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

Author:

Sila Assaad1,Haddar Anissa1,Martinez-Alvarez Oscar2,Bougatef Ali3

Affiliation:

1. Laboratory Enzyme and Bioconversion, National School of Engineering, PB 1173, 3038 Sfax, Tunisia

2. Institute of Food Science, Technology and Nutrition (ICTAN, CSIC), C/José Antonio Novais 10, 28040 Madrid, Spain

3. Higher Institute of Biotechnology of Sfax, PB 1175, 3038 Sfax, Tunisia

Abstract

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 (CI50=0.92 mg/mL). The antioxidant activities of protein hydrolysate at different concentrations were evaluated using variousin vitroantioxidant 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 byin vitrosystems 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.

Funder

Ministry of Higher Education and Scientific Research, Tunisia

Publisher

Hindawi Limited

Subject

General Chemistry

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