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Journal of Chemistry
Volume 2013, Article ID 545303, 6 pages
Research Article

Angiotensin-I-Converting Enzyme Inhibitory and Antioxidant Activities of Protein Hydrolysate from Muscle of Barbel (Barbus callensis)

1Laboratory Enzyme and Bioconversion, National School of Engineering, PB 1173, 3038 Sfax, Tunisia
2Institute of Food Science, Technology and Nutrition (ICTAN, CSIC), C/José Antonio Novais 10, 28040 Madrid, Spain
3Higher Institute of Biotechnology of Sfax, PB 1175, 3038 Sfax, Tunisia

Received 31 May 2013; Accepted 16 August 2013

Academic Editor: Souhail Besbes

Copyright © 2013 Assaad Sila et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.


The present study investigated angiotensin-I-converting enzyme (ACE) inhibitory and antioxidant activities of barbel muscle protein hydrolysate prepared with Alcalase. The barbel muscle protein hydrolysate displayed a high ACE inhibitory activity ( mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using various in vitro antioxidant assays, including 1,1-diphenyl-2-picrylhydrazyl (DPPH) radical method and reducing power assay. The barbel muscle protein hydrolysate exhibited an important radical scavenging effect and reducing power. These results obtained by in vitro systems obviously established the antioxidant potency of barbel hydrolysate to donate electron or hydrogen atom to reduce the free radical. Furthermore, these bioactive substances can be exploited into functional foods or used as source of nutraceuticals.