Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus
Autor(a) principal: | |
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Data de Publicação: | 2004 |
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/10400.14/6719 |
Resumo: | The effect of coagulant level on the quality and quantity of protein breakdown during the first 24 h of ripening of cheese-like systems, manufactured with sterilized ovine milk using crude aqueous extracts of Cynara cardunculus as coagulant, was experimentally assessed. Urea-polyacrylamide gel electrophoresis was performed on both water-soluble and water-insoluble cheese extracts to monitor the casein degradation pattern; the ripening extension index and the ripening depth index were thus calculated. Peptides from the water-soluble fraction were isolated by reverse-phase, high-performance liquid chromatography and partially sequenced by Edman degradation. Higher residual coagulant levels in curdled milk led to earlier breakdown of caseins, as expected. The primary cleavage sites were Phe105-Met106 in k-casein, Phe23-Val24 in s1-casein, and Leu127-Thr128, Ser142-Trp143, Leu165-Ser166, and Leu190-Tyr191 in β-casein. |
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Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculusPlant rennetRipeningDairy foodHPLCElectrophoresisThe effect of coagulant level on the quality and quantity of protein breakdown during the first 24 h of ripening of cheese-like systems, manufactured with sterilized ovine milk using crude aqueous extracts of Cynara cardunculus as coagulant, was experimentally assessed. Urea-polyacrylamide gel electrophoresis was performed on both water-soluble and water-insoluble cheese extracts to monitor the casein degradation pattern; the ripening extension index and the ripening depth index were thus calculated. Peptides from the water-soluble fraction were isolated by reverse-phase, high-performance liquid chromatography and partially sequenced by Edman degradation. Higher residual coagulant levels in curdled milk led to earlier breakdown of caseins, as expected. The primary cleavage sites were Phe105-Met106 in k-casein, Phe23-Val24 in s1-casein, and Leu127-Thr128, Ser142-Trp143, Leu165-Ser166, and Leu190-Tyr191 in β-casein.WileyVeritati - Repositório Institucional da Universidade Católica PortuguesaSilva, S. V.Malcata, F. X.2011-10-21T15:28:55Z2004-082004-08-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/6719eng"Journal of Food Science". ISSN 0022-1147. 69:7 (2004) C579-C584info: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:RCAAP2023-07-12T17:09:34Zoai:repositorio.ucp.pt:10400.14/6719Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:05:08.102243Repositório 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 |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
title |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
spellingShingle |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus Silva, S. V. Plant rennet Ripening Dairy food HPLC Electrophoresis |
title_short |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
title_full |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
title_fullStr |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
title_full_unstemmed |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
title_sort |
Influence of the coagulant level on early proteolysis in ovine cheese-like systems made with sterilized milk and Cynara cardunculus |
author |
Silva, S. V. |
author_facet |
Silva, S. V. Malcata, F. X. |
author_role |
author |
author2 |
Malcata, F. X. |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Silva, S. V. Malcata, F. X. |
dc.subject.por.fl_str_mv |
Plant rennet Ripening Dairy food HPLC Electrophoresis |
topic |
Plant rennet Ripening Dairy food HPLC Electrophoresis |
description |
The effect of coagulant level on the quality and quantity of protein breakdown during the first 24 h of ripening of cheese-like systems, manufactured with sterilized ovine milk using crude aqueous extracts of Cynara cardunculus as coagulant, was experimentally assessed. Urea-polyacrylamide gel electrophoresis was performed on both water-soluble and water-insoluble cheese extracts to monitor the casein degradation pattern; the ripening extension index and the ripening depth index were thus calculated. Peptides from the water-soluble fraction were isolated by reverse-phase, high-performance liquid chromatography and partially sequenced by Edman degradation. Higher residual coagulant levels in curdled milk led to earlier breakdown of caseins, as expected. The primary cleavage sites were Phe105-Met106 in k-casein, Phe23-Val24 in s1-casein, and Leu127-Thr128, Ser142-Trp143, Leu165-Ser166, and Leu190-Tyr191 in β-casein. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-08 2004-08-01T00:00:00Z 2011-10-21T15:28:55Z |
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/10400.14/6719 |
url |
http://hdl.handle.net/10400.14/6719 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
"Journal of Food Science". ISSN 0022-1147. 69:7 (2004) C579-C584 |
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 |
Wiley |
publisher.none.fl_str_mv |
Wiley |
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 |
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Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação |
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RCAAP |
institution |
RCAAP |
reponame_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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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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1799131714084143104 |