Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen
Autor(a) principal: | |
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Data de Publicação: | 2021 |
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/10400.14/36603 |
Resumo: | Collagen is the most abundant protein in the animal kingdom. Industrial collagen is mainly bovine and porcine origin. However, due to religious beliefs, allergic issues, and infectious diseases, alternative sources of collagen as marine are gaining increasing interest. In this work, the acid-soluble collagen (ASC) were extracted from salt-cured Atlantic cod (Gadus morhua) skin and characterized. The extraction yield was about 2.0%, equivalent to the extraction yield reported for other fish skins. The electrophoretic pattern showed the typical type I structure (α, β and γ chains). UV-VIS and FTIR absorbance spectra suggested a very pure ASC with an intact triple helical structure. The integrity and the adequate porosity required for different applications were then confirmed by electron micrograph. Our findings allow us to say that, for the first time, we extracted acid-soluble type I collagen from salt-cured Atlantic cod skin, with characteristics suitable for application in various fields, such as biomedical. |
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Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagenSalt-cured cod skinGadus morhuaCollagenFishery by-productsBiomaterialsCollagen is the most abundant protein in the animal kingdom. Industrial collagen is mainly bovine and porcine origin. However, due to religious beliefs, allergic issues, and infectious diseases, alternative sources of collagen as marine are gaining increasing interest. In this work, the acid-soluble collagen (ASC) were extracted from salt-cured Atlantic cod (Gadus morhua) skin and characterized. The extraction yield was about 2.0%, equivalent to the extraction yield reported for other fish skins. The electrophoretic pattern showed the typical type I structure (α, β and γ chains). UV-VIS and FTIR absorbance spectra suggested a very pure ASC with an intact triple helical structure. The integrity and the adequate porosity required for different applications were then confirmed by electron micrograph. Our findings allow us to say that, for the first time, we extracted acid-soluble type I collagen from salt-cured Atlantic cod skin, with characteristics suitable for application in various fields, such as biomedical.Veritati - Repositório Institucional da Universidade Católica PortuguesaCoscueta, Ezequiel R.Brassesco, María EmiliaPintado, Manuela2022-02-04T15:24:21Z2021-02-172021-02-17T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/36603eng10.20944/preprints202102.0378.v1info: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:RCAAP2023-07-12T17:42:04Zoai:repositorio.ucp.pt:10400.14/36603Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:29:45.170925Repositório 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 |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
title |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
spellingShingle |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen Coscueta, Ezequiel R. Salt-cured cod skin Gadus morhua Collagen Fishery by-products Biomaterials |
title_short |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
title_full |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
title_fullStr |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
title_full_unstemmed |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
title_sort |
Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen |
author |
Coscueta, Ezequiel R. |
author_facet |
Coscueta, Ezequiel R. Brassesco, María Emilia Pintado, Manuela |
author_role |
author |
author2 |
Brassesco, María Emilia Pintado, Manuela |
author2_role |
author author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Coscueta, Ezequiel R. Brassesco, María Emilia Pintado, Manuela |
dc.subject.por.fl_str_mv |
Salt-cured cod skin Gadus morhua Collagen Fishery by-products Biomaterials |
topic |
Salt-cured cod skin Gadus morhua Collagen Fishery by-products Biomaterials |
description |
Collagen is the most abundant protein in the animal kingdom. Industrial collagen is mainly bovine and porcine origin. However, due to religious beliefs, allergic issues, and infectious diseases, alternative sources of collagen as marine are gaining increasing interest. In this work, the acid-soluble collagen (ASC) were extracted from salt-cured Atlantic cod (Gadus morhua) skin and characterized. The extraction yield was about 2.0%, equivalent to the extraction yield reported for other fish skins. The electrophoretic pattern showed the typical type I structure (α, β and γ chains). UV-VIS and FTIR absorbance spectra suggested a very pure ASC with an intact triple helical structure. The integrity and the adequate porosity required for different applications were then confirmed by electron micrograph. Our findings allow us to say that, for the first time, we extracted acid-soluble type I collagen from salt-cured Atlantic cod skin, with characteristics suitable for application in various fields, such as biomedical. |
publishDate |
2021 |
dc.date.none.fl_str_mv |
2021-02-17 2021-02-17T00:00:00Z 2022-02-04T15:24:21Z |
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/10400.14/36603 |
url |
http://hdl.handle.net/10400.14/36603 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.20944/preprints202102.0378.v1 |
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 |
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1799132018659819521 |