ACE-inhibitory and antihypertensive properties of a bovine casein hydrolysate

The aim of this study was to investigate the potential angiotensin converting enzyme (ACE)-inhibitory activity and the antihypertensive effect, after a single oral administration, of a pepsin hydrolysed bovine casein (HBC) and a fraction with molecular mass lower than 3000 Da (HBC < 3000). ACE-in...

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Published inFood chemistry Vol. 112; no. 1; pp. 211 - 214
Main Authors Miguel, M., Contreras, M.M., Recio, I., Aleixandre, A.
Format Journal Article
LanguageEnglish
Published Oxford Elsevier Ltd 2009
[Amsterdam]: Elsevier Science
Elsevier
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Summary:The aim of this study was to investigate the potential angiotensin converting enzyme (ACE)-inhibitory activity and the antihypertensive effect, after a single oral administration, of a pepsin hydrolysed bovine casein (HBC) and a fraction with molecular mass lower than 3000 Da (HBC < 3000). ACE-inhibitory activity was measured by spectrophotometric assay. These products were orally administered by gastric intubation. The systolic (SBP) and the diastolic blood pressure (DBP) were measured in spontaneously hypertensive rats by the tail cuff method before administration and also 2, 4, 6, 8, and 24 h post-administration. HBC showed a potent ACE-inhibitory activity. This activity was 10 times higher in HBC < 3000. HBC and HBC < 3000 decreased the arterial blood pressure of the rats. The decrease in the SBP observed for HBC (400 mg/kg) or HBC < 3000 (200 mg/kg) was less pronounced than that caused by 50 mg/kg of captopril (antihypertensive positive control). However, the maximal decreases in DBP caused by HBC or HBC < 3000 were as high as the maximum decrease observed for captopril. The antihypertensive effect of these products was transient and reverted 24 h after the administration. HBC and HBC < 3000 exert antihypertensive effect caused by small peptides with ACE-inhibitory activity.
Bibliography:http://dx.doi.org/10.1016/j.foodchem.2008.05.041
ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0308-8146
1873-7072
DOI:10.1016/j.foodchem.2008.05.041