Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from Glycinin, the 11S Globulin of Soybean (Glycine max)

Angiotensin I-converting enzyme (ACE), a dipeptidyl carboxypeptidase, catalyzes the conversion of Angiotensin I to the potent vasoconstrictor Angiotensin II and plays an important physiological role in regulating blood pressure. Inhibitors of angiotensin 1-converting enzyme derived from food protein...

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Bibliographic Details
Published in:Journal of agricultural and food chemistry 2006-06, Vol.54 (13), p.4568-4573
Main Authors: Mallikarjun Gouda, K. G, Gowda, Lalitha R, Rao, A. G. Appu, Prakash, V
Format: Article
Language:English
Subjects:
Amino Acid Sequence
angiotensin-converting enzyme inhibitor
Angiotensin-Converting Enzyme Inhibitors - isolation & purification
Angiotensin-Converting Enzyme Inhibitors - pharmacology
Animal, plant, fungal and microbial proteins, edible seaweeds and food yeasts
antihypertensive effect
Biological and medical sciences
carboxypeptidases
Chromatography, High Pressure Liquid
dipeptidyl carboxypeptidase
Drug Stability
enzyme inhibition
enzyme inhibitors
Food industries
Fruit and vegetable industries
functional foods
Fundamental and applied biological sciences. Psychology
Globulins - chemistry
Globulins - metabolism
Glycine max - chemistry
glycinin
Peptide Hydrolases - metabolism
peptides
Peptides - chemistry
Peptides - isolation & purification
Peptides - pharmacology
peptidyl-dipeptidase A
Soybean Proteins
soybeans
Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
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Summary:Angiotensin I-converting enzyme (ACE), a dipeptidyl carboxypeptidase, catalyzes the conversion of Angiotensin I to the potent vasoconstrictor Angiotensin II and plays an important physiological role in regulating blood pressure. Inhibitors of angiotensin 1-converting enzyme derived from food proteins are utilized for pharmaceuticals and physiologically functional foods. ACE inhibitory properties of different enzymatic hydrolysates of glycinin, the major storage protein of soybean, have been demonstrated. The IC50 value for the different enzyme digests ranges from 4.5 to 35 μg of N2. The Protease P hydrolysate contained the most potent suite of ACE inhibitory peptides. The ACE inhibitory activity of the Protease P hydrolysate after fractionation by RP-HPLC and ion-pair chromatography was ascribed to a single peptide. The peptide was homogeneous as evidenced by MALDI-TOF and identified to be a pentapeptide. The sequence was Val-Leu-Ile-Val-Pro. This peptide was synthesized using solid-phase FMOC chemistry. The IC50 for ACE inhibition was 1.69 ± 0.17 μM. The synthetic peptide was a potent competitive inhibitor of ACE with a K i of 4.5 ± 0.25 × 10-6 M. This peptide was resistant to digestion by proteases of the gastrointestinal tract. The antihypertensive property of this peptide derived from glycinin might find importance in the development of therapeutic functional foods. Keywords: Angiotensin-converting enzyme; angiotensin-converting enzyme inhibitor; soybean; Glycine max; glycinin; peptide
ISSN:0021-8561
1520-5118
DOI:10.1021/jf060264q