Novel Angiotensin I-Converting Enzyme Inhibitory Peptides Found in a Thermolysin-Treated Elastin with Antihypertensive Activity
Novel Angiotensin I-Converting Enzyme Inhibitory Peptides Found in a Thermolysin-Treated Elastin with Antihypertensive Activity
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DOI：
10.1271/bbb.120083
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发表时间：
2012-07-01
影响因子：
1.6
通讯作者：
Mura, Kiyoshi
中科院分区：
文献类型：
--
作者：
Sato, Yuko;Toyoda, Tsudoi;Mura, Kiyoshi
通过用嗜热菌蛋白酶水解弹性蛋白和胶原蛋白来产生血管紧张素I转换酶（ACE）抑制活性。弹性蛋白水解产物对ACE抑制的531.6 μ g/mL的IC 50值比胶原蛋白水解产物的2885.1 μ g/mL小5倍。我们通过给自发性高血压大鼠（雄性）喂食含有1%弹性蛋白水解产物的饮食9周，证实了弹性蛋白水解产物在体内的抗高血压活性。约4周后，弹性蛋白水解物组大鼠的收缩压变得显著低于对照组。我们确定了新的ACE抑制肽，VGHyp，VVPG和VYPGG，在弹性蛋白水解物，通过使用蛋白质测序仪和四极线性离子阱（QIT）-LC/MS/MS。VYPGG对ACE的最高IC 50值为244 μ M，可能有潜在的用途作为功能性食品。
Angiotensin I-converting enzyme (ACE) inhibitory activity was generated from elastin and collagen by hydrolyzing with thermolysin. The IC50 value of 531.6 mu g/mL for ACE inhibition by the elastin hydrolysate was five times less than 2885.1 mu g/mL by the collagen hydrolysate. We confirmed the antihypertensive activity of the elastin hydrolysate in vivo by feeding spontaneously hypertensive rats (male) on a diet containing 1% of the elastin hydrolysate for 9 weeks. About 4 week later, the systolic blood pressure of the rats in the elastin hydrolysate group had become significantly lower than that of the control group. We identified novel ACE inhibitory peptides, VGHyp, VVPG and VYPGG, in the elastin hydrolysate by using a protein sequencer and quadrupole linear ion trap (QIT)-LC/MS/MS. VYPGG had the highest IC50 value of 244 mu M against ACE and may have potential use as a functional food.