Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese
- Autores
- Hynes, Erica Rut; Candioti, Mario César; Zalazar, Carlos Antonio; McSweeney. P.L.H
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- It is generally believed that enzymes in rennet are largely denatured by cooking during the manufacture of hard cheese. However, typical products of rennet action on αs1-casein have been detected in these varieties. The aim of the present work was to relate residual rennet activity with proteolysis in Reggianito Argentino, a hard cooked cheese. For that purpose, we analysed samples of cheese cooked at low (45°C), control (52°C) or high temperature (60°C) for residual rennet activity. We also studied proteolysis in cheese at the end of ripening by means of peptide mapping and electrophoresis. Rennet activity was inversely proportional to cooking temperature, although the activity was quantifiable even in cheeses cooked at high temperature, suggesting renaturation or incomplete denaturation of the enzyme. Indices of proteolysis, especially the levels of the peptide αs1-CN(f24-199), were consistent with residual rennet activity. Secondary proteolysis was also different for cheeses cooked at different temperatures.
Fil: Hynes, Erica Rut. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina
Fil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina
Fil: Zalazar, Carlos Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina
Fil: McSweeney. P.L.H. No especifíca; - Materia
-
HARD CHEESES
RENNETING
CHEESEMAKING
PROTEOLYSIS - CHEESE RIPENING - Nivel de accesibilidad
- acceso abierto
- Condiciones de uso
- https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
- Repositorio
- Institución
- Consejo Nacional de Investigaciones Científicas y Técnicas
- OAI Identificador
- oai:ri.conicet.gov.ar:11336/151266
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheeseHynes, Erica RutCandioti, Mario CésarZalazar, Carlos AntonioMcSweeney. P.L.HHARD CHEESESRENNETINGCHEESEMAKINGPROTEOLYSIS - CHEESE RIPENINGhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1It is generally believed that enzymes in rennet are largely denatured by cooking during the manufacture of hard cheese. However, typical products of rennet action on αs1-casein have been detected in these varieties. The aim of the present work was to relate residual rennet activity with proteolysis in Reggianito Argentino, a hard cooked cheese. For that purpose, we analysed samples of cheese cooked at low (45°C), control (52°C) or high temperature (60°C) for residual rennet activity. We also studied proteolysis in cheese at the end of ripening by means of peptide mapping and electrophoresis. Rennet activity was inversely proportional to cooking temperature, although the activity was quantifiable even in cheeses cooked at high temperature, suggesting renaturation or incomplete denaturation of the enzyme. Indices of proteolysis, especially the levels of the peptide αs1-CN(f24-199), were consistent with residual rennet activity. Secondary proteolysis was also different for cheeses cooked at different temperatures.Fil: Hynes, Erica Rut. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; ArgentinaFil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; ArgentinaFil: Zalazar, Carlos Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; ArgentinaFil: McSweeney. P.L.H. No especifíca;Dairy Industry Assoc Australia2004-10info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/151266Hynes, Erica Rut; Candioti, Mario César; Zalazar, Carlos Antonio; McSweeney. P.L.H; Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese; Dairy Industry Assoc Australia; Australian Journal Of Dairy Technology; 59; 43; 10-2004; 209-2130004-9433CONICET DigitalCONICETenginfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T09:56:15Zoai:ri.conicet.gov.ar:11336/151266instacron:CONICETInstitucionalhttp://ri.conicet.gov.ar/Organismo científico-tecnológicoNo correspondehttp://ri.conicet.gov.ar/oai/requestdasensio@conicet.gov.ar; lcarlino@conicet.gov.arArgentinaNo correspondeNo correspondeNo correspondeopendoar:34982025-09-03 09:56:15.925CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
title |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
spellingShingle |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese Hynes, Erica Rut HARD CHEESES RENNETING CHEESEMAKING PROTEOLYSIS - CHEESE RIPENING |
title_short |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
title_full |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
title_fullStr |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
title_full_unstemmed |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
title_sort |
Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese |
dc.creator.none.fl_str_mv |
Hynes, Erica Rut Candioti, Mario César Zalazar, Carlos Antonio McSweeney. P.L.H |
author |
Hynes, Erica Rut |
