Protein hydrolysates from salmon heads and cape hake by-products: comparing enzymatic method with subcritical water extraction on bioactivity properties
Autor(a) principal: | |
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Data de Publicação: | 2024 |
Outros Autores: | , , , , , , , , , , , , , , |
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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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 |
format |
article |
status_str |
publishedVersion |
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 85200759318 39123610 001287213100001 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
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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1817547135450611712 |