to 1.6 billion worldwide by 2025 [2]. Angiotensin I converting enzyme (ACE) is regarded a crucial enzyme in regulating blood pressure by promoting the conversion of angiotensin I to angiotensin II in the circulatory or endocrine of human renin-angiotensin system [3,4].…”

Section: Introductionmentioning

confidence: 99%

Purification, Characterization and Evaluation of Inhibitory Mechanism of ACE Inhibitory Peptides from Pearl Oyster (Pinctada fucata martensii) Meat Protein Hydrolysate

et al. 2019

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Angiotensin-I-converting enzyme (ACE) inhibitory peptides derived from natural products have shown a blood pressure lowering effect with no side effects. In this study, two novel ACE inhibitory peptides (His-Leu-His-Thr, HLHT and Gly-Trp-Ala, GWA) were purified from pearl oyster (Pinctada fucata martensii) meat protein hydrolysate with alkaline protease by ultrafiltration, polyethylene glycol methyl ether modified immobilized metal ion affinity medium, and reverse-phase high performance liquid chromatography. Both peptides exhibited high ACE inhibitory activity with IC50 values of 458.06 ± 3.24 μM and 109.25 ± 1.45 μM, respectively. Based on the results of a Lineweaver-Burk plot, HLHT and GWA were found to be non-competitive inhibitor and competitive inhibitor respectively, which were confirmed by molecular docking. Furthermore, the pearl oyster meat protein hydrolysate exhibited an effective antihypertensive effect on SD rats. These results conclude that pearl oyster meat protein is a potential resource of ACE inhibitory peptides and the purified peptides, HLHT and GWA, can be exploited as functional food ingredients against hypertension.

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Towards a continuous adsorption process for the enrichment of ACE-inhibiting peptides from food protein hydrolysates

Cited by 23 publications

References 33 publications

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

Efficacy of a Novel ACE-Inhibitory Peptide from Sargassum maclurei in Hypertension and Reduction of Intracellular Endothelin-1

Isolation of novel ACE‐inhibitory peptide from naked oat globulin hydrolysates in silico approach: Molecular docking, in vivo antihypertension and effects on renin and intracellular endothelin‐1

Purification, Characterization and Evaluation of Inhibitory Mechanism of ACE Inhibitory Peptides from Pearl Oyster (Pinctada fucata martensii) Meat Protein Hydrolysate

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