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Dernière publication 12/04/2013

Nine novel angiotensin I-converting enzyme -ACE- inhibitory peptides from cuttle

This study aimed to identify novel ACE inhibitory peptides from the muscle of cuttlefish. Proteins were hydrolyzed and the hydrolysates were then...

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    [title] => Nine novel angiotensin I-converting enzyme -ACE- inhibitory peptides from cuttle
    [paragraph] => Nine novel angiotensin I-converting enzyme (ACE) inhibitory peptides from cuttlefish (Sepia officinalis) muscle protein hydrolysates and antihypertensive effect of the potent active peptide in spontaneously hypertensive rats
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Authors
R. Baltia, A. Bougatefb, A. Silaa, D. Guillochona, P. Dhulstera and N. Nedjar-Arroumea

 Lab
Laboratoire de Procédés Biologiques, Génie Enzymatique et Microbien (ProBioGEM), UPRES-EA 1026, Polytech’Lille/IUT, Lille, FRANCE
Journal
Food Chemistry
Abstract
This study aimed to identify novel ACE inhibitory peptides from the muscle of cuttlefish. Proteins were hydrolyzed and the hydrolysates were then subjected to various types of chromatography to isolate the active peptides. Nine ACE inhibitory peptides were isolated and their molecular masses and amino acid sequences were determined using ESI-MS and ESI-MS/MS, respectively. The structures of the most potent peptides were identified as Val-Glu-Leu-Tyr-Pro, Ala-Phe-Val-Gly-Tyr-Val-Leu-Pro and Glu-Lys-Ser-Tyr-Glu-Leu-Pro. The first peptide displayed the highest ACE inhibitory activity with an IC50 of 5.22 μM. Lineweaver–Burk plots suggest that Val-Glu-Leu-Tyr-Pro acts as a non-competitive inhibitor against ACE. Furthermore, antihypertensive effects in spontaneously hypertensive rats (SHR) also revealed that oral administration of Val-Glu-Leu-Tyr-Pro can decrease systolic blood pressure significantly (p < 0.01). These results suggest that the Val-Glu-Leu-Tyr-Pro would be a beneficial ingredient for nutraceuticals and pharmaceuticals acting against hypertension and its related diseases.
BIOSEB Instruments Used
Non Invasive Pressure Measurement (LE5001)

Keywords/Topics
Domaines de recherche divers
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