author_facet |
Hynes, Erica Rut Candioti, Mario César Zalazar, Carlos Antonio McSweeney. P.L.H |
author_role |
author |
author2 |
Candioti, Mario César Zalazar, Carlos Antonio McSweeney. P.L.H |
author2_role |
author author author |
dc.subject.none.fl_str_mv |
HARD CHEESES RENNETING CHEESEMAKING PROTEOLYSIS - CHEESE RIPENING |
topic |
HARD CHEESES RENNETING CHEESEMAKING PROTEOLYSIS - CHEESE RIPENING |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
It is generally believed that enzymes in rennet are largely denatured by cooking during the manufacture of hard cheese. However, typical products of rennet action on αs1-casein have been detected in these varieties. The aim of the present work was to relate residual rennet activity with proteolysis in Reggianito Argentino, a hard cooked cheese. For that purpose, we analysed samples of cheese cooked at low (45°C), control (52°C) or high temperature (60°C) for residual rennet activity. We also studied proteolysis in cheese at the end of ripening by means of peptide mapping and electrophoresis. Rennet activity was inversely proportional to cooking temperature, although the activity was quantifiable even in cheeses cooked at high temperature, suggesting renaturation or incomplete denaturation of the enzyme. Indices of proteolysis, especially the levels of the peptide αs1-CN(f24-199), were consistent with residual rennet activity. Secondary proteolysis was also different for cheeses cooked at different temperatures. Fil: Hynes, Erica Rut. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina Fil: Candioti, Mario César. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina Fil: Zalazar, Carlos Antonio. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Santa Fe. Instituto de Lactología Industrial. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Instituto de Lactología Industrial; Argentina Fil: McSweeney. P.L.H. No especifíca; |
description |
It is generally believed that enzymes in rennet are largely denatured by cooking during the manufacture of hard cheese. However, typical products of rennet action on αs1-casein have been detected in these varieties. The aim of the present work was to relate residual rennet activity with proteolysis in Reggianito Argentino, a hard cooked cheese. For that purpose, we analysed samples of cheese cooked at low (45°C), control (52°C) or high temperature (60°C) for residual rennet activity. We also studied proteolysis in cheese at the end of ripening by means of peptide mapping and electrophoresis. Rennet activity was inversely proportional to cooking temperature, although the activity was quantifiable even in cheeses cooked at high temperature, suggesting renaturation or incomplete denaturation of the enzyme. Indices of proteolysis, especially the levels of the peptide αs1-CN(f24-199), were consistent with residual rennet activity. Secondary proteolysis was also different for cheeses cooked at different temperatures. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-10 |
dc.type.none.fl_str_mv |
info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion http://purl.org/coar/resource_type/c_6501 info:ar-repo/semantics/articulo |
format |
article |
status_str |
publishedVersion |
dc.identifier.none.fl_str_mv |
http://hdl.handle.net/11336/151266 Hynes, Erica Rut; Candioti, Mario César; Zalazar, Carlos Antonio; McSweeney. P.L.H; Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese; Dairy Industry Assoc Australia; Australian Journal Of Dairy Technology; 59; 43; 10-2004; 209-213 0004-9433 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/151266 |
identifier_str_mv |
Hynes, Erica Rut; Candioti, Mario César; Zalazar, Carlos Antonio; McSweeney. P.L.H; Rennet activity and proteolysis in Reggianito Argentino hard cooked cheese; Dairy Industry Assoc Australia; Australian Journal Of Dairy Technology; 59; 43; 10-2004; 209-213 0004-9433 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.rights.none.fl_str_mv |
info:eu-repo/semantics/openAccess https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
eu_rights_str_mv |
openAccess |
rights_invalid_str_mv |
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ |
dc.format.none.fl_str_mv |
application/pdf application/pdf application/pdf |
dc.publisher.none.fl_str_mv |
Dairy Industry Assoc Australia |
publisher.none.fl_str_mv |
Dairy Industry Assoc Australia |
dc.source.none.fl_str_mv |
reponame:CONICET Digital (CONICET) instname:Consejo Nacional de Investigaciones Científicas y Técnicas |
reponame_str |
CONICET Digital (CONICET) |
collection |
CONICET Digital (CONICET) |
instname_str |
Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.name.fl_str_mv |
CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicas |
repository.mail.fl_str_mv |
dasensio@conicet.gov.ar; lcarlino@conicet.gov.ar |
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1842269394352209920 |
score |
13.13397 |