Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10539851 | Food Chemistry | 2013 | 9 Pages |
Abstract
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 μg/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 αS2-casein-derived tripeptide Met-Lys-Pro (or MKP) was identified as a novel peptide with strong ACE-inhibitory activity (IC50 = 0.12 μg/mL, 0.3 μM). 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.
Related Topics
Physical Sciences and Engineering
Chemistry
Analytical Chemistry
Authors
Akio Yamada, Takuma Sakurai, Daisuke Ochi, Eri Mitsuyama, Koji Yamauchi, Fumiaki Abe,