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dc.contributor.author
Estévez, Natalia  
dc.contributor.author
Fuciños, Pablo  
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Bargiela, Verónica  
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Picó, Guillermo Alfredo  
dc.contributor.author
Woitovich Valetti, Nadia  
dc.contributor.author
Tovar, Clara Asunción  
dc.contributor.author
Rúa, M. Luisa  
dc.date.available
2018-07-26T18:34:19Z  
dc.date.issued
2017-03  
dc.identifier.citation
Estévez, Natalia; Fuciños, Pablo; Bargiela, Verónica; Picó, Guillermo Alfredo; Woitovich Valetti, Nadia; et al.; Influence of pH on viscoelastic properties of heat-induced gels obtained with a β-Lactoglobulin fraction isolated from bovine milk whey hydrolysates; Elsevier; Food Chemistry; 219; 3-2017; 169-178  
dc.identifier.issn
0308-8146  
dc.identifier.uri
http://hdl.handle.net/11336/53182  
dc.description.abstract
A β-Lactoglobulin fraction (r-βLg) was isolated from whey hydrolysates produced with cardosins from Cynara cardunculus. The impact of the hydrolysis process on the r-βLg structure and the rheological properties of heat-induced gels obtained thereafter were studied at different pH values. Differences were observed between r-βLg and commercial β-Lg used as control. Higher values for the fluorescence emission intensity and red shifts of the emission wavelength of r-βLg suggested changes in its tertiary structure and more solvent-exposed tryptophan residues. Circular dichroism spectra also supported these evidences indicating that hydrolysis yielded an intermediate (non-native) β-Lg state. The thermal history of r-βLg through the new adopted conformation improved the microstructure of the gels at acidic pH. So, a new microstructure with better rheological characteristics (higher conformational flexibility and lower rigidity) and greater water holding ability was founded for r-βLg gel. These results were reflected in the microstructural analysis by scanning electron microscopy.  
dc.format
application/pdf  
dc.language.iso
eng  
dc.publisher
Elsevier  
dc.rights
info:eu-repo/semantics/openAccess  
dc.rights.uri
https://creativecommons.org/licenses/by-nc-sa/2.5/ar/  
dc.subject
Conformational Changes  
dc.subject
Enzymatic Hydrolysis  
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Gelation  
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Rheological Properties  
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Whey Protein  
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Β-Lactoglobulin  
dc.subject.classification
Bioquímica y Biología Molecular  
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Ciencias Biológicas  
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CIENCIAS NATURALES Y EXACTAS  
dc.title
Influence of pH on viscoelastic properties of heat-induced gels obtained with a β-Lactoglobulin fraction isolated from bovine milk whey hydrolysates  
dc.type
info:eu-repo/semantics/article  
dc.type
info:ar-repo/semantics/artículo  
dc.type
info:eu-repo/semantics/publishedVersion  
dc.date.updated
2018-07-26T13:59:01Z  
dc.journal.volume
219  
dc.journal.pagination
169-178  
dc.journal.pais
Países Bajos  
dc.journal.ciudad
Amsterdam  
dc.description.fil
Fil: Estévez, Natalia. Universidad de Vigo; España  
dc.description.fil
Fil: Fuciños, Pablo. International Iberian Nanotechnology Laboratory; Portugal  
dc.description.fil
Fil: Bargiela, Verónica. Universidad de Vigo; España  
dc.description.fil
Fil: Picó, Guillermo Alfredo. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina  
dc.description.fil
Fil: Woitovich Valetti, Nadia. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Rosario. Instituto de Procesos Biotecnológicos y Químicos Rosario. Universidad Nacional de Rosario. Facultad de Ciencias Bioquímicas y Farmacéuticas. Instituto de Procesos Biotecnológicos y Químicos Rosario; Argentina  
dc.description.fil
Fil: Tovar, Clara Asunción. Universidad de Vigo; España  
dc.description.fil
Fil: Rúa, M. Luisa. Universidad de Vigo; España  
dc.journal.title
Food Chemistry  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.foodchem.2016.09.137  
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0308814616315333