Proteolysis, Texture and Microstructure of Goat Cheese

Autores
Burgos, Laura Silvina; Pece Azar, Nora Beatriz del Carmen; Maldonado, S.
Año de publicación
2016
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Changes in the structure of cheese are mostly due to changes in the protein matrix, mainly because of the degradation of α- and β- and k-casein. Therefore, the objective of this work was to study the effect of proteolysis on the microstructure and texture of goat cheese during ripening. The cheeses were made using Creole goat milk from the Quebrada de Humahuaca in Jujuy and ripened at 10 °C and 90% RH. Samples were taken after 5 hours of preparation and after 10, 20, 30, 40, 60 and 80 days of ripening. Proteolysis was studied by the evolution of the major fractions of casein (α, β and para-κ) determined by HPLC and soluble nitrogen, allowing the calculation of the rate of maturation. The texture profile was determined using a texture analyzer QTS 25. The changes in the protein matrix of the cheese were observed by scanning electron microscopy using a JEOL JSM-6480 LV. We found that the α-casein was hydrolyzed at a low speed at the beginning and until 30 days, between 30 and 40 days of ripening, α-casein was hydrolyzed faster. After this time, this fraction content became stable until the end of the ripening. The rate of hydrolysis of para-κ-casein increased starting from 30 days up to 60 days of ripening, when it became stable. It was observed that the initial matrix of cheese protein was formed by free large cavities with a heterogeneous dispersion of casein particles. During ripening, the size of the cavities decreased and the cheese protein matrix became more compact. The size of the holes was reduced and the globular characteristic of the micelles was lost after 40 days of maturation, coinciding with accentuated hydrolysis α-caseins. The soluble nitrogen at pH 4.6, increased significantly until 30 days. After that, it remained statistically unchanged for 80 days. The velocity of maturation determined as soluble nitrogen in TCA, rose steadily until 60 days of ripening. Hardness, gumminess, adhesiveness and chewiness increased sharply at 40 days of maturation. After this time, these parameters increased slowly until the end of the sampling period, when the changes in the microstructure of the cheeses revealed the highest compaction of the matrix. This may be related to the formation of soluble nitrogen and degradation of α-caseins during ripening
Fil: Burgos, Laura Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Jujuy. Facultad de Ingeniería. Centro de Investigación en Tecnología Alimentaria; Argentina
Fil: Pece Azar, Nora Beatriz del Carmen. No especifíca;
Fil: Maldonado, S.. No especifíca;
Materia
Proteolysis
Goat Cheese
Texture and Microstructure
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/105957

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oai_identifier_str oai:ri.conicet.gov.ar:11336/105957
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Proteolysis, Texture and Microstructure of Goat CheeseBurgos, Laura SilvinaPece Azar, Nora Beatriz del CarmenMaldonado, S.ProteolysisGoat CheeseTexture and Microstructurehttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Changes in the structure of cheese are mostly due to changes in the protein matrix, mainly because of the degradation of α- and β- and k-casein. Therefore, the objective of this work was to study the effect of proteolysis on the microstructure and texture of goat cheese during ripening. The cheeses were made using Creole goat milk from the Quebrada de Humahuaca in Jujuy and ripened at 10 °C and 90% RH. Samples were taken after 5 hours of preparation and after 10, 20, 30, 40, 60 and 80 days of ripening. Proteolysis was studied by the evolution of the major fractions of casein (α, β and para-κ) determined by HPLC and soluble nitrogen, allowing the calculation of the rate of maturation. The texture profile was determined using a texture analyzer QTS 25. The changes in the protein matrix of the cheese were observed by scanning electron microscopy using a JEOL JSM-6480 LV. We found that the α-casein was hydrolyzed at a low speed at the beginning and until 30 days, between 30 and 40 days of ripening, α-casein was hydrolyzed faster. After this time, this fraction content became stable until the end of the ripening. The rate of hydrolysis of para-κ-casein increased starting from 30 days up to 60 days of ripening, when it became stable. It was observed that the initial matrix of cheese protein was formed by free large cavities with a heterogeneous dispersion of casein