Salt-cured Atlantic cod skin: a sustainable source of acid-soluble type I collagen

Detalhes bibliográficos
Autor(a) principal: Coscueta, Ezequiel R.
Data de Publicação: 2021
Outros Autores: Brassesco, María Emilia, Pintado, Manuela
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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spelling 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
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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
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