Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese
- Autores
- Hynes, Erica Rut; Aparo, Luciana; Candioti, Mario César
- Año de publicación
- 2004
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on αs1-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on αs1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and αs1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of αs1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of αs1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide αs1-I was not detected in 60°C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from αs1-casein in hard cheeses may be at least, partially due to this proteolytic agent.
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: Aparo, Luciana. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Programa 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 - Materia
-
HARD COOKED CHEESE
MILK-CLOTTING ENZYME
PROTEOLYSIS
ΑS1- CASEIN - 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:11336/117718
Ver los metadatos del registro completo
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CONICET Digital (CONICET) |
spelling |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheeseHynes, Erica RutAparo, LucianaCandioti, Mario CésarHARD COOKED CHEESEMILK-CLOTTING ENZYMEPROTEOLYSISΑS1- CASEINhttps://purl.org/becyt/ford/1.6https://purl.org/becyt/ford/1Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on αs1-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on αs1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and αs1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of αs1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of αs1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide αs1-I was not detected in 60°C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from αs1-casein in hard cheeses may be at least, partially due to this proteolytic agent.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: Aparo, Luciana. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Programa 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; ArgentinaAmerican Dairy Science Association2004-04info: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/11336/117718Hynes, Erica Rut; Aparo, Luciana; Candioti, Mario César; Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese; American Dairy Science Association; Journal of Dairy Science; 87; 3; 4-2004; 565-5730022-0302CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.3168/jds.S0022-0302(04)73198-7info:eu-repo/semantics/altIdentifier/url/https://www.journalofdairyscience.org/article/S0022-0302(04)73198-7/fulltextinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:05:28Zoai:ri.conicet.gov.ar:11336/117718instacron: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 10:05:28.715CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
title |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
spellingShingle |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese Hynes, Erica Rut HARD COOKED CHEESE MILK-CLOTTING ENZYME PROTEOLYSIS ΑS1- CASEIN |
title_short |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
title_full |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
title_fullStr |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
title_full_unstemmed |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
title_sort |
Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese |
dc.creator.none.fl_str_mv |
Hynes, Erica Rut Aparo, Luciana Candioti, Mario César |
author |
Hynes, Erica Rut |
author_facet |
Hynes, Erica Rut Aparo, Luciana Candioti, Mario César |
author_role |
author |
author2 |
Aparo, Luciana Candioti, Mario César |
author2_role |
author author |
dc.subject.none.fl_str_mv |
HARD COOKED CHEESE MILK-CLOTTING ENZYME PROTEOLYSIS ΑS1- CASEIN |
topic |
HARD COOKED CHEESE MILK-CLOTTING ENZYME PROTEOLYSIS ΑS1- CASEIN |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/1.6 https://purl.org/becyt/ford/1 |
dc.description.none.fl_txt_mv |
Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on αs1-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on αs1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and αs1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of αs1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of αs1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide αs1-I was not detected in 60°C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from αs1-casein in hard cheeses may be at least, partially due to this proteolytic agent. 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: Aparo, Luciana. Universidad Nacional del Litoral. Facultad de Ingeniería Química. Programa 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 |
description |
Milk-clotting enzyme is considered largely denatured after the cooking step in hard cheeses. Nevertheless, typical hydrolysis products derived from rennet action on αs1-casein have been detected during the ripening of hard cheeses. The aim of the present work was to investigate the influence of residual milk-clotting enzyme on αs1-casein hydrolysis in Reggianito cheeses. For that purpose, we studied the influence of cooking temperature (45, 52, and 60°C) on milk-clotting enzyme residual activity and αs1-casein hydrolysis during ripening. Milk-clotting enzyme residual activity in cheeses was assessed using a chromatographic method, and the hydrolysis of αs1-casein was determined by electrophoresis and high performance liquid chromatography. Milk-clotting enzyme activity was very low or undetectable in 60°C- and 52°C-cooked cheeses at the beginning of the ripening, but it increased afterwards, particularly in 52°C-cooked cheeses. Cheese curds that were cooked at 45°C had higher initial milk clotting activity, but also in this case, there was a later increase. Hydrolysis of αs1-casein was detected early in cheeses made at 45°C, and later in those made at higher temperatures. The peptide αs1-I was not detected in 60°C-cooked cheeses. The results suggest that residual milk-clotting enzyme can contribute to proteolysis during ripening of hard cheeses, because it probably renatures partially after the cooking step. Consequently, the production of peptides derived from αs1-casein in hard cheeses may be at least, partially due to this proteolytic agent. |
publishDate |
2004 |
dc.date.none.fl_str_mv |
2004-04 |
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/11336/117718 Hynes, Erica Rut; Aparo, Luciana; Candioti, Mario César; Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese; American Dairy Science Association; Journal of Dairy Science; 87; 3; 4-2004; 565-573 0022-0302 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/117718 |
identifier_str_mv |
Hynes, Erica Rut; Aparo, Luciana; Candioti, Mario César; Influence of residual milk-clotting enzyme on αs1 casein hydrolysis during ripening of Reggianito Argentino cheese; American Dairy Science Association; Journal of Dairy Science; 87; 3; 4-2004; 565-573 0022-0302 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/doi/10.3168/jds.S0022-0302(04)73198-7 info:eu-repo/semantics/altIdentifier/url/https://www.journalofdairyscience.org/article/S0022-0302(04)73198-7/fulltext |
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 |
American Dairy Science Association |
publisher.none.fl_str_mv |
American Dairy Science Association |
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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1842269911939809280 |
score |
13.13397 |