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Cold-Set Whey Protein Gels with Addition of Polysaccharides

Author:
Cavallieri, Ângelo Luiz Fazani, Cunha, Rosiane Lopes
Source:
Food biophysics 2009 v.4 no.2 pp. 94-105
ISSN:
1557-1858
Subject:
acidification, electrostatic interactions, fractal dimensions, gelation, gels, gluconolactone, mechanical properties, pH, protein-protein interactions, scanning electron microscopy, separation, whey protein, xanthan gum
Abstract:
Cold-set whey protein (WP) gels with addition of xanthan or guar were evaluated by mechanical properties and scanning electron microscopy. Gels were formed after the addition of different amounts of glucono-δ-lactone to thermally denatured WP solutions, leading to different acidification rates and final pH values. At lower acidification rates and higher final pH, gels showed more discontinuous structure and weaker and less elastic network, which was attributed to a predominance of phase separation during gel formation due to slower gelation kinetics. In contrast, at higher acidification rates and lower final pHs, gelation prevailed over phase separation, favoring the formation of less porous structures, resulting in stronger and more elastic gels. The gels' fractal dimension (D f; structure complexity) and lacunarity were also influenced by the simultaneous effects of gelation and phase separation. For systems where phase separation was the prevailing mechanism, greater lacunarity parameters were usually observed, describing the heterogeneity of pore distribution, while the opposite occurred at prevailing gelation conditions. Increase in guar concentration or lower final pH of xanthan gels entailed in D f reduction, while the increase in xanthan concentration resulted in higher D f. Such a result suggests that the network contour length was rugged, but this pattern was reduced by the increase of electrostatic interactions among WP and xanthan. Guar addition caused the formation of gel network with smoother surfaces, which could be attributed to the guar-protein excluded volume effects leading to an increase in protein-protein interactions.
Agid:
2178730