dc.creator | Estévez, Natalia | |
dc.creator | Fuciños, Pablo | |
dc.creator | Bargiela, Verónica | |
dc.creator | Picó, Guillermo Alfredo | |
dc.creator | Woitovich Valetti, Nadia | |
dc.creator | Tovar, Clara Asunción | |
dc.creator | Rúa, M. Luisa | |
dc.date.accessioned | 2018-07-26T18:34:19Z | |
dc.date.accessioned | 2018-11-06T14:46:26Z | |
dc.date.available | 2018-07-26T18:34:19Z | |
dc.date.available | 2018-11-06T14:46:26Z | |
dc.date.created | 2018-07-26T18:34:19Z | |
dc.date.issued | 2017-03 | |
dc.identifier | 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 | 0308-8146 | |
dc.identifier | http://hdl.handle.net/11336/53182 | |
dc.identifier | CONICET Digital | |
dc.identifier | CONICET | |
dc.identifier.uri | http://repositorioslatinoamericanos.uchile.cl/handle/2250/1890105 | |
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.language | eng | |
dc.publisher | Elsevier | |
dc.relation | info:eu-repo/semantics/altIdentifier/doi/https://dx.doi.org/10.1016/j.foodchem.2016.09.137 | |
dc.relation | info:eu-repo/semantics/altIdentifier/url/https://www.sciencedirect.com/science/article/pii/S0308814616315333 | |
dc.rights | https://creativecommons.org/licenses/by-nc-sa/2.5/ar/ | |
dc.rights | info:eu-repo/semantics/restrictedAccess | |
dc.subject | CONFORMATIONAL CHANGES | |
dc.subject | ENZYMATIC HYDROLYSIS | |
dc.subject | GELATION | |
dc.subject | RHEOLOGICAL PROPERTIES | |
dc.subject | WHEY PROTEIN | |
dc.subject | Β-LACTOGLOBULIN | |
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 | Artículos de revistas | |
dc.type | Artículos de revistas | |
dc.type | Artículos de revistas | |