Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards

Pedro Jesús García Moreno; F. Javier Espejo-Carpio; Antonio Guadix; Emilia M. Guadix

doi:10.1016/j.jff.2015.06.062

Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards

Pedro Jesús García Moreno, F. Javier Espejo-Carpio, Antonio Guadix, Emilia M. Guadix

University of Granada

Research output: Contribution to journal › Journal article › Research › peer-review

Abstract

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 302 mu g/mL, respectively). For horse mackerel hydrolysate, fraction B (130-2350 Da) exhibited the highest ACE-inhibitory activity (IC50 = 85 mu g/mL). In the case of small-spotted catshark hydrolysate, fraction D (

Original language	English
Journal	Journal of Functional Foods
Volume	18
Pages (from-to)	95-105
Number of pages	11
ISSN	1756-4646
DOIs	https://doi.org/10.1016/j.jff.2015.06.062
Publication status	Published - 2015
Externally published	Yes

Keywords

Fish discards
Enzymatic hydrolysis
SEC fractionation
ACE-inhibitory activity
Bioactive peptides
Food Science
Medicine (miscellaneous)
Nutrition and Dietetics

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title = "Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards",

abstract = "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 302 mu g/mL, respectively). For horse mackerel hydrolysate, fraction B (130-2350 Da) exhibited the highest ACE-inhibitory activity (IC50 = 85 mu g/mL). In the case of small-spotted catshark hydrolysate, fraction D (",

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author = "{Garc{\'i}a Moreno}, {Pedro Jes{\'u}s} and {Javier Espejo-Carpio}, F. and Antonio Guadix and Guadix, {Emilia M.}",

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AU - García Moreno, Pedro Jesús

AU - Javier Espejo-Carpio, F.

AU - Guadix, Antonio

AU - Guadix, Emilia M.

PY - 2015

Y1 - 2015

N2 - 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 302 mu g/mL, respectively). For horse mackerel hydrolysate, fraction B (130-2350 Da) exhibited the highest ACE-inhibitory activity (IC50 = 85 mu g/mL). In the case of small-spotted catshark hydrolysate, fraction D (

AB - 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 302 mu g/mL, respectively). For horse mackerel hydrolysate, fraction B (130-2350 Da) exhibited the highest ACE-inhibitory activity (IC50 = 85 mu g/mL). In the case of small-spotted catshark hydrolysate, fraction D (

KW - Fish discards

KW - Enzymatic hydrolysis

KW - SEC fractionation

KW - ACE-inhibitory activity

KW - Bioactive peptides

KW - Food Science

KW - Medicine (miscellaneous)

KW - Nutrition and Dietetics

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DO - 10.1016/j.jff.2015.06.062

M3 - Journal article

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SP - 95

EP - 105

JO - Journal of Functional Foods

JF - Journal of Functional Foods

ER -

Production and identification of angiotensin I-converting enzyme (ACE) inhibitory peptides from Mediterranean fish discards

Abstract

Keywords

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