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

Detalhes bibliográficos
Autor(a) principal: Pires, Carla
Data de Publicação: 2024
Outros Autores: Leitão, Matilde, Sapatinha, Maria, Gonçalves, Amparo, Oliveira, Helena, Nunes, Maria Leonor, Teixeira, Bárbara, Mendes, Rogério, Camacho, Carolina, Machado, Manuela, Pintado, Manuela, Ribeiro, Ana Rita, Vieira, Elsa F., Delerue-Matos, Cristina, Lourenço, Helena Maria, Marques, António
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10400.14/46050
Resumo: Fish 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.
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spelling Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity propertiesFPHFish wasteEnzymatic hydrolysisSWHBiochemical compositionContaminantsCytotoxicityAntioxidantACEα-amylase inhibitory activitiesFish 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.Veritati - Repositório Institucional da Universidade Católica PortuguesaPires, CarlaLeitão, MatildeSapatinha, MariaGonçalves, AmparoOliveira, HelenaNunes, Maria LeonorTeixeira, BárbaraMendes, RogérioCamacho, CarolinaMachado, ManuelaPintado, ManuelaRibeiro, Ana RitaVieira, Elsa F.Delerue-Matos, CristinaLourenço, Helena MariaMarques, António2024-08-05T14:05:51Z2024-07-302024-07-30T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/46050eng2304-815810.3390/foods131524188520075931839123610001287213100001info:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-09-06T12:48:28Zoai:repositorio.ucp.pt:10400.14/46050Portal AgregadorONGhttps://www.rcaap.pt/oai/openairemluisa.alvim@gmail.comopendoar:71602024-09-06T12:48:28Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
title Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
spellingShingle Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
Pires, Carla
FPH
Fish waste
Enzymatic hydrolysis
SWH
Biochemical composition
Contaminants
Cytotoxicity
Antioxidant
ACE
α-amylase inhibitory activities
title_short Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
title_full Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
title_fullStr Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
title_full_unstemmed Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
title_sort Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
author Pires, Carla
author_facet Pires, Carla
Leitão, Matilde
Sapatinha, Maria
Gonçalves, Amparo
Oliveira, Helena
Nunes, Maria Leonor
Teixeira, Bárbara
Mendes, Rogério
Camacho, Carolina
Machado, Manuela
Pintado, Manuela
Ribeiro, Ana Rita
Vieira, Elsa F.
Delerue-Matos, Cristina
Lourenço, Helena Maria
Marques, António
author_role author
author2 Leitão, Matilde
Sapatinha, Maria
Gonçalves, Amparo
Oliveira, Helena
Nunes, Maria Leonor
Teixeira, Bárbara
Mendes, Rogério
Camacho, Carolina
Machado, Manuela
Pintado, Manuela
Ribeiro, Ana Rita
Vieira, Elsa F.
Delerue-Matos, Cristina
Lourenço, Helena Maria
Marques, António
author2_role author
author
author
author
author
author
author
author
author
author
author
author
author
author
author
dc.contributor.none.fl_str_mv Veritati - Repositório Institucional da Universidade Católica Portuguesa
dc.contributor.author.fl_str_mv Pires, Carla
Leitão, Matilde
Sapatinha, Maria
Gonçalves, Amparo
Oliveira, Helena
Nunes, Maria Leonor
Teixeira, Bárbara
Mendes, Rogério
Camacho, Carolina
Machado, Manuela
Pintado, Manuela
Ribeiro, Ana Rita
Vieira, Elsa F.
Delerue-Matos, Cristina
Lourenço, Helena Maria
Marques, António
dc.subject.por.fl_str_mv FPH
Fish waste
Enzymatic hydrolysis
SWH
Biochemical composition
Contaminants
Cytotoxicity
Antioxidant
ACE
α-amylase inhibitory activities
topic FPH
Fish waste
Enzymatic hydrolysis
SWH
Biochemical composition
Contaminants
Cytotoxicity
Antioxidant
ACE
α-amylase inhibitory activities
description Fish 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.
publishDate 2024
dc.date.none.fl_str_mv 2024-08-05T14:05:51Z
2024-07-30
2024-07-30T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
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dc.identifier.uri.fl_str_mv http://hdl.handle.net/10400.14/46050
url http://hdl.handle.net/10400.14/46050
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2304-8158
10.3390/foods13152418
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39123610
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dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
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dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv mluisa.alvim@gmail.com
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