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Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties

2024-07-30Journal article Open access
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dc.contributor.authorPires, Carla
dc.contributor.authorLeitão, Matilde
dc.contributor.authorSapatinha, Maria
dc.contributor.authorGonçalves, Amparo
dc.contributor.authorOliveira, Helena
dc.contributor.authorNunes, Maria Leonor
dc.contributor.authorTeixeira, Bárbara
dc.contributor.authorMendes, Rogério
dc.contributor.authorCamacho, Carolina
dc.contributor.authorMachado, Manuela
dc.contributor.authorPintado, Manuela
dc.contributor.authorRibeiro, Ana Rita
dc.contributor.authorVieira, Elsa F.
dc.contributor.authorDelerue-Matos, Cristina
dc.contributor.authorLourenço, Helena Maria
dc.contributor.authorMarques, António
dc.date.accessioned2024-08-05T14:05:51Z
dc.date.available2024-08-05T14:05:51Z
dc.date.issued2024-07-30
dc.description.abstractFish by-products can be converted into high-value-added products like fish protein hydrolysates (FPHs), which have high nutritional value and are rich in bioactive peptides with health benefits. This study aims to characterise FPHs derived from salmon heads (HPSs) and Cape hake trimmings (HPHs) using Alcalase for enzymatic hydrolysis and Subcritical Water Hydrolysis (SWH) as an alternative method. All hydrolysates demonstrated high protein content (70.4–88.7%), with the degree of hydrolysis (DH) ranging from 10.7 to 36.4%. The peptide profile of FPHs indicated the breakdown of proteins into small peptides. HPSs showed higher levels of glycine and proline, while HPHs had higher concentrations of glutamic acid, leucine, threonine, and phenylalanine. Similar elemental profiles were observed in both HPHs and HPSs, and the levels of Cd, Pb, and Hg were well below the legislated limits. Hydrolysates do not have a negative effect on cell metabolism and contribute to cell growth. HPSs and HPHs exhibited high 2,2′–azino-bis(3 ethylbenzthiazoline-6)-sulfonic acid (ABTS) radical scavenging activity, Cu2+ and Fe2+ chelating activities, and angiotensin-converting enzyme (ACE) inhibitory activity, with HPHs generally displaying higher activities. The α-amylase inhibition of both FPHs was relatively low. These results indicate that HPHs are a promising natural source of nutritional compounds and bioactive peptides, making them potential candidates for use as an ingredient in new food products or nutraceuticals. SWH at 250 °C is a viable alternative to enzymatic methods for producing FPHs from salmon heads with high antioxidant and chelating properties.pt_PT
dc.description.versioninfo:eu-repo/semantics/publishedVersionpt_PT
dc.identifier.doi10.3390/foods13152418pt_PT
dc.identifier.eid85200759318
dc.identifier.issn2304-8158
dc.identifier.pmcPMC11311982
dc.identifier.pmid39123610
dc.identifier.urihttp://hdl.handle.net/10400.14/46050
dc.identifier.wos001287213100001
dc.language.isoengpt_PT
dc.peerreviewedyespt_PT
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/pt_PT
dc.subjectFPHpt_PT
dc.subjectFish wastept_PT
dc.subjectEnzymatic hydrolysispt_PT
dc.subjectSWHpt_PT
dc.subjectBiochemical compositionpt_PT
dc.subjectContaminantspt_PT
dc.subjectCytotoxicitypt_PT
dc.subjectAntioxidantpt_PT
dc.subjectACEpt_PT
dc.subjectα-amylase inhibitory activitiespt_PT
dc.titleProtein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity propertiespt_PT
dc.typejournal article
dspace.entity.typePublication
oaire.citation.issue15pt_PT
oaire.citation.titleFoodspt_PT
oaire.citation.volume13pt_PT
rcaap.rightsopenAccesspt_PT
rcaap.typearticlept_PT

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