Isolation of angiotensin I converting enzyme inhibitory peptides from a fish by-products hydrolysate Tensideal®
Many ACE inhibitory peptides have been isolated from various protein hydrolysates such as casein, soybean or fish protein. The purpose of this work is to isolate ACE inhibitory peptides derived from an enzymatic hydrolysate of fish by-products named Tensideal®, which is actually produced industrially by IDMER.
The measurement of ACE inhibitory activity was performed using a HPLC method consisting on measuring the levels of the substrate (FAPGG (N-(3-[2-furylacryloyl)-Phe-Gly-Gly)) or the product formed (FAP) with and without inhibitor. By this method, the hydrolysate Tensideal® showed an IC50 of 65µg of peptides while the reference Captopril® showed an IC50 of 0.3ng.
To isolate ACE inhibitory peptides from the hydrolysate, different chromatographic methods were successively applied to select step by step the most active fraction. Gel filtration has demonstrated that major peptides have molecular weight less than 1000 Da and some tests realised by C18 HPLC have showed that act ...
- Isolation of angiotensin I converting enzyme inhibitory peptides from a fish by-products hydrolysate Tensideal®
- Book Title
- Peptides for Youth
- Book Subtitle
- The Proceedings of the 20th American Peptide Symposium
- pp 483-484
- Print ISBN
- Online ISBN
- Series Title
- Advances in Experimental Medicine and Biology
- Series Volume
- Series ISSN
- Springer New York
- Copyright Holder
- Springer-Verlag New York
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- Editor Affiliations
- 1. Department of Chemistry & Biochemistry, New Mexico State University
- 2. Department of Pharmacology, University of Sherbrooke Medical School
- 3. Département de Chimie, Université de Montréal
- Author Affiliations
- 4. Laboratoire de Biotechnologie et Chimie Marines, Université de Bretagne Sud, BP 92116, Lorient, 56321, France
- 5. IDMER, 2 rue Batelière, Lorient, 56100, France
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