Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films
Autor(a) principal: | |
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Data de Publicação: | 2018 |
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/1822/59336 |
Resumo: | The commercial use of biodegradable proteins films is still limited due to their poor mechanical and barrier performance. However, processing of proteins to modify their structure may have a significant impact on films properties. Thus, the effect of thermal or pH-induced denaturation on the gelation behavior of Withemouth Croacker proteins was investigated in the development of films for packaging. Denaturation at pH 2 and pH 10 yielded the toughest protein gels. Gelation through pH modification is related to conformational changes in the structure of fish proteins, especially in secondary structure. Rheology tests demonstrated that a stronger gel was formed at pH 2, which might be due to the positively charged proteins. This behavior is related to the lower mesh size of the gel as demonstrated by small-angle X-ray scattering experiments. Gels prepared at both pH 2 and pH 10 had the ability to form cohesive films; however, no significant differences were observed between these treatments for water vapor permeability and mechanical properties. The modification of protein structure through gelation produced more soluble and less permeable films. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging filmsProteins from fish (Whitemouth croaker)Packaging filmsProtein gelationSecondary structureScience & TechnologyThe commercial use of biodegradable proteins films is still limited due to their poor mechanical and barrier performance. However, processing of proteins to modify their structure may have a significant impact on films properties. Thus, the effect of thermal or pH-induced denaturation on the gelation behavior of Withemouth Croacker proteins was investigated in the development of films for packaging. Denaturation at pH 2 and pH 10 yielded the toughest protein gels. Gelation through pH modification is related to conformational changes in the structure of fish proteins, especially in secondary structure. Rheology tests demonstrated that a stronger gel was formed at pH 2, which might be due to the positively charged proteins. This behavior is related to the lower mesh size of the gel as demonstrated by small-angle X-ray scattering experiments. Gels prepared at both pH 2 and pH 10 had the ability to form cohesive films; however, no significant differences were observed between these treatments for water vapor permeability and mechanical properties. The modification of protein structure through gelation produced more soluble and less permeable films.The authors acknowledge the financial support by the Coordination for the Improvement of Higher Education Personnel and National Counsel of Technological and Scientific Development of Brazil.info:eu-repo/semantics/publishedVersionElsevier Science LtdUniversidade do MinhoRomani, Viviane P.Machado, A. V.Olsen, Bradley D.Martins, Vilasia G.20182018-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/1822/59336eng0268-005X10.1016/j.foodhyd.2017.08.021info: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:RCAAP2023-07-21T12:50:28ZPortal AgregadorONG |
dc.title.none.fl_str_mv |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
title |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
spellingShingle |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films Romani, Viviane P. Proteins from fish (Whitemouth croaker) Packaging films Protein gelation Secondary structure Science & Technology |
title_short |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
title_full |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
title_fullStr |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
title_full_unstemmed |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
title_sort |
Effects of pH modification in proteins from fish (Whitemouth croaker) and their application in food packaging films |
author |
Romani, Viviane P. |
author_facet |
Romani, Viviane P. Machado, A. V. Olsen, Bradley D. Martins, Vilasia G. |
author_role |
author |
author2 |
Machado, A. V. Olsen, Bradley D. Martins, Vilasia G. |
author2_role |
author author author |
dc.contributor.none.fl_str_mv |
Universidade do Minho |
dc.contributor.author.fl_str_mv |
Romani, Viviane P. Machado, A. V. Olsen, Bradley D. Martins, Vilasia G. |
dc.subject.por.fl_str_mv |
Proteins from fish (Whitemouth croaker) Packaging films Protein gelation Secondary structure Science & Technology |
topic |
Proteins from fish (Whitemouth croaker) Packaging films Protein gelation Secondary structure Science & Technology |
description |
The commercial use of biodegradable proteins films is still limited due to their poor mechanical and barrier performance. However, processing of proteins to modify their structure may have a significant impact on films properties. Thus, the effect of thermal or pH-induced denaturation on the gelation behavior of Withemouth Croacker proteins was investigated in the development of films for packaging. Denaturation at pH 2 and pH 10 yielded the toughest protein gels. Gelation through pH modification is related to conformational changes in the structure of fish proteins, especially in secondary structure. Rheology tests demonstrated that a stronger gel was formed at pH 2, which might be due to the positively charged proteins. This behavior is related to the lower mesh size of the gel as demonstrated by small-angle X-ray scattering experiments. Gels prepared at both pH 2 and pH 10 had the ability to form cohesive films; however, no significant differences were observed between these treatments for water vapor permeability and mechanical properties. The modification of protein structure through gelation produced more soluble and less permeable films. |
publishDate |
2018 |
dc.date.none.fl_str_mv |
2018 2018-01-01T00:00:00Z |
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/1822/59336 |
url |
http://hdl.handle.net/1822/59336 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
0268-005X 10.1016/j.foodhyd.2017.08.021 |
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.publisher.none.fl_str_mv |
Elsevier Science Ltd |
publisher.none.fl_str_mv |
Elsevier Science Ltd |
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) |
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repository.mail.fl_str_mv |
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_version_ |
1777303856756031488 |