High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties...
- Autores
- Speroni Aguirre, Francisco José; Szerman, Natalia; Vaudagna, Sergio Ramon
- Año de publicación
- 2014
- Idioma
- inglés
- Tipo de recurso
- artículo
- Estado
- versión publicada
- Descripción
- Beef patties added with sodium tripolyphosphate (STPP; 0, 0.25 or 0.5%) and/or NaCl (0, 1 or 2%) were treated at 200 or 300 MPa (5 min, 5 °C) or kept refrigerated (non-pressurized). In non-pressurized patties, NaCl solubilized proteins which resulted denatured, whereas STPP solubilized proteins which remained in a native state. At 200 MPa, myosin head was more sensitive to high hydrostatic pressure (HHP) than actin. 1% NaCl favored HHP-induced denaturation of myosin head and actin, whereas 0.25% STPP protected against that effect. At 300 MPa, STPP favored HHP-induced denaturation of myosin head, actin and other proteins. The effect of STPP at 200 MPa may depend on the presence of specific binding sites for STPP anion. These sites would be destroyed due to unfolding at 300 MPa, because of the higher pressure level. No formation of insoluble aggregates occurred at 200 MPa, whereas insoluble aggregates were formed at 300 MPa in samples without salts. Salts minimized protein aggregation observed at 300 MPa. Noticeable differences in thermal and aggregative behavior occurred whether HHP level was 200 or 300 MPa.
Fil: Speroni Aguirre, Francisco José. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina
Fil: Szerman, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina
Fil: Vaudagna, Sergio Ramon. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina - Materia
-
High Hydrostatic Pressure
Beef
Thermal Behavior
Low Sodium Content
Sodium Tripolyphosphate - 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:11336/33307
Ver los metadatos del registro completo
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3498 |
network_name_str |
CONICET Digital (CONICET) |
spelling |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteinsSperoni Aguirre, Francisco JoséSzerman, NataliaVaudagna, Sergio RamonHigh Hydrostatic PressureBeefThermal BehaviorLow Sodium ContentSodium Tripolyphosphatehttps://purl.org/becyt/ford/2.11https://purl.org/becyt/ford/2Beef patties added with sodium tripolyphosphate (STPP; 0, 0.25 or 0.5%) and/or NaCl (0, 1 or 2%) were treated at 200 or 300 MPa (5 min, 5 °C) or kept refrigerated (non-pressurized). In non-pressurized patties, NaCl solubilized proteins which resulted denatured, whereas STPP solubilized proteins which remained in a native state. At 200 MPa, myosin head was more sensitive to high hydrostatic pressure (HHP) than actin. 1% NaCl favored HHP-induced denaturation of myosin head and actin, whereas 0.25% STPP protected against that effect. At 300 MPa, STPP favored HHP-induced denaturation of myosin head, actin and other proteins. The effect of STPP at 200 MPa may depend on the presence of specific binding sites for STPP anion. These sites would be destroyed due to unfolding at 300 MPa, because of the higher pressure level. No formation of insoluble aggregates occurred at 200 MPa, whereas insoluble aggregates were formed at 300 MPa in samples without salts. Salts minimized protein aggregation observed at 300 MPa. Noticeable differences in thermal and aggregative behavior occurred whether HHP level was 200 or 300 MPa.Fil: Speroni Aguirre, Francisco José. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; ArgentinaFil: Szerman, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; ArgentinaFil: Vaudagna, Sergio Ramon. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; ArgentinaElsevier2014-06info: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/11336/33307Speroni Aguirre, Francisco José; Vaudagna, Sergio Ramon; Szerman, Natalia; High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins; Elsevier; Innovative Food Science & Emerging Technologies; 23; 6-2014; 10-171466-8564CONICET DigitalCONICETenginfo:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1466856414000678info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ifset.2014.03.011info:eu-repo/semantics/openAccesshttps://creativecommons.org/licenses/by-nc-sa/2.5/ar/reponame:CONICET Digital (CONICET)instname:Consejo Nacional de Investigaciones Científicas y Técnicas2025-09-29T10:14:08Zoai:ri.conicet.gov.ar:11336/33307instacron: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 10:14:08.319CONICET Digital (CONICET) - Consejo Nacional de Investigaciones Científicas y Técnicasfalse |
dc.title.none.fl_str_mv |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
title |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
spellingShingle |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins Speroni Aguirre, Francisco José High Hydrostatic Pressure Beef Thermal Behavior Low Sodium Content Sodium Tripolyphosphate |
title_short |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
title_full |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
