Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study

Autores
Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos
Año de publicación
2002
Idioma
inglés
Tipo de recurso
artículo
Estado
versión publicada
Descripción
Denaturation of proteins from striated and smooth muscles of scallop (Zygochlamys patagonica) was studied with differential scanning calorimetry (DSC) by monitoring maximum temperatures of transition and denaturation enthalpies. DSC thermograms of both striated and smooth whole muscles showed two transitions: Tmax 55.0, 79.2°C; and Tmax 54.7, 78.7°C, respectively. The DSC thermograms of myofibrils and actomyosin were similar to those corresponding to their respective whole muscles. As pH and ionic strength increased, the thermal stability of whole muscles decreased. The pH increase (5.0-8.0) significantly (p < 0.01) decreased the denaturation enthalpies (ΔH total, ΔH peakl, and ΔH peakll) of whole striated muscles. A significant decrease (p < 0.05) in the ΔH total and the ΔH peakl was also observed in DSC thermograms of smooth muscles at pH 8.0. Denaturation enthalpies (ΔH total and ΔH peakl) significantly decreased (p < 0.01) when the ionic strength increased from 0.05 to 0.5 in both types of muscles. Striated muscles were more affected than smooth muscles by changes in the chemical environment.
Fil: Paredi, María Elida. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); 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. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); Argentina
Materia
MYOFIBRILLAR PROTEINS
PATAGONIAN SCALLOP
THERMAL DENATURATION
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:11336/120149
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/120149
network_acronym_str CONICETDig
repository_id_str 3498
network_name_str CONICET Digital (CONICET)
spelling Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric StudyParedi, María ElidaTomás, Mabel CristinaCrupkin, MarcosMYOFIBRILLAR PROTEINSPATAGONIAN SCALLOPTHERMAL DENATURATIONhttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Denaturation of proteins from striated and smooth muscles of scallop (Zygochlamys patagonica) was studied with differential scanning calorimetry (DSC) by monitoring maximum temperatures of transition and denaturation enthalpies. DSC thermograms of both striated and smooth whole muscles showed two transitions: Tmax 55.0, 79.2°C; and Tmax 54.7, 78.7°C, respectively. The DSC thermograms of myofibrils and actomyosin were similar to those corresponding to their respective whole muscles. As pH and ionic strength increased, the thermal stability of whole muscles decreased. The pH increase (5.0-8.0) significantly (p < 0.01) decreased the denaturation enthalpies (ΔH total, ΔH peakl, and ΔH peakll) of whole striated muscles. A significant decrease (p < 0.05) in the ΔH total and the ΔH peakl was also observed in DSC thermograms of smooth muscles at pH 8.0. Denaturation enthalpies (ΔH total and ΔH peakl) significantly decreased (p < 0.01) when the ionic strength increased from 0.05 to 0.5 in both types of muscles. Striated muscles were more affected than smooth muscles by changes in the chemical environment.Fil: Paredi, María Elida. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); 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. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); ArgentinaAmerican Chemical Society2002-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersionhttp://purl.org/coar/resource_type/c_6501info:ar-repo/semantics/articuloapplication/pdfapplication/pdfhttp://hdl.handle.net/11336/120149Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study; American Chemical Society; Journal of Agricultural and Food Chemistry; 50; 4; 1-2002; 830-8340021-8561CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/https://tinyurl.com/y543899zinfo:eu-repo/semantics/altIdentifier/doi/10.1021/jf010767qinfo:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T09:34:33Zoai:ri.conicet.gov.ar:11336/120149instacron: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 09:34:34.264CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse
dc.title.none.fl_str_mv Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
title Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
spellingShingle Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
Paredi, María Elida
MYOFIBRILLAR PROTEINS
PATAGONIAN SCALLOP
THERMAL DENATURATION
title_short Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
title_full Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
title_fullStr Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
title_full_unstemmed Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
title_sort Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study
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 MYOFIBRILLAR PROTEINS
PATAGONIAN SCALLOP
THERMAL DENATURATION
topic MYOFIBRILLAR PROTEINS
PATAGONIAN SCALLOP
THERMAL DENATURATION
purl_subject.fl_str_mv https://purl.org/becyt/ford/2.11
https://purl.org/becyt/ford/2
dc.description.none.fl_txt_mv Denaturation of proteins from striated and smooth muscles of scallop (Zygochlamys patagonica) was studied with differential scanning calorimetry (DSC) by monitoring maximum temperatures of transition and denaturation enthalpies. DSC thermograms of both striated and smooth whole muscles showed two transitions: Tmax 55.0, 79.2°C; and Tmax 54.7, 78.7°C, respectively. The DSC thermograms of myofibrils and actomyosin were similar to those corresponding to their respective whole muscles. As pH and ionic strength increased, the thermal stability of whole muscles decreased. The pH increase (5.0-8.0) significantly (p < 0.01) decreased the denaturation enthalpies (ΔH total, ΔH peakl, and ΔH peakll) of whole striated muscles. A significant decrease (p < 0.05) in the ΔH total and the ΔH peakl was also observed in DSC thermograms of smooth muscles at pH 8.0. Denaturation enthalpies (ΔH total and ΔH peakl) significantly decreased (p < 0.01) when the ionic strength increased from 0.05 to 0.5 in both types of muscles. Striated muscles were more affected than smooth muscles by changes in the chemical environment.
Fil: Paredi, María Elida. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); 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. Instituto Nacional de Tecnología Industrial. Centro Regional Sur (pesca y Agroind); Argentina
description Denaturation of proteins from striated and smooth muscles of scallop (Zygochlamys patagonica) was studied with differential scanning calorimetry (DSC) by monitoring maximum temperatures of transition and denaturation enthalpies. DSC thermograms of both striated and smooth whole muscles showed two transitions: Tmax 55.0, 79.2°C; and Tmax 54.7, 78.7°C, respectively. The DSC thermograms of myofibrils and actomyosin were similar to those corresponding to their respective whole muscles. As pH and ionic strength increased, the thermal stability of whole muscles decreased. The pH increase (5.0-8.0) significantly (p < 0.01) decreased the denaturation enthalpies (ΔH total, ΔH peakl, and ΔH peakll) of whole striated muscles. A significant decrease (p < 0.05) in the ΔH total and the ΔH peakl was also observed in DSC thermograms of smooth muscles at pH 8.0. Denaturation enthalpies (ΔH total and ΔH peakl) significantly decreased (p < 0.01) when the ionic strength increased from 0.05 to 0.5 in both types of muscles. Striated muscles were more affected than smooth muscles by changes in the chemical environment.
publishDate 2002
dc.date.none.fl_str_mv 2002-01
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/11336/120149
Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study; American Chemical Society; Journal of Agricultural and Food Chemistry; 50; 4; 1-2002; 830-834
0021-8561
CONICET Digital
CONICET
url http://hdl.handle.net/11336/120149
identifier_str_mv Paredi, María Elida; Tomás, Mabel Cristina; Crupkin, Marcos; Thermal Denaturation of Myofibrillar Proteins of Striated and Smooth Adductor Muscles of Scallop (Zygochlamys patagonica). A Differential Scanning Calorimetric Study; American Chemical Society; Journal of Agricultural and Food Chemistry; 50; 4; 1-2002; 830-834
0021-8561
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://tinyurl.com/y543899z
info:eu-repo/semantics/altIdentifier/doi/10.1021/jf010767q
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 American Chemical Society
publisher.none.fl_str_mv American Chemical Society
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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