High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate
The influence of ion type, ion concentration and pH on the effect of high hydrostatic pressure (HHP) on solubility and dispersion stability of soybean protein isolate (SPI) was analyzed. Solubilizing effect of HHP was detected for calcium-, magnesium- and iron- added SPI, the magnitude of this effec...
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| Format: | info:ar-repo/semantics/artículo |
| Language: | Inglés |
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2018
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| Online Access: | https://www.sciencedirect.com/science/article/pii/S0268005X1400263X http://hdl.handle.net/20.500.12123/2379 https://doi.org/10.1016/j.foodhyd.2014.07.020 |
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| author | Manassero, Carlos Alberto Vaudagna, Sergio Ramon Añón, María Cristina Speroni, Francisco |
| author_browse | Añón, María Cristina Manassero, Carlos Alberto Speroni, Francisco Vaudagna, Sergio Ramon |
| author_facet | Manassero, Carlos Alberto Vaudagna, Sergio Ramon Añón, María Cristina Speroni, Francisco |
| author_sort | Manassero, Carlos Alberto |
| collection | INTA Digital |
| description | The influence of ion type, ion concentration and pH on the effect of high hydrostatic pressure (HHP) on solubility and dispersion stability of soybean protein isolate (SPI) was analyzed. Solubilizing effect of HHP was detected for calcium-, magnesium- and iron- added SPI, the magnitude of this effect was dependent on ion type, ion concentration and pH. The solubilizing effect was highest for calcium, followed by magnesium and iron at pH 7.0. The pH value affected the levels of solubility and the range of calcium concentration where solubility was increased. HHP-denatured soybean proteins may coexist with different minerals and at different pHs in the form of soluble species. For a given calcium concentration, pH may affect the structure of HHP-induced aggregates, leading to different solubilities and dispersion stabilities. HHP improved the stability of insoluble proteins in calcium-added SPI dispersions, avoiding their settling. Our results confirm that thermal treatment and HHP differentially affect protein–protein interactions. A transient dissociation of calcium from proteins during HHP is postulated. This dissociation would play a role in the structure of aggregates. When calcium is present during denaturation, different aggregates may be formed if calcium is bound to (thermal treatment) or transiently dissociated from (HHP) SPI proteins |
| format | info:ar-repo/semantics/artículo |
| id | INTA2379 |
| institution | Instituto Nacional de Tecnología Agropecuaria (INTA -Argentina) |
| language | Inglés |
| publishDate | 2018 |
| publishDateRange | 2018 |
| publishDateSort | 2018 |
| record_format | dspace |
| spelling | INTA23792018-07-04T12:28:15Z High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate Manassero, Carlos Alberto Vaudagna, Sergio Ramon Añón, María Cristina Speroni, Francisco Soja Tecnología Alta Presión Aislado de Proteínas Solubilidad Soybeans High Pressure Technology Protein Isolates Solubility The influence of ion type, ion concentration and pH on the effect of high hydrostatic pressure (HHP) on solubility and dispersion stability of soybean protein isolate (SPI) was analyzed. Solubilizing effect of HHP was detected for calcium-, magnesium- and iron- added SPI, the magnitude of this effect was dependent on ion type, ion concentration and pH. The solubilizing effect was highest for calcium, followed by magnesium and iron at pH 7.0. The pH value affected the levels of solubility and the range of calcium concentration where solubility was increased. HHP-denatured soybean proteins may coexist with different minerals and at different pHs in the form of soluble species. For a given calcium concentration, pH may affect the structure of HHP-induced aggregates, leading to different solubilities and dispersion stabilities. HHP improved the stability of insoluble proteins in calcium-added SPI dispersions, avoiding their settling. Our results confirm that thermal treatment and HHP differentially affect protein–protein interactions. A transient dissociation of calcium from proteins during HHP is postulated. This dissociation would play a role in the structure of aggregates. When calcium is present during denaturation, different aggregates may be formed if calcium is bound to (thermal treatment) or transiently dissociated from (HHP) SPI proteins Instituto de Tecnología de Alimentos Fil: Manassero, Carlos Alberto. Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Tecnología de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Área Bioquímica y Control de Alimentos; Argentina Fil: Vaudagna, Sergio Ramon . Instituto Nacional de Tecnología Agropecuaria (INTA). Instituto de Tecnología de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnica; Argentina Fil: Añón, María Cristina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina. Universidad Nacional de La Plata. Facultad de Ciencias Exactas. Departamento de Ciencias Biológicas. Área Bioquímica y Control de Alimentos; Argentina. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.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: Speroni, Francisco. Consejo Nacional de Investigaciones Científicas y Técnicas; Argentina.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 2018-05-14T11:45:58Z 2018-05-14T11:45:58Z 2015-01 info:ar-repo/semantics/artículo info:eu-repo/semantics/article info:eu-repo/semantics/publishedVersion https://www.sciencedirect.com/science/article/pii/S0268005X1400263X http://hdl.handle.net/20.500.12123/2379 0268-005X https://doi.org/10.1016/j.foodhyd.2014.07.020 eng info:eu-repo/semantics/restrictedAccess application/pdf Food hydrocolloids 43 : 629-635. (January 2015) |
| spellingShingle | Soja Tecnología Alta Presión Aislado de Proteínas Solubilidad Soybeans High Pressure Technology Protein Isolates Solubility Manassero, Carlos Alberto Vaudagna, Sergio Ramon Añón, María Cristina Speroni, Francisco High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title | High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title_full | High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title_fullStr | High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title_full_unstemmed | High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title_short | High hydrostatic pressure improves protein solubility and dispersion stability of mineral-added soybean protein isolate |
| title_sort | high hydrostatic pressure improves protein solubility and dispersion stability of mineral added soybean protein isolate |
| topic | Soja Tecnología Alta Presión Aislado de Proteínas Solubilidad Soybeans High Pressure Technology Protein Isolates Solubility |
| url | https://www.sciencedirect.com/science/article/pii/S0268005X1400263X http://hdl.handle.net/20.500.12123/2379 https://doi.org/10.1016/j.foodhyd.2014.07.020 |
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