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

Mallikarjun Gouda, K. G. and Lalitha, R. Gowda and Appu Rao, A. G. and Prakash, V. (2006) Angiotensin I-Converting Enzyme Inhibitory Peptide Derived from Glycinin, the 11S Globulin of Soybean ( Glycine max). Journal of Agricultural and Food Chemistry, 54. pp. 4568-4573.

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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 Ìg 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 chromatographywas 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 ÌM. The synthetic peptide was a potent competitive inhibitor of ACE with a Ki 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.

Item Type: Article
Uncontrolled Keywords: Angiotensin-converting enzyme; angiotensin-converting enzyme inhibitor; soybean; Glycine max; glycinin; peptide
Subjects: 500 Natural Sciences and Mathematics > 04 Chemistry and Allied Sciences > 29 Protein Chemistry
600 Technology > 08 Food technology > 22 Legumes-Pulses > 05 Soya bean
Divisions: Protein Chemistry and Technology
Depositing User: Food Sci. & Technol. Information Services
Date Deposited: 07 Apr 2007
Last Modified: 28 Dec 2011 09:27
URI: http://ir.cftri.res.in/id/eprint/581

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