Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)

Autores
Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos
Año de publicación
2003
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Muscles and different proteins obtained from scallops (Chlamys tehuelchus and Zygochlamys patagonica) were analyzed. In both species of scallop, the thermograms of striated and smooth muscles showed two endothermic transitions. The Tmax values corresponding to striated and smooth muscles from C. tehuelchus were 53.2, 79.0°C and 52.7, 78.0°C, respectively. The Tmax corresponding to striated and smooth muscles of Z. patagonica were 55.0, 79.2°C and 54.7, 78.7°C, respectively. No significant differences were observed between the thermal transitions of myofibrils and actomyosin of both types of muscles from both species of scallop. Irrespective of the species, the thermal stability decreased when the pH of the muscles was increased. The increase in ionic strength greatly affected Tmax, the ΔH total and the ΔH of the first transition. A significant decrease in ΔH total and ΔH corresponding to both transitions was observed, particularly in the striated muscles of Zygochlamys patagonica. These results indicate a major sensitivity of the adductor muscles of Zygochlamys to changes in the chemical environment.
Fil: Paredi, María Elida. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); Argentina
Fil: Tomás, Mabel Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Crupkin, Marcos. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); Argentina
Materia
CHEMICAL ENVIRONMENT
SCALLOP
THERMAL STABILITY
Nivel de accesibilidad
acceso abierto
Condiciones de uso
https://creativecommons.org/licenses/by/2.5/ar/
Repositorio
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/129532
Acceder
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network_name_str CONICET Digital (CONICET)
spelling Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)Paredi, María ElidaTomás, Mabel CristinaCrupkin, MarcosCHEMICAL ENVIRONMENTSCALLOPTHERMAL STABILITYhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Muscles and different proteins obtained from scallops (Chlamys tehuelchus and Zygochlamys patagonica) were analyzed. In both species of scallop, the thermograms of striated and smooth muscles showed two endothermic transitions. The Tmax values corresponding to striated and smooth muscles from C. tehuelchus were 53.2, 79.0°C and 52.7, 78.0°C, respectively. The Tmax corresponding to striated and smooth muscles of Z. patagonica were 55.0, 79.2°C and 54.7, 78.7°C, respectively. No significant differences were observed between the thermal transitions of myofibrils and actomyosin of both types of muscles from both species of scallop. Irrespective of the species, the thermal stability decreased when the pH of the muscles was increased. The increase in ionic strength greatly affected Tmax, the ΔH total and the ΔH of the first transition. A significant decrease in ΔH total and ΔH corresponding to both transitions was observed, particularly in the striated muscles of Zygochlamys patagonica. These results indicate a major sensitivity of the adductor muscles of Zygochlamys to changes in the chemical environment.Fil: Paredi, María Elida. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); ArgentinaFil: Tomás, Mabel Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; ArgentinaFil: Crupkin, Marcos. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); ArgentinaBrazilian Society of Chemical Engineering2003-06info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/vnd.openxmlformats-officedocument.wordprocessingml.documentapplication/pdfhttp://hdl.handle.net/11336/129532Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC); Brazilian Society of Chemical Engineering; Brazilian Journal of Chemical Engineering; 20; 2; 6-2003; 153-1590104-66321678-4383CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/doi/10.1590/S0104-66322003000200009info:eu-repo/semantics/altIdentifier/url/https://tinyurl.com/yb7xjvksinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:06:26Zoai:ri.conicet.gov.ar:11336/129532instacron: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:34982025-09-29 10:06:26.878CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
title Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
spellingShingle Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
Paredi, María Elida
CHEMICAL ENVIRONMENT
SCALLOP
THERMAL STABILITY
title_short Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
title_full Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
title_fullStr Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
title_full_unstemmed Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
title_sort Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC)
dc.creator.none.fl_str_mv Paredi, María Elida
Tomás, Mabel Cristina
Crupkin, Marcos
author Paredi, María Elida
author_facet Paredi, María Elida
Tomás, Mabel Cristina
Crupkin, Marcos
author_role author
author2 Tomás, Mabel Cristina
Crupkin, Marcos
author2_role author
author
dc.subject.none.fl_str_mv CHEMICAL ENVIRONMENT
SCALLOP
THERMAL STABILITY
topic CHEMICAL ENVIRONMENT
SCALLOP
THERMAL STABILITY
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Muscles and different proteins obtained from scallops (Chlamys tehuelchus and Zygochlamys patagonica) were analyzed. In both species of scallop, the thermograms of striated and smooth muscles showed two endothermic transitions. The Tmax values corresponding to striated and smooth muscles from C. tehuelchus were 53.2, 79.0°C and 52.7, 78.0°C, respectively. The Tmax corresponding to striated and smooth muscles of Z. patagonica were 55.0, 79.2°C and 54.7, 78.7°C, respectively. No significant differences were observed between the thermal transitions of myofibrils and actomyosin of both types of muscles from both species of scallop. Irrespective of the species, the thermal stability decreased when the pH of the muscles was increased. The increase in ionic strength greatly affected Tmax, the ΔH total and the ΔH of the first transition. A significant decrease in ΔH total and ΔH corresponding to both transitions was observed, particularly in the striated muscles of Zygochlamys patagonica. These results indicate a major sensitivity of the adductor muscles of Zygochlamys to changes in the chemical environment.
