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

机译:酶修饰干酪中血管紧张素转化酶抑制肽的降压作用

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Two angiotensin converting enzyme (ACE)-inhibitory peptides were isolated from enzyme modified cheese (EMC) and their amino acid sequences were identified as Leu-Gin-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 (IC_(50) = 0.8 μm) and antihypertensive activity in spontaneously hypertensive rats (SHR) after single oral administration. The IC_(50) 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.
机译:从酶修饰的干酪(EMC)中分离出两个抑制血管紧张素转化酶(ACE)的肽,并将其氨基酸序列鉴定为Leu-Gin-Pro和Met-Ala-Pro。通过蛋白酶N,Umamizyme和Flavourzyme 500L的组合制备EMC。两种肽分别衍生自β-酪蛋白,f 88-90和f 102-104。单独口服后,Met-Ala-Pro在自发性高血压大鼠(SHR)中显示出较强的ACE抑制活性(IC_(50)= 0.8μm)和降压活性。 Met-Ala-Pro的IC_(50)值不受ACE预温育的影响,表明该肽是真正的ACE抑制肽。我们在这里首次报告来自EMC的降压肽。

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