particles. During ripening, the size of the cavities decreased and the cheese protein matrix became more compact. The size of the holes was reduced and the globular characteristic of the micelles was lost after 40 days of maturation, coinciding with accentuated hydrolysis α-caseins. The soluble nitrogen at pH 4.6, increased significantly until 30 days. After that, it remained statistically unchanged for 80 days. The velocity of maturation determined as soluble nitrogen in TCA, rose steadily until 60 days of ripening. Hardness, gumminess, adhesiveness and chewiness increased sharply at 40 days of maturation. After this time, these parameters increased slowly until the end of the sampling period, when the changes in the microstructure of the cheeses revealed the highest compaction of the matrix. This may be related to the formation of soluble nitrogen and degradation of α-caseins during ripeningFil: Burgos, Laura Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Jujuy. Facultad de Ingeniería. Centro de Investigación en Tecnología Alimentaria; ArgentinaFil: Pece Azar, Nora Beatriz del Carmen. No especifíca; Fil: Maldonado, S.. No especifíca; Jaipur: international Journal of Engineering and Applied Sciences2016-05info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/105957Burgos, Laura Silvina; Pece Azar, Nora Beatriz del Carmen; Maldonado, S.; Proteolysis, Texture and Microstructure of Goat Cheese; Jaipur: international Journal of Engineering and Applied Sciences; International Journal of Engineering and Applied Sciences; 3; 5; 5-2016; 14-192394-3661CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://www.ijeas.org/Volume-3-Issue-5info:eu-repo/semantics/altIdentifier/url/https://www.ijeas.org/proteolysis-texture-and-microstructure-of-goat-cheeseinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-03T10:09:40Zoai:ri.conicet.gov.ar:11336/105957instacron: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 10:09:41.013CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Proteolysis, Texture and Microstructure of Goat Cheese
title Proteolysis, Texture and Microstructure of Goat Cheese
spellingShingle Proteolysis, Texture and Microstructure of Goat Cheese
Burgos, Laura Silvina
Proteolysis
Goat Cheese
Texture and Microstructure
title_short Proteolysis, Texture and Microstructure of Goat Cheese
title_full Proteolysis, Texture and Microstructure of Goat Cheese
title_fullStr Proteolysis, Texture and Microstructure of Goat Cheese
title_full_unstemmed Proteolysis, Texture and Microstructure of Goat Cheese
title_sort Proteolysis, Texture and Microstructure of Goat Cheese
dc.creator.none.fl_str_mv Burgos, Laura Silvina
Pece Azar, Nora Beatriz del Carmen
Maldonado, S.
author Burgos, Laura Silvina
author_facet Burgos, Laura Silvina
Pece Azar, Nora Beatriz del Carmen
Maldonado, S.
author_role author
author2 Pece Azar, Nora Beatriz del Carmen
Maldonado, S.
author2_role author
author
dc.subject.none.fl_str_mv Proteolysis
Goat Cheese
Texture and Microstructure
topic Proteolysis
Goat Cheese
Texture and Microstructure
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Changes in the structure of cheese are mostly due to changes in the protein matrix, mainly because of the degradation of α- and β- and k-casein. Therefore, the objective of this work was to study the effect of proteolysis on the microstructure and texture of goat cheese during ripening. The cheeses were made using Creole goat milk from the Quebrada de Humahuaca in Jujuy and ripened at 10 °C and 90% RH. Samples were taken after 5 hours of preparation and after 10, 20, 30, 40, 60 and 80 days of ripening. Proteolysis was studied by the evolution of the major fractions of casein (α, β and para-κ) determined by HPLC and soluble nitrogen, allowing the calculation of the rate of maturation. The texture profile was determined using a texture analyzer QTS 25. The changes in the protein matrix of the cheese were observed by scanning electron microscopy using a JEOL JSM-6480 LV. We found that the α-casein was hydrolyzed at a low speed at the beginning and until 30 days, between 30 and 40 days of ripening, α-casein was hydrolyzed faster. After this time, this fraction content became stable until the end of the ripening. The rate of hydrolysis of para-κ-casein increased starting from 30 days up to 60 days of ripening, when it became stable. It was observed that the initial matrix of cheese protein was formed by free large cavities with a heterogeneous dispersion of casein particles. During ripening, the size of the cavities decreased and the cheese protein matrix became more compact. The size of the holes was reduced and the globular characteristic of the micelles was lost after 40 days of maturation, coinciding with accentuated hydrolysis α-caseins. The soluble nitrogen at pH 4.6, increased significantly until 30 days. After that, it remained statistically unchanged for 80 days. The velocity of maturation determined as soluble nitrogen in TCA, rose steadily until 60 days of ripening. Hardness, gumminess, adhesiveness and chewiness increased sharply at 40 days of maturation. After this time, these parameters increased slowly until the end of the sampling period, when the changes in the microstructure of the cheeses revealed the highest compaction of the matrix. This may be related to the formation of soluble nitrogen and degradation of α-caseins during ripening
Fil: Burgos, Laura Silvina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de Jujuy. Facultad de Ingeniería. Centro de Investigación en Tecnología Alimentaria; Argentina
Fil: Pece Azar, Nora Beatriz del Carmen. No especifíca;
Fil: Maldonado, S.. No especifíca;
description Changes in the structure of cheese are mostly due to changes in the protein matrix, mainly because of the degradation of α- and β- and k-casein. Therefore, the objective of this work was to study the effect of proteolysis on the microstructure and texture of goat cheese during ripening. The cheeses were made using Creole goat milk from the Quebrada de Humahuaca in Jujuy and ripened at 10 °C and 90% RH. Samples were taken after 5 hours of preparation and after 10, 20, 30, 40, 60 and 80 days of ripening. Proteolysis was studied by the evolution of the major fractions of casein (α, β and para-κ) determined by HPLC and soluble nitrogen, allowing the calculation of the rate of maturation. The texture profile was determined using a texture analyzer QTS 25. The changes in the protein matrix of the cheese were observed by scanning electron microscopy using a JEOL JSM-6480 LV. We found that the α-casein was hydrolyzed at a low speed at the beginning and until 30 days, between 30 and 40 days of ripening, α-casein was hydrolyzed faster. After this time, this fraction content became stable until the end of the ripening. The rate of hydrolysis of para-κ-casein increased starting from 30 days up to 60 days of ripening, when it became stable. It was observed that the initial matrix of cheese protein was formed by free large cavities with a heterogeneous dispersion of casein particles. During ripening, the size of the cavities decreased and the cheese protein matrix became more compact. The size of the holes was reduced and the globular characteristic of the micelles was lost after 40 days of maturation, coinciding with accentuated hydrolysis α-caseins. The soluble nitrogen at pH 4.6, increased significantly until 30 days. After that, it remained statistically unchanged for 80 days. The velocity of maturation determined as soluble nitrogen in TCA, rose steadily until 60 days of ripening. Hardness, gumminess, adhesiveness and chewiness increased sharply at 40 days of maturation. After this time, these parameters increased slowly until the end of the sampling period, when the changes in the microstructure of the cheeses revealed the highest compaction of the matrix. This may be related to the formation of soluble nitrogen and degradation of α-caseins during ripening
publishDate 2016
dc.date.none.fl_str_mv 2016-05
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/11336/105957
Burgos, Laura Silvina; Pece Azar, Nora Beatriz del Carmen; Maldonado, S.; Proteolysis, Texture and Microstructure of Goat Cheese; Jaipur: international Journal of Engineering and Applied Sciences; International Journal of Engineering and Applied Sciences; 3; 5; 5-2016; 14-19
2394-3661
CONICET Digital
CONICET
url http://hdl.handle.net/11336/105957
identifier_str_mv Burgos, Laura Silvina; Pece Azar, Nora Beatriz del Carmen; Maldonado, S.; Proteolysis, Texture and Microstructure of Goat Cheese; Jaipur: international Journal of Engineering and Applied Sciences; International Journal of Engineering and Applied Sciences; 3; 5; 5-2016; 14-19
2394-3661
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/url/https://www.ijeas.org/Volume-3-Issue-5
info:eu-repo/semantics/altIdentifier/url/https://www.ijeas.org/proteolysis-texture-and-microstructure-of-goat-cheese
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
dc.publisher.none.fl_str_mv Jaipur: international Journal of Engineering and Applied Sciences
publisher.none.fl_str_mv Jaipur: international Journal of Engineering and Applied Sciences
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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