Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards García Moreno, Pedro Jesús Espejo Carpio, Francisco Javier Guadix Escobar, Antonio María Guadix Escobar, Emilia María Fish discards Enzymatic hydrolysis SEC fractionation ACE-inhibitory activity Bioactive peptides The production of peptides exhibiting Angiotensin I-converting enzyme (ACE)-inhibitory activity from discarded Mediterranean fish species such as sardine, horse mackerel, axillary seabream, bogue and small-spotted catshark was studied. The evolution of the ACE-inhibitory activity with the degree of hydrolysis (DH) of protein hydrolysates was also investigated. Hydrolysates of horse mackerel and small-spotted catshark, both obtained with the simultaneous addition of subtilisin and trypsin, showed the highest antihypertensive activity (IC50 of 279 and 302μg/mL, respectively). For horse mackerel hydrolysate, fraction B (130-2350Da) exhibited the highest ACE-inhibitory activity (IC50=85μg/mL). In the case of small-spotted catshark hydrolysate, fraction D (<470Da) presented the lowest IC50 value (27μg/mL). In addition, 14 novel ACE-inhibitory peptides were identified in horse mackerel and small-spotted catshark hydrolysates. The peptide VAMPF, identified in fraction D of small-spotted catshark hydrolysate, is one of the most promising peptides according to its low IC50 value obtained by the QSAR-model (IC50=0.44μM) 2024-01-29T13:05:21Z 2024-01-29T13:05:21Z 2015-10-01 info:eu-repo/semantics/article P.J. García-Moreno, F.J. Espejo-Carpio, A. Guadix, E.M. Guadix (2015). Journal of Functional Foods, 18: 95-105 https://hdl.handle.net/10481/87518 10.1016/j.jff.2015.06.062 eng http://creativecommons.org/licenses/by-nc-sa/4.0/ info:eu-repo/semantics/openAccess Atribución-NoComercial-CompartirIgual 4.0 Internacional ELSEVIER