Production of Fish Protein Hydrolysates from Scyliorhinus canicula Discards with Antihypertensive and Antioxidant Activities by Enzymatic Hydrolysis and Mathematical Optimization Using Response Surface Methodology

• Published in: Marine drugs 2017-10, Vol.15 (10), p.306
• Main Authors: Vázquez, José A, Blanco, Maria, Massa, Agueda E, Amado, Isabel Rodríguez, Pérez-Martín, Ricardo I
• Format: Article
• Language: English
• Subjects: Angiotensin; Angiotensin-Converting Enzyme Inhibitors - metabolism; Angiotensin-Converting Enzyme Inhibitors - pharmacology; Animals; antihypertensive activity; Antihypertensive Agents - metabolism; Antihypertensive Agents - pharmacology; Antihypertensives; antioxidant activity; Antioxidants; Antioxidants - metabolism; Antioxidants - pharmacology; Bioactive compounds; Biological activity; Biomass; By products; Common Fishery Policy; Discards; Drugs; Elasmobranchii - metabolism; enzyme hydrolysis; Enzymes; Enzymolysis; Fish; fish discards; fish protein hydrolysates; Fisheries; Fishing; Gillnets; Hydrogen-Ion Concentration; Hydrolysates; Hydrolysis; Industrial fisheries; Lipids; Longline fishing; Optimization; Peptide Hydrolases - metabolism; Peptides; Peptidyl-dipeptidase A; pH effects; Policies; Protein Hydrolysates - metabolism; Protein Hydrolysates - pharmacology; Proteins; Response surface methodology; Scyliorhinus canicula; Scyliorhinus canicula muscle by-products; Subtilisin; Temperature; Viability; Waste Products
• ISSN: 1660-3397; 1660-3397
• DOI: 10.3390/md15100306

Fish discards are of major concern in new EU policies. Alternatives for the management of the new biomass that has to be landed is compulsory. The production of bioactive compounds from fish protein hydrolysates (FPH) has been explored in recent years. However, the viability of discards, which might account for up to 90-100% of captures in mixed trawler, gillnet, and longline industrial fisheries, to produce FPH from the muscle with bioactivities has still not been studied in terms of the optimization of the experimental conditions to enhance its production. The effect of and temperature on the hydrolysis of the muscle was mediated by three commercial proteases using response surface methodology. Temperatures of 64.6 °C and 60.8 °C and pHs of 9.40 and 8.90 were established as the best hydrolysis conditions for Alcalase and Esperase, respectively. Optimization of the best conditions for the maximization of antihypertensive and antioxidant activities was performed. Higher Angiotensin-converting enzyme (ACE) activity was found with Esperase. The optimum and temperature optimum for antioxidants were 55 °C/pH8.0 for ABTS/DPPH-Esperase, 63.1 °C/pH9.0 for DPPH-Alcalase, and 55 °C/pH9.0 for ABTS-Alcalase. No hydrolysis was detected when using Protamex.