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

Published online by Cambridge University Press:  14 July 2008

Hidekazu Tonouchi ,
Masayuki Suzuki ,
Masayuki Uchida  and
Munehiro Oda
Hidekazu Tonouchi*
Affiliation:
Food Science Institute Division of Research and Development Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
Masayuki Suzuki
Affiliation:
Food Science Institute Division of Research and Development Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
Masayuki Uchida
Affiliation:
Food Science Institute Division of Research and Development Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
Munehiro Oda
Affiliation:
Food Science Institute Division of Research and Development Meiji Dairies Corporation, 540 Naruda, Odawara, Kanagawa 250-0862, Japan
*
*For correspondence; e-mail: HIDEKAZU_TONOUCHI@MEIJI-MILK.COM
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Abstract

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.

Keywords

enzyme modified cheesepeptideantihypertensiveangiotensin converting enzyme
Type
Research Article
Information
Journal of Dairy Research , Volume 75 , Issue 3 , August 2008 , pp. 284 - 290
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

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References

Cheung, HS, Wang, FL, Ondetti, MA, Sabo, EF & Cushman, DW 1980 Binding of peptide substrates and inhibitors of angiotensin-converting enzyme. Importance of the COOH-terminal dipeptide sequence. Journal of Biological Chemistry 255(2) 401–407CrossRefGoogle ScholarPubMed
Cushman, DW & Cheung, HS 1971 Spectrophotometric assay and properties of the angiotensin-converting enzyme of rabbit lung. Biochemical Pharmacology 20(7) 1637–1648CrossRefGoogle ScholarPubMed
Fujita, H, Yokoyama, K & Yoshikawa, M 2000 Classification and antihypertensive activity of angiotensin I-converting enzyme inhibitory peptides derived from food proteins. Journal of Food Science 65(4) 564–569Google Scholar
Fujita, H & Yoshikawa, M 1999 LKPNM: a prodrug-type ACE-inhibitory peptide derived from fish protein. Immunopharmacology 44(1–2) 123–129CrossRefGoogle ScholarPubMed
Haileselassie, SS, Lee, BH & Gibbs, BF 1999 Purification and identification of potentially bioactive peptides from enzyme-modified cheese. Journal of Dairy Science 82(8) 1612–1617CrossRefGoogle ScholarPubMed
Hartmann, R & Meisel, H 2007 Food-derived peptides with biological activity: from research to food applications. Current Opinion in Biotechnology April; 18(2) 163–169CrossRefGoogle Scholar
Kilcawley, KN, Wilkinson, MG & Fox, PF 1998 Enzyme-modified cheese. International Dairy Journal 8 1–10CrossRefGoogle Scholar
Kitts, DD & Weiler, K 2003 Bioactive proteins and peptides from food sources. Applications of bioprocesses used in isolation and recovery. Current Pharmaceutical Design 9(16) 1309–1323CrossRefGoogle ScholarPubMed
Matsufuji, H, Matsui, T, Ohshige, S, Kawasaki, T, Osajima, K & Osajima, Y 1995 Antihypertensive effects of angiotensin fragments in SHR. Bioscience Biotechnology and Biochemistry 59(8) 1398–1401CrossRefGoogle ScholarPubMed
Miyoshi, S, Ishikawa, H, Kaneko, T, Fukui, F, Tanaka, H & Maruyama, S 1991 Structures and activity of angiotensin-converting enzyme inhibitors in an alpha-zein hydrolysate. Agricultural and Biological Chemistry 55(5) 1313–1318Google Scholar
Murakami, M, Tonouchi, H, Takahashi, R, Kitazawa, H, Kawai, Y, Negishi, H & Saito, T 2004 Structural analysis of a new anti-hypertensive peptide (beta-lactosin B) isolated from a commercial whey product. Journal of Dairy Science 87(7) 1967–1974CrossRefGoogle ScholarPubMed
Murray, BA & FitzGerald, RJ 2007 Angiotensin converting enzyme inhibitory peptides derived from food proteins: biochemistry, bioactivity and production. Current Pharmaceutical Design 13(8) 773–791CrossRefGoogle ScholarPubMed
Nakamura, Y, Yamamoto, N, Sakai, K & Takano, T 1995 Antihypertensive effect of sour milk and peptides isolated from it that are inhibitors to angiotensin I-converting enzyme. Journal of Dairy Science 78(6) 1253–1257Google Scholar
Pihlanto, A & Korhonen, H 2003 Bioactive peptides and proteins. Advances in Food and Nutrition Research 47 175–276CrossRefGoogle ScholarPubMed
Silva, SV & Malcata, FX 2005 Caseins as source of bioactive peptides. International Dairy Journal 15 1–15Google Scholar
Suzuki, M, Uchida, M, Tonouchi, H & Oda, M 2007 Inhibition of angiotensin I converting enzyme and hypotensive effect in spontaneously hypertensive rats by enzyme-modified cheese. Nippon Shokuhin Kagaku Kogaku Kaishi 54(4) 181–186CrossRefGoogle Scholar
Tanabe, S, Isobe, N, Miyauchi, E, Kobayashi, S, Suzuki, M & Oda, M 2006 Identification of a peptide in enzymatic hydrolyzate of cheese that inhibits ovalbumin permeation in Caco-2 cells. Journal of Agricultural and Food Chemistry Sep 6;54(18) 6904–6908CrossRefGoogle ScholarPubMed
Vermeirssen, V, Van, CJ & Verstraete, W 2004 Bioavailability of angiotensin I converting enzyme inhibitory peptides. British Journal of Nutrition 92(3) 357–366CrossRefGoogle ScholarPubMed