Antihypertensive effect of an angiotensin converting enzyme inhibitory peptide from enzyme modified cheese

Two angiotensin converting enzyme (ACE)-inhibitory peptides were isolated from enzyme modified cheese (EMC) and their amino acid sequences were identified as Leu-Gln-Pro and Met-Ala-Pro. The EMC was prepared by a combination of Protease N, Umamizyme, and Flavourzyme 500L. Both peptides were derived from β-casein, f 88-90 and f 102-104, respectively. Met-Ala-Pro showed strong ACE inhibitory activity (IC50=0·8 μm) and antihypertensive activity in spontaneously hypertensive rats (SHR) after single oral administration. The IC50 value of Met-Ala-Pro was not affected by pre-incubation with ACE, suggesting that this peptide was a true ACE-inhibitory peptide. We report here, for the first time antihypertensive peptides from EMC.

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Novel Angiotensin-Converting Enzyme Inhibitory Peptides Identified from Walnut Glutelin-1 Hydrolysates: Molecular Interaction, Stability, and Antihypertensive Effects

Nutrients ◽

10.3390/nu14010151 ◽

2021 ◽

Vol 14 (1) ◽

pp. 151

Author(s):

Jing Wang ◽

Guoliang Wang ◽

Yufeng Zhang ◽

Runguang Zhang ◽

Youlin Zhang

Keyword(s):

Angiotensin Converting Enzyme ◽

High Performance ◽

Gel Chromatography ◽

Converting Enzyme ◽

Pressure Balance ◽

Molecular Docking Study ◽

Inhibitory Peptide ◽

Inhibitory Peptides ◽

Ace Inhibitory Peptides ◽

Ace Inhibitory

In recent years, angiotensin-converting enzyme (ACE) inhibitory peptide has become a research hotspot because of its essential role in maintaining human blood pressure balance. In this study, two novel ACE inhibitory peptides of Val-Glu-Arg-Gly-Arg-Arg-lle-Thr-Ser-Val (Valine-Glutamate-Arginine-Glycine-Arginine-Arginine-Isoleucine-Threonine-Serine-Valine, VERGRRITSV) and Phe-Val-Ile-Glu-Pro-Asn-Ile-Thr-Pro-Ala (Phenylalanine-Valine-Isoleucine-Glutamate-Proline-Asparagine-Isoleucine-Threonine-Proline-Alanine, FVIEPNITPA) were isolated and purified from defatted walnut meal hydrolysates through a series of preparation processes including ultrafiltration, Sephadex G-15 gel chromatography, and reverse high performance liquid chromatography (RP-HPLC). Both peptides showed high ACE inhibitory activities. The molecular docking study revealed that VERGRRITSV and FVIEPNITPA were primarily attributed to the formation of strong hydrogen bonds with the active pockets of ACE. The binding free energies of VERGRRITSV and FVIEPNITPA with ACE were −14.99 and −14.69 kcal/mol, respectively. Moreover, these ACE inhibitory peptides showed good stability against gastrointestinal enzymes digestion and common food processing conditions (e.g., temperature and pH, sugar, and salt treatments). Furthermore, animal experiment results indicated that the administration of VERGRRITSV or FVIEPNITPA exhibited antihypertensive effects in spontaneously hypertensive rats. Our results demonstrated that walnut could be a potential source of bioactive peptides with ACE inhibitory activity.

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Transport, In Vivo Antihypertensive Effect, and Pharmacokinetics of an Angiotensin-Converting Enzyme (ACE) Inhibitory Peptide LVLPGE

Journal of Agricultural and Food Chemistry ◽

10.1021/acs.jafc.0c07048 ◽

2021 ◽

Vol 69 (7) ◽

pp. 2149-2156

Author(s):

Jingyan Pei ◽

Ying Hua ◽

Tingyi Zhou ◽

Xinchang Gao ◽

Yali Dang ◽

...

Keyword(s):

Angiotensin Converting Enzyme ◽

Antihypertensive Effect ◽

Converting Enzyme ◽

Inhibitory Peptide ◽

Ace Inhibitory Peptide ◽

Ace Inhibitory

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Antihypertensive Effect of Angiotensin-Converting Enzyme Inhibitory Peptide RVPSL on Spontaneously Hypertensive Rats by Regulating Gene Expression of the Renin–Angiotensin System

Journal of Agricultural and Food Chemistry ◽

10.1021/jf405189y ◽

2014 ◽

Vol 62 (4) ◽

pp. 912-917 ◽

Cited By ~ 35

Author(s):

Zhipeng Yu ◽

Yongguang Yin ◽

Wenzhu Zhao ◽

Feng Chen ◽

Jingbo Liu

Keyword(s):

Gene Expression ◽

Angiotensin Converting Enzyme ◽

Spontaneously Hypertensive Rats ◽

Antihypertensive Effect ◽

Renin Angiotensin System ◽

Converting Enzyme ◽

Hypertensive Rats ◽

Inhibitory Peptide ◽

Angiotensin System ◽

Spontaneously Hypertensive

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Novel angiotensin-I-converting enzyme inhibitory peptides derived from recombinant human αs1-casein expressed in Escherichia coli

Journal of Dairy Research ◽

10.1017/s0022029999003556 ◽

1999 ◽

Vol 66 (3) ◽

pp. 431-439 ◽

Cited By ~ 30

Author(s):

YOO-KYEONG KIM ◽

SUN YOON ◽

DAE-YEUL YU ◽

BO LÖNNERDAL ◽

BONG-HYUN CHUNG

Keyword(s):

Escherichia Coli ◽

Amino Acid Sequences ◽

Converting Enzyme ◽

Angiotensin I ◽

Ace Inhibitory Activity ◽

Inhibitory Peptides ◽

Angiotensin I Converting Enzyme ◽

Ace Inhibitory Peptides ◽

Treatment Of Hypertension ◽

Ace Inhibitory

Recombinant human αs1-casein expressed in Escherichia coli was purified and digested with trypsin in an attempt to find peptides with angiotensin-I-converting enzyme (ACE) inhibitory activity. Three novel ACE inhibitory peptides, A-II, B-II and C, were isolated and their amino acid sequences identified as Tyr–Pro–Glu–Arg (residues 8–11), Tyr–Tyr–Pro–Gln–Ile–Met–Gln–Tyr (residues 136–143) and Asn–Asn–Val–Met–Leu–Gln–Trp (residues 164–170) respectively. ACE inhibitory activities were measured for the corresponding synthetic peptides, and the ACE IC50 (the amount of peptide causing 50% inhibition of ACE activity) values of A-II, B-II and C estimated to be 132·5, 24·8 and 41·0 μmol/l respectively. Peptides A-II and C were resistant to further digestion by pepsin, whereas peptide B-II was hydrolysed. All three peptides were resistant to digestion by chymotrypsin. These ACE inhibitory peptides may prove useful for oral administration in the treatment of hypertension.

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