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
CONICET Digital (CONICET)
Institución
Consejo Nacional de Investigaciones Científicas y Técnicas
OAI Identificador
oai:ri.conicet.gov.ar:11336/33307
Acceder
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oai_identifier_str oai:ri.conicet.gov.ar:11336/33307
network_acronym_str CONICETDig
repository_id_str 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 Técnicas2025-10-15T15:11:17Zoai: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:34982025-10-15 15:11:18.271CONICET 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
_version_ 1846083261098360832
score 13.22299

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