Novel angiotensin I-converting enzyme inhibitory peptide derived from bovine casein

作者：Yamada Akio^*; Sakurai Takuma; Ochi Daisuke; Mitsuyama Eri; Yamauchi Koji; Abe Fumiaki

来源：Food Chemistry, 2013, 141(4): 3781-3789.

DOI：10.1016/j.foodchem.2013.06.089

• Angiotensin I-converting enzyme
• Casein
• Hydrolysate
• MKP
• Met-Lys-Pro

Bovine lactic casein was hydrolysed using a combination of three enzymes, namely, subtilisin, bacillolysin, and trypsin, and the resulting preparation was coined CH-3. CH-3 showed angiotensin I-converting enzyme (ACE)-inhibitory activity (IC50: 74 mu g/mL). A single oral administration of CH-3 led to a transient but significant decrease in the systolic blood pressure (SBP) of spontaneously hypertensive rats (SHRs), while daily oral administration of CH-3 for 28 consecutive days led to a lower rate of SBP increase. The CH-3 preparation was then fractionated and the (alpha S)2-casein-derived tripeptide Met-Lys-Pro (or MKP) was identified as a novel peptide with strong ACE-inhibitory activity (IC50 = 0.12 mu g/mL, 0.3 mu M). The MKP peptide constituted only 0.053% of CH-3 but its activity was accounted for 33% of the total ACE-inhibitory activity of CH-3. In addition, a single oral administration of MKP also led to a transient but significant decrease in the SBP of SHRs.

• 出版日期2013-12-15