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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: [email protected]
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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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