title_fullStr |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
title_full_unstemmed |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
title_sort |
High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins |
dc.creator.none.fl_str_mv |
Speroni Aguirre, Francisco José Szerman, Natalia Vaudagna, Sergio Ramon |
author |
Speroni Aguirre, Francisco José |
author_facet |
Speroni Aguirre, Francisco José Szerman, Natalia Vaudagna, Sergio Ramon |
author_role |
author |
author2 |
Szerman, Natalia Vaudagna, Sergio Ramon |
author2_role |
author author |
dc.subject.none.fl_str_mv |
High Hydrostatic Pressure Beef Thermal Behavior Low Sodium Content Sodium Tripolyphosphate |
topic |
High Hydrostatic Pressure Beef Thermal Behavior Low Sodium Content Sodium Tripolyphosphate |
purl_subject.fl_str_mv |
https://purl.org/becyt/ford/2.11 https://purl.org/becyt/ford/2 |
dc.description.none.fl_txt_mv |
Beef patties added with sodium tripolyphosphate (STPP; 0, 0.25 or 0.5%) and/or NaCl (0, 1 or 2%) were treated at 200 or 300 MPa (5 min, 5 °C) or kept refrigerated (non-pressurized). In non-pressurized patties, NaCl solubilized proteins which resulted denatured, whereas STPP solubilized proteins which remained in a native state. At 200 MPa, myosin head was more sensitive to high hydrostatic pressure (HHP) than actin. 1% NaCl favored HHP-induced denaturation of myosin head and actin, whereas 0.25% STPP protected against that effect. At 300 MPa, STPP favored HHP-induced denaturation of myosin head, actin and other proteins. The effect of STPP at 200 MPa may depend on the presence of specific binding sites for STPP anion. These sites would be destroyed due to unfolding at 300 MPa, because of the higher pressure level. No formation of insoluble aggregates occurred at 200 MPa, whereas insoluble aggregates were formed at 300 MPa in samples without salts. Salts minimized protein aggregation observed at 300 MPa. Noticeable differences in thermal and aggregative behavior occurred whether HHP level was 200 or 300 MPa. Fil: Speroni Aguirre, Francisco José. 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. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina Fil: Szerman, Natalia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina Fil: Vaudagna, Sergio Ramon. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - La Plata; Argentina. Instituto Nacional de Tecnología Agropecuaria. Centro de Investigación de Agroindustria. Instituto de Tecnología de Alimentos; Argentina |
description |
Beef patties added with sodium tripolyphosphate (STPP; 0, 0.25 or 0.5%) and/or NaCl (0, 1 or 2%) were treated at 200 or 300 MPa (5 min, 5 °C) or kept refrigerated (non-pressurized). In non-pressurized patties, NaCl solubilized proteins which resulted denatured, whereas STPP solubilized proteins which remained in a native state. At 200 MPa, myosin head was more sensitive to high hydrostatic pressure (HHP) than actin. 1% NaCl favored HHP-induced denaturation of myosin head and actin, whereas 0.25% STPP protected against that effect. At 300 MPa, STPP favored HHP-induced denaturation of myosin head, actin and other proteins. The effect of STPP at 200 MPa may depend on the presence of specific binding sites for STPP anion. These sites would be destroyed due to unfolding at 300 MPa, because of the higher pressure level. No formation of insoluble aggregates occurred at 200 MPa, whereas insoluble aggregates were formed at 300 MPa in samples without salts. Salts minimized protein aggregation observed at 300 MPa. Noticeable differences in thermal and aggregative behavior occurred whether HHP level was 200 or 300 MPa. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014-06 |
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/11336/33307 Speroni Aguirre, Francisco José; Vaudagna, Sergio Ramon; Szerman, Natalia; High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins; Elsevier; Innovative Food Science & Emerging Technologies; 23; 6-2014; 10-17 1466-8564 CONICET Digital CONICET |
url |
http://hdl.handle.net/11336/33307 |
identifier_str_mv |
Speroni Aguirre, Francisco José; Vaudagna, Sergio Ramon; Szerman, Natalia; High hydrostatic pressure processing of beef patties: Effects of pressure level and sodium tripolyphosphate and sodium chloride concentrations on thermal and aggregative properties of proteins; Elsevier; Innovative Food Science & Emerging Technologies; 23; 6-2014; 10-17 1466-8564 CONICET Digital CONICET |
dc.language.none.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
info:eu-repo/semantics/altIdentifier/url/http://www.sciencedirect.com/science/article/pii/S1466856414000678 info:eu-repo/semantics/altIdentifier/doi/10.1016/j.ifset.2014.03.011 |
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 |
Elsevier |
publisher.none.fl_str_mv |
Elsevier |
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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1844614065408704512 |
score |
13.070432 |