Showing posts with label Conformational changes. Show all posts
Showing posts with label Conformational changes. Show all posts

Monday, 2 May 2016

Structural and thermo-rheological analysis of solutions and gels of a β-lactoglobulin fraction isolated from bovine whey

Food Chemistry, 198 (2016) 45–53
http://dx.doi.org/10.1016/j.foodchem.2015.11.090


A β-Lactoglobulin fraction (r-βLg) was isolated from milk whey hydrolysates produced with cardosins from Cynara cardunculus. The impact of the technological process on the r-βLg structure and how in turn this determined its heat-induced gelation was investigated. Results were analysed taking pure β-Lg (p-βLg) as control sample. The process induced changes in the r-βLg native conformation causing exposure of hydrophobic groups, lower thermal stability and also, shorter thermal treatments needed to give rise to non-native and aggregated species.

At pH 3.2, r-βLg and p-βLg solutions exhibited two gelation steps, with the advantage that r-βLg protein may form stable gels at lower temperature than p-βLg. At pH 7.2, a specific thermo-viscoelastic stability to 73 °C was found, which corresponded to the gel point in both protein solutions. The difference was that while for p-βLg solution in sol state δ < 45° (solid-like), however for r-βLg solution δ > 45° (fluid-like).

Tuesday, 15 March 2016

Influence of pH on viscoelastic properties of heat-induced gels obtained with a β-Lactoglobulin fraction isolated from bovine milk whey hydrolysates

Food Chemistry, 219, 2017, 169–178


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.