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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
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
Corresponding

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.

Type
Research Article
Copyright
Copyright © Proprietors of Journal of Dairy Research 2008

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References

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