Novel angiotensin I-converting enzyme inhibitory peptide derived from bovine casein
•We hydrolysed bovine casein by combination of subtilisin, bacillolysin, and trypsin.•The hydrolysate (CH-3) had a strong ACE inhibitory activity in vitro.•The CH-3 lowered the blood pressure of spontaneously hypertensive rats.•We analysed CH-3 and found the novel ACE inhibitory peptide (Met-Lys-Pro...
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Published in | Food chemistry Vol. 141; no. 4; pp. 3781 - 3789 |
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Main Authors | , , , , , |
Format | Journal Article |
Language | English |
Published |
Kidlington
Elsevier Ltd
15.12.2013
Elsevier |
Subjects | |
Online Access | Get full text |
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Summary: | •We hydrolysed bovine casein by combination of subtilisin, bacillolysin, and trypsin.•The hydrolysate (CH-3) had a strong ACE inhibitory activity in vitro.•The CH-3 lowered the blood pressure of spontaneously hypertensive rats.•We analysed CH-3 and found the novel ACE inhibitory peptide (Met-Lys-Pro).•The Met-Lys-Pro lowered the blood pressure of spontaneously hypertensive rats.
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: 74μg/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=0.12μg/mL, 0.3μM). 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. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0308-8146 1873-7072 |
DOI: | 10.1016/j.foodchem.2013.06.089 |