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Título

Production of fish protein hydrolysates from Scyliorhinus canicula discards with antihypertensive and antioxidant activities by enzymatic hydrolysis and mathematical optimization using response surface methodology

AutorVázquez, José Antonio CSIC ORCID; Blanco Comesaña, M. CSIC ORCID; Massa, Agueda E.; Rodríguez-Amado, I. CSIC; Pérez Martín, Ricardo Isaac CSIC ORCID
Palabras claveCommon Fishery Policy
Scyliorhinus canicula muscle by-products
Antihypertensive activity
Antioxidant activity
Enzyme hydrolysis
Fish discards
Fish protein hydrolysates
Response surface methodology
Fecha de publicación2017
EditorMultidisciplinary Digital Publishing Institute
CitaciónMarine Drugs 15(10): 306 (2017)
ResumenFish 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 Scyliorhinus canicula 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 pH and temperature on the hydrolysis of the S.canicula 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 pH 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.
Descripción15 pages, 3 tables, 3 figures
Versión del editorhttps://doi.org/10.3390/md15100306
URIhttp://hdl.handle.net/10261/306965
DOI10.3390/md15100306
E-ISSN1660-3397
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