Comparative Study of Angiotensin I-Converting Enzyme (ACE) Inhibition of Soy Foods as Affected by Processing Methods and Protein Isolation

Angiotensin converting enzyme (ACE) converts angiotensin I into the vasoconstrictor angiotensin II and eventually elevates blood pressure. High blood pressure is a major risk factor for heart disease and stroke. Studies show peptides present anti-hypertensive activity by ACE inhibition. During food processing and digestion, food proteins may be hydrolyzed and release peptides. Our objective was to determine and compare the ACE inhibitory potential of fermented and non-fermented soy foods and isolated 7S and 11S protein fractions. Soy foods (e.g., soybean, natto, tempeh, yogurt, soymilk, tofu, soy-sprouts) and isolated proteins were in vitro digested prior to the determination of ACE inhibitory activity. Peptide molecular weight distribution in digested samples was analyzed and correlated with ACE inhibitory capacity. Raw and cooked soymilk showed the highest ACE inhibitory potential. Bacteria-fermented soy foods had higher ACE inhibitory activity than fungus-fermented soy food, and 3 day germinated sprouts had higher ACE inhibition than those germinated for 5 and 7 days. The 11S hydrolysates showed higher ACE inhibitory capacity than 7S. Peptides of 1–4.5 kDa showed a higher contribution to reducing IC50. This study provides evidence that soy foods and isolated 7S and 11S proteins may be used as functional foods or ingredients to prevent or control hypertension.

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Effect ofJatropha curcasPeptide Fractions on the Angiotensin I-Converting Enzyme Inhibitory Activity

BioMed Research International ◽

10.1155/2013/541947 ◽

2013 ◽

Vol 2013 ◽

pp. 1-8 ◽

Cited By ~ 4

Author(s):

Maira R. Segura-Campos ◽

Fanny Peralta-González ◽

Arturo Castellanos-Ruelas ◽

Luis A. Chel-Guerrero ◽

David A. Betancur-Ancona

Keyword(s):

Inhibitory Activity ◽

Protein Hydrolysate ◽

Gel Filtration ◽

Ace Inhibition ◽

Degree Of Hydrolysis ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

Hypertension is one of the most common worldwide diseases in humans. Angiotensin I-converting enzyme (ACE) plays an important role in regulating blood pressure and hypertension. An evaluation was done on the effect of Alcalase hydrolysis of defattedJatropha curcaskernel meal on ACE inhibitory activity in the resulting hydrolysate and its purified fractions. Alcalase exhibited broad specificity and produced a protein hydrolysate with a 21.35% degree of hydrolysis and 34.87% ACE inhibition. Ultrafiltration of the hydrolysate produced peptide fractions with increased biological activity (24.46–61.41%). Hydrophobic residues contributed substantially to the peptides’ inhibitory potency. The 5–10 and <1 kDa fractions were selected for further fractionation by gel filtration chromatography. ACE inhibitory activity (%) ranged from 22.66 to 45.96% with the 5–10 kDa ultrafiltered fraction and from 36.91 to 55.83% with the <1 kDa ultrafiltered fraction. The highest ACE inhibitory activity was observed inF2 ( μg/mL) from the 5–10 kDa fraction andF1 ( μg/mL) from the <1 kDa fraction. ACE inhibitory fractions fromJatrophakernel have potential applications in alternative hypertension therapies, adding a new application for theJatrophaplant protein fraction and improving the financial viability and sustainability of a Jatropha-based biodiesel industry.

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A Novel Angiotensin-I-Converting Enzyme (ACE) Inhibitory Peptide from Takifugu flavidus

Marine Drugs ◽

10.3390/md19120651 ◽

2021 ◽

Vol 19 (12) ◽

pp. 651

Author(s):

Yongchang Su ◽

Shicheng Chen ◽

Shuilin Cai ◽

Shuji Liu ◽

Nan Pan ◽

...

Keyword(s):

Blood Pressure ◽

Inhibitory Activity ◽

Gel Chromatography ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Inhibitory Peptide ◽

Ace Inhibitory Peptide ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

Alcalase, neutral protease, and pepsin were used to hydrolyze the skin of Takifugu flavidus. The T. flavidus hydrolysates (TFHs) with the maximum degree of hydrolysis (DH) and angiotensin-I-converting enzyme (ACE)-inhibitory activity were selected and then ultra-filtered to obtain fractions with components of different molecular weights (MWs) (<1, 1–3, 3–10, 10–50, and >50 kDa). The components with MWs < 1 kDa showed the strongest ACE-inhibitory activity with a half-maximal inhibitory concentration (IC50) of 0.58 mg/mL. Purification and identification using semi-preparative liquid chromatography, Sephadex G-15 gel chromatography, RP-HPLC, and LC–MS/MS yielded one new potential ACE-inhibitory peptide, PPLLFAAL (non-competitive suppression mode; IC50 of 28 μmmol·L−1). Molecular docking and molecular dynamics simulations indicated that the peptides should bind well to ACE and interact with amino acid residues and the zinc ion at the ACE active site. Furthermore, a short-term assay of antihypertensive activity in spontaneously hypertensive rats (SHRs) revealed that PPLLFAAL could significantly decrease the systolic blood pressure (SBP) and diastolic blood pressure (DBP) of SHRs after intravenous administration. These results suggested that PPLLFAAL may have potential applications in functional foods or pharmaceuticals as an antihypertensive agent.

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Angiotensin I-Converting Enzyme (ACE) Inhibitory Activity of Elk (Cervus elaphus) Velvet Antler

Preventive Nutrition and Food Science ◽

10.3746/jfn.2005.10.3.239 ◽

2005 ◽

Vol 10 (3) ◽

pp. 239-243 ◽

Cited By ~ 3

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

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Angiotensin I Converting Enzyme (ACE) inhibitory activity and antihypertensive effects of grass carp peptides

Food Science and Biotechnology ◽

10.1007/s10068-014-0226-x ◽

2014 ◽

Vol 23 (5) ◽

pp. 1661-1666 ◽

Cited By ~ 2

Author(s):

Shen Wang ◽

Li-mei Lin ◽

Yong-ning Wu ◽

Min Fang ◽

Ya-qin Yu ◽

...

Keyword(s):

Inhibitory Activity ◽

Grass Carp ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory

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Effect of Different Proteases on the Degree of Hydrolysis and Angiotensin I-Converting Enzyme-Inhibitory Activity in Goat and Cow Milk

Biomolecules ◽

10.3390/biom8040101 ◽

2018 ◽

Vol 8 (4) ◽

pp. 101 ◽

Cited By ~ 7

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.

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