Fil: Paredi, María Elida. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas; Argentina. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); Argentina
Fil: Tomás, Mabel Cristina. Provincia de Buenos Aires. Gobernación. Comisión de Investigaciones Científicas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata. Centro de Investigación y Desarrollo en Criotecnología de Alimentos. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Centro de Investigación y Desarrollo en Criotecnología de Alimentos; Argentina
Fil: Crupkin, Marcos. Universidad Nacional de Mar del Plata. Facultad de Ciencias Agrarias; Argentina. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (Pesca y Agroindustria); Argentina
description Muscles and different proteins obtained from scallops (Chlamys tehuelchus and Zygochlamys patagonica) were analyzed. In both species of scallop, the thermograms of striated and smooth muscles showed two endothermic transitions. The Tmax values corresponding to striated and smooth muscles from C. tehuelchus were 53.2, 79.0°C and 52.7, 78.0°C, respectively. The Tmax corresponding to striated and smooth muscles of Z. patagonica were 55.0, 79.2°C and 54.7, 78.7°C, respectively. No significant differences were observed between the thermal transitions of myofibrils and actomyosin of both types of muscles from both species of scallop. Irrespective of the species, the thermal stability decreased when the pH of the muscles was increased. The increase in ionic strength greatly affected Tmax, the ΔH total and the ΔH of the first transition. A significant decrease in ΔH total and ΔH corresponding to both transitions was observed, particularly in the striated muscles of Zygochlamys patagonica. These results indicate a major sensitivity of the adductor muscles of Zygochlamys to changes in the chemical environment.
publishDate 2003
dc.date.none.fl_str_mv 2003-06
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/11336/129532
Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC); Brazilian Society of Chemical Engineering; Brazilian Journal of Chemical Engineering; 20; 2; 6-2003; 153-159
0104-6632
1678-4383
CONICET Digital
CONICET
url http://hdl.handle.net/11336/129532
identifier_str_mv Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal behavior of myofibrillar proteins from the adductor muscles of scallops. A differential scanning calorimetric study (DSC); Brazilian Society of Chemical Engineering; Brazilian Journal of Chemical Engineering; 20; 2; 6-2003; 153-159
0104-6632
1678-4383
CONICET Digital
CONICET
dc.language.none.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv info:eu-repo/semantics/altIdentifier/doi/10.1590/S0104-66322003000200009
info:eu-repo/semantics/altIdentifier/url/https://tinyurl.com/yb7xjvks
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
https://creativecommons.org/licenses/by/2.5/ar/
eu_rights_str_mv openAccess
rights_invalid_str_mv https://creativecommons.org/licenses/by/2.5/ar/
dc.format.none.fl_str_mv application/pdf
application/vnd.openxmlformats-officedocument.wordprocessingml.document
application/pdf
dc.publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
publisher.none.fl_str_mv Brazilian Society of Chemical Engineering
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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score 13.070432

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