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

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 T max values corresponding to striated and smooth muscles from C. te...

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Autores principales: Paredi, M.E., Tomás, Mabel Cristina, Crupkin, M.
Formato: Articulo
Lenguaje:Español
Publicado: 2003
Materias:
Química
chemical environment
scallop
thermal stability
Biología Marina
proteina
Acceso en línea:http://sedici.unlp.edu.ar/handle/10915/62097
http://ref.scielo.org/wx3dqp
Aporte de:
SEDICI (UNLP) de Universidad Nacional de La Plata
id I19-R120-10915-62097
record_format dspace
institution Universidad Nacional de La Plata
institution_str I-19
repository_str R-120
collection SEDICI (UNLP)
language Español
topic Química
chemical environment
scallop
thermal stability
Biología Marina
proteina
spellingShingle Química
chemical environment
scallop
thermal stability
Biología Marina
proteina
Paredi, M.E.
Tomás, Mabel Cristina
Crupkin, M.
Thermal behavior of myofibrillar proteins from the adductor muscles of scallops : A differential scanning calorimetric study (DSC)
topic_facet Química
chemical environment
scallop
thermal stability
Biología Marina
proteina
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 T max values corresponding to striated and smooth muscles from C. tehuelchus were 53.2, 79.0°C and 52.7, 78.0°C, respectively. The T max 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 T max, 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.
format Articulo
Articulo
author Paredi, M.E.
Tomás, Mabel Cristina
Crupkin, M.
author_facet Paredi, M.E.
Tomás, Mabel Cristina
Crupkin, M.
author_sort Paredi, M.E.
title Thermal behavior of myofibrillar proteins from the adductor muscles of scallops : A differential scanning calorimetric study (DSC)
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)
publishDate 2003
url http://sedici.unlp.edu.ar/handle/10915/62097
http://ref.scielo.org/wx3dqp
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AT tomasmabelcristina thermalbehaviorofmyofibrillarproteinsfromtheadductormusclesofscallopsadifferentialscanningcalorimetricstudydsc
AT crupkinm thermalbehaviorofmyofibrillarproteinsfromtheadductormusclesofscallopsadifferentialscanningcalorimetricstudydsc
bdutipo_str Repositorios
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