Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso
Autor(a) principal: | |
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Data de Publicação: | 1998 |
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/10400.14/6660 |
Resumo: | Primary proteolysis of ovine and caprine Na-caseinate at 30°C in phosphate buffer at pH 6.5 or 5.5 in the absence of NaCl and at pH 5.2 with 5% (w/v) NaCl by cardosins in aqueous extracts of Cynara cardunculus flowers was investigated using urea-polyacrylamide gel electrophoresis and reversed-phase high performance liquid chromatography. Caprine caseinate underwent more extensive degradation than ovine caseinate under the same conditions (pH 6.5 and pH 5.5); proteolysis of b- and as-caseins in ovine and, to a lesser extent, in caprine caseinates was reduced in the presence of 5% (w/v) NaCl. Peptide profiles of the pH 4.6-soluble extract had different patterns throughout ripening arising from the different specificity of cardosins toward ovine and caprine Na-caseinates. The major cleavage sites in ovine (caprine) caseinate were Phe105-Met106 (Lys116-Thr117) for k-casein, Leu127-Thr128 and Leu190-Tyr191 (Glu100-Thr101, Leu127-Thr128, Leu136-Pro137 and Leu190- Tyr191) for b-casein, Phe23-Val24 (Phe23-Val24, Trp164-Tyr165 and Tyr173-Thr174) for as1-casein and Phe88-Tyr89 (Ser9-Ser10, Phe88-Tyr89 and Tyr179-Leu180) for as2-casein. |
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Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculusoPlant rennetCheese ripeningProteasesEnzyme specificityPrimary proteolysis of ovine and caprine Na-caseinate at 30°C in phosphate buffer at pH 6.5 or 5.5 in the absence of NaCl and at pH 5.2 with 5% (w/v) NaCl by cardosins in aqueous extracts of Cynara cardunculus flowers was investigated using urea-polyacrylamide gel electrophoresis and reversed-phase high performance liquid chromatography. Caprine caseinate underwent more extensive degradation than ovine caseinate under the same conditions (pH 6.5 and pH 5.5); proteolysis of b- and as-caseins in ovine and, to a lesser extent, in caprine caseinates was reduced in the presence of 5% (w/v) NaCl. Peptide profiles of the pH 4.6-soluble extract had different patterns throughout ripening arising from the different specificity of cardosins toward ovine and caprine Na-caseinates. The major cleavage sites in ovine (caprine) caseinate were Phe105-Met106 (Lys116-Thr117) for k-casein, Leu127-Thr128 and Leu190-Tyr191 (Glu100-Thr101, Leu127-Thr128, Leu136-Pro137 and Leu190- Tyr191) for b-casein, Phe23-Val24 (Phe23-Val24, Trp164-Tyr165 and Tyr173-Thr174) for as1-casein and Phe88-Tyr89 (Ser9-Ser10, Phe88-Tyr89 and Tyr179-Leu180) for as2-casein.ElsevierVeritati - Repositório Institucional da Universidade Católica PortuguesaSousa, M. JoséMalcata, F. Xavier2011-10-21T12:55:36Z19981998-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.14/6660engSOUSA, M. José; MALCATA, F. Xavier - Proteolysis of Ovine and Caprine Caseins in Solution by Enzymatic Extracts from Flowers of Cynara cardunculus. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 22 (1998), p. 305–314info: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:RCAAP2023-07-12T17:10:55Zoai:repositorio.ucp.pt:10400.14/6660Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T18:06:04.272877Repositório 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 |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
title |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
spellingShingle |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso Sousa, M. José Plant rennet Cheese ripening Proteases Enzyme specificity |
title_short |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
title_full |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
title_fullStr |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
title_full_unstemmed |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
title_sort |
Proteolysis of ovine and caprine Caseins in solution by enzymatic extracts from flowers of Cynara cardunculuso |
author |
Sousa, M. José |
author_facet |
Sousa, M. José Malcata, F. Xavier |
author_role |
author |
author2 |
Malcata, F. Xavier |
author2_role |
author |
dc.contributor.none.fl_str_mv |
Veritati - Repositório Institucional da Universidade Católica Portuguesa |
dc.contributor.author.fl_str_mv |
Sousa, M. José Malcata, F. Xavier |
dc.subject.por.fl_str_mv |
Plant rennet Cheese ripening Proteases Enzyme specificity |
topic |
Plant rennet Cheese ripening Proteases Enzyme specificity |
description |
Primary proteolysis of ovine and caprine Na-caseinate at 30°C in phosphate buffer at pH 6.5 or 5.5 in the absence of NaCl and at pH 5.2 with 5% (w/v) NaCl by cardosins in aqueous extracts of Cynara cardunculus flowers was investigated using urea-polyacrylamide gel electrophoresis and reversed-phase high performance liquid chromatography. Caprine caseinate underwent more extensive degradation than ovine caseinate under the same conditions (pH 6.5 and pH 5.5); proteolysis of b- and as-caseins in ovine and, to a lesser extent, in caprine caseinates was reduced in the presence of 5% (w/v) NaCl. Peptide profiles of the pH 4.6-soluble extract had different patterns throughout ripening arising from the different specificity of cardosins toward ovine and caprine Na-caseinates. The major cleavage sites in ovine (caprine) caseinate were Phe105-Met106 (Lys116-Thr117) for k-casein, Leu127-Thr128 and Leu190-Tyr191 (Glu100-Thr101, Leu127-Thr128, Leu136-Pro137 and Leu190- Tyr191) for b-casein, Phe23-Val24 (Phe23-Val24, Trp164-Tyr165 and Tyr173-Thr174) for as1-casein and Phe88-Tyr89 (Ser9-Ser10, Phe88-Tyr89 and Tyr179-Leu180) for as2-casein. |
publishDate |
1998 |
dc.date.none.fl_str_mv |
1998 1998-01-01T00:00:00Z 2011-10-21T12:55:36Z |
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/10400.14/6660 |
url |
http://hdl.handle.net/10400.14/6660 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
SOUSA, M. José; MALCATA, F. Xavier - Proteolysis of Ovine and Caprine Caseins in Solution by Enzymatic Extracts from Flowers of Cynara cardunculus. Enzyme and Microbial Technology. ISSN 0141-0229. Vol. 22 (1998), p. 305–314 |
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 |
publisher.none.fl_str_mv |
Elsevier |
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 |
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1799131726438465536 |