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

2008; Cambridge University Press; Volume: 75; Issue: 3 Linguagem: Inglês

10.1017/s0022029908003452

1469-7629

Hidekazu Tonouchi, Masayuki Suzuki, Masayuki Uchida, Munehiro Oda,

Meat and Animal Product Quality

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 beta-casein, f 88-90 and f 102-104, respectively. Met-Ala-Pro showed strong ACE inhibitory activity (IC50=0.8 mum